Q9Y520 · PRC2C_HUMAN
- ProteinProtein PRRC2C
- GenePRRC2C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2896 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for efficient formation of stress granules.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic stress granule | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Molecular Function | RNA binding | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | stress granule assembly |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein PRRC2C
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y520
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046290 | 235 | in dbSNP:rs10913157 | |||
Sequence: A → T | ||||||
Natural variant | VAR_046291 | 343 | in dbSNP:rs36013361 | |||
Sequence: N → K | ||||||
Natural variant | VAR_046292 | 468 | in dbSNP:rs704839 | |||
Sequence: E → G | ||||||
Natural variant | VAR_046293 | 906 | in dbSNP:rs760644 | |||
Sequence: A → T | ||||||
Natural variant | VAR_046294 | 959 | in dbSNP:rs34269512 | |||
Sequence: P → S | ||||||
Natural variant | VAR_046295 | 1624 | in dbSNP:rs235468 | |||
Sequence: S → C | ||||||
Natural variant | VAR_046296 | 1771 | in dbSNP:rs1687056 | |||
Sequence: P → S | ||||||
Natural variant | VAR_046297 | 1868 | in dbSNP:rs3820169 | |||
Sequence: L → R | ||||||
Natural variant | VAR_046298 | 1885 | in dbSNP:rs12025905 | |||
Sequence: A → T | ||||||
Natural variant | VAR_046299 | 1924 | in dbSNP:rs183523 | |||
Sequence: P → R | ||||||
Natural variant | VAR_059584 | 2717 | in dbSNP:rs2421847 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000349239 | 1-2896 | UniProt | Protein PRRC2C | |||
Sequence: MSEKSGQSTKAKDGKKYATLSLFNTYKGKSLETQKTTARHGLQSLGKVGISRRMPPPANLPSLKAENKGNDPNVNIVPKDGTGWASKQEQHEEEKTPEVPPAQPKPGVAAPPEVAPAPKSWASNKQGGQGDGIQVNSQFQQEFPSLQAAGDQEKKEKETNDDNYGPGPSLRPPNVACWRDGGKAAGSPSSSDQDEKLPGQDESTAGTSEQNDILKVVEKRIACGPPQAKLNGQQAALASQYRAMMPPYMFQQYPRMTYPPLHGPMRFPPSLSETNKGLRGRGPPPSWASEPERPSILSASELKELDKFDNLDAEADEGWAGAQMEVDYTEQLNFSDDDEQGSNSPKENNSEDQGSKASENNENKKETDEVSNTKSSSQIPAQPSVAKVPYGKGPSFNQERGTSSHLPPPPKLLAQQHPPPDRQAVPGRPGPFPSKQQVADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVHETEPESGSQPRPAVLSGYFKQFQKSLPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQPSSSTVPPPPHRPLYQPMQPHPQHLASMGFDPRWLMMQSYMDPRMMSGRPAMDIPPIHPGMIPPKPLMRRDQMEGSPNSSESFEHIARSARDHAISLSEPRMLWGSDPYPHAEPQQATTPKATEEPEDVRSEAALDQEQITAAYSVEHNQLEAHPKADFIRESSEAQVQKFLSRSVEDVRPHHTDANNQSACFEAPDQKTLSAPQEERISAVESQPSRKRSVSHGSNHTQKPDEQRSEPSAGIPKVTSRCIDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDLPPPPPPPQPPAPIQPQSVPPPIQPEAEKFPSTETATLAQKPSQDTEKPLEPVSTVQVEPAVKTVNQQTMAAPVVKEEKQPEKVISKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYSRGRSYRGSYGGRGRGGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPGGRPSRPSTLRRPAYRDNQWNPRQSEVPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASKSNEVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETASESSDFNERRERDEKKNADLNAQTVVKVGENVLPPKREIAKRSFSSQRPVDRQNRRGNNGPPKSGRNFSGPRNERRSGPPSKSGKRGPFDDQPAGTTGVDLINGSSAHHQEGVPNGTGQKNSKDSTGKKREDPKPGPKKPKEKVDALSQFDLNNYASVVIIDDHPEVTVIEDPQSNLNDDGFTEVVSKKQQKRLQDEERRKKEEQVIQVWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPPLASAPLPPSTSASVPASTSAPLPATLTPVPASTSAPVPASTLAPVLASTSAPVPASPLAPVSASASVSASVPASTSAAAITSSSAPASAPAPTPILASVSTPASVTILASASIPILASALASTSAPTPAPAASSPAAPVITAPTIPASAPTASVPLAPASASAPAPAPTPVSAPNPAPPAPAQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTAELWDNKVAPPAVLNDISKKLGPISPPQPPSVSAWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVVPVLSEKSADKIPEPKEQRQKQPRAGPIKAQKLPDLSPVENKEHKPGPIGKERSLKNRKVKDAQQVEPEGQEKPSPATVRSTDPVTTKETKAVSEMSTEIGTMISVSSAEYGTNAKESVTDYTTPSSSLPNTVATNNTKMEDTLVNNVPLPNTLPLPKRETIQQSSSLTSVPPTTFSLTFKMESARKAWENSPNVREKGSPVTSTAPPIATGVSSSASGPSTANYNSFSSASMPQIPVASVTPTASLSGAGTYTTSSLSTKSTTTSDPPNICKVKPQQLQTSSLPSASHFSQLSCMPSLIAQQQQNPQVYVSQSAAAQIPAFYMDTSHLFNTQHARLAPPSLAQQQGFQPGLSQPTSVQQIPIPIYAPLQGQHQAQLSLGAGPAVSQAQELFSSSLQPYRSQPAFMQSSLSQPSVVLSGTAIHNFPTVQHQELAKAQSGLAFQQTSNTQPIPILYEHQLGQASGLGGSQLIDTHLLQARANLTQASNLYSGQVQQPGQTNFYNTAQSPSALQQVTVPLPASQLSLPNFGSTGQPLIALPQTLQPPLQHTTPQAQAQSLSRPAQVSQPFRGLIPAGTQHSMIATTGKMSEMELKAFGSGIDIKPGTPPIAGRSTTPTSSPFRATSTSPNSQSSKMNSIVYQKQFQSAPATVRMTQPFPTQFAPQILSQPNLVPPLVRAPHTNTFPAPVQRPPMALASQMPPPLTTGLMSHARLPHVARGPCGSLSGVRGNQAQAALKAEQDMKAKQRAEVLQSTQRFFSEQQQSKQIGGGKAQKVDSDSSKPPETLTDPPGVCQEKVEEKPPPAPSIATKPVRTGPIKPQAIKTEETKS | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 27 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 187 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 191 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 242 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 255 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 266 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 279 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 281 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 335 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 392 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 395 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 500 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 633 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 636 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 779 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 779 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 785 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 799 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 801 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 801 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 812 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 821 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 822 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 847 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 867 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 876 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 878 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 878 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 917 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 920 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 920 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 924 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 926 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 929 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1133 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1218 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1242 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1244 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1246 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1246 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1248 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1249 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1249 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1263 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1265 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1265 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1267 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1267 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1480 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1498 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1544 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1545 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1965 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1965 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1971 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1980 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1983 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2013 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2029 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2032 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2035 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2036 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2143 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2143 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2190 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 2192 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2260 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2260 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2665 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2673 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2673 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2682 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2682 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2684 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2685 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2686 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2686 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2692 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2694 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2694 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2707 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 2814 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 2823 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 2823 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Overexpressed in bladder cancer.
Gene expression databases
Organism-specific databases
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-212 | Disordered | ||||
Sequence: GKSLETQKTTARHGLQSLGKVGISRRMPPPANLPSLKAENKGNDPNVNIVPKDGTGWASKQEQHEEEKTPEVPPAQPKPGVAAPPEVAPAPKSWASNKQGGQGDGIQVNSQFQQEFPSLQAAGDQEKKEKETNDDNYGPGPSLRPPNVACWRDGGKAAGSPSSSDQDEKLPGQDESTAGTSEQND | ||||||
Compositional bias | 85-99 | Basic and acidic residues | ||||
Sequence: ASKQEQHEEEKTPEV | ||||||
Compositional bias | 122-147 | Polar residues | ||||
Sequence: ASNKQGGQGDGIQVNSQFQQEFPSLQ | ||||||
Compositional bias | 186-211 | Polar residues | ||||
Sequence: GSPSSSDQDEKLPGQDESTAGTSEQN | ||||||
Region | 264-729 | Disordered | ||||
Sequence: PMRFPPSLSETNKGLRGRGPPPSWASEPERPSILSASELKELDKFDNLDAEADEGWAGAQMEVDYTEQLNFSDDDEQGSNSPKENNSEDQGSKASENNENKKETDEVSNTKSSSQIPAQPSVAKVPYGKGPSFNQERGTSSHLPPPPKLLAQQHPPPDRQAVPGRPGPFPSKQQVADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVHETEPESGSQPRPAVLSGYFKQFQKSLPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQPSSSTVPPPPHRPLYQPMQPHPQHLA | ||||||
Compositional bias | 297-314 | Basic and acidic residues | ||||
Sequence: LSASELKELDKFDNLDAE | ||||||
Compositional bias | 357-371 | Basic and acidic residues | ||||
Sequence: ASENNENKKETDEVS | ||||||
Compositional bias | 411-427 | Pro residues | ||||
Sequence: KLLAQQHPPPDRQAVPG | ||||||
Compositional bias | 439-645 | Basic and acidic residues | ||||
Sequence: ADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVH | ||||||
Compositional bias | 671-703 | Polar residues | ||||
Sequence: LPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQ | ||||||
Compositional bias | 704-720 | Pro residues | ||||
Sequence: PSSSTVPPPPHRPLYQP | ||||||
Region | 750-788 | Disordered | ||||
Sequence: SGRPAMDIPPIHPGMIPPKPLMRRDQMEGSPNSSESFEH | ||||||
Region | 804-1118 | Disordered | ||||
Sequence: RMLWGSDPYPHAEPQQATTPKATEEPEDVRSEAALDQEQITAAYSVEHNQLEAHPKADFIRESSEAQVQKFLSRSVEDVRPHHTDANNQSACFEAPDQKTLSAPQEERISAVESQPSRKRSVSHGSNHTQKPDEQRSEPSAGIPKVTSRCIDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDLPPPPPPPQPPAPIQPQSVPPPIQPEAEKFPSTETATLAQKPSQDTEKPLEPVSTVQVEPA | ||||||
Compositional bias | 906-926 | Polar residues | ||||
Sequence: APQEERISAVESQPSRKRSVS | ||||||
Compositional bias | 954-1058 | Basic and acidic residues | ||||
Sequence: IDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDL | ||||||
Coiled coil | 1020-1046 | |||||
Sequence: VLRDMKEEREQRKEKEGEKAEKVTEKV | ||||||
Compositional bias | 1059-1084 | Pro residues | ||||
Sequence: PPPPPPPQPPAPIQPQSVPPPIQPEA | ||||||
Compositional bias | 1087-1108 | Polar residues | ||||
Sequence: FPSTETATLAQKPSQDTEKPLE | ||||||
Compositional bias | 1143-1195 | Basic and acidic residues | ||||
Sequence: SKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYS | ||||||
Region | 1143-1647 | Disordered | ||||
Sequence: SKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYSRGRSYRGSYGGRGRGGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPGGRPSRPSTLRRPAYRDNQWNPRQSEVPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASKSNEVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETASESSDFNERRERDEKKNADLNAQTVVKVGENVLPPKREIAKRSFSSQRPVDRQNRRGNNGPPKSGRNFSGPRNERRSGPPSKSGKRGPFDDQPAGTTGVDLINGSSAHHQEGVPNGTGQKNSKDSTGKKREDPKPGPKKPKEKVDALS | ||||||
Compositional bias | 1210-1356 | Basic and acidic residues | ||||
Sequence: GGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPG | ||||||
Compositional bias | 1382-1448 | Basic and acidic residues | ||||
Sequence: VPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASK | ||||||
Compositional bias | 1451-1499 | Polar residues | ||||
Sequence: EVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETA | ||||||
Compositional bias | 1501-1519 | Basic and acidic residues | ||||
Sequence: ESSDFNERRERDEKKNADL | ||||||
Compositional bias | 1533-1548 | Basic and acidic residues | ||||
Sequence: PPKREIAKRSFSSQRP | ||||||
Compositional bias | 1549-1565 | Polar residues | ||||
Sequence: VDRQNRRGNNGPPKSGR | ||||||
Compositional bias | 1597-1621 | Polar residues | ||||
Sequence: GVDLINGSSAHHQEGVPNGTGQKNS | ||||||
Compositional bias | 1622-1645 | Basic and acidic residues | ||||
Sequence: KDSTGKKREDPKPGPKKPKEKVDA | ||||||
Region | 1670-1785 | Disordered | ||||
Sequence: EDPQSNLNDDGFTEVVSKKQQKRLQDEERRKKEEQVIQVWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPPLASAPLPPSTSASVPASTSAPLPATLTPVPASTSAPV | ||||||
Coiled coil | 1682-1717 | |||||
Sequence: TEVVSKKQQKRLQDEERRKKEEQVIQVWNKKNANEK | ||||||
Compositional bias | 1684-1707 | Basic and acidic residues | ||||
Sequence: VVSKKQQKRLQDEERRKKEEQVIQ | ||||||
Compositional bias | 1708-1748 | Polar residues | ||||
Sequence: VWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPP | ||||||
Compositional bias | 1755-1785 | Polar residues | ||||
Sequence: PPSTSASVPASTSAPLPATLTPVPASTSAPV | ||||||
Region | 1905-1991 | Disordered | ||||
Sequence: APASASAPAPAPTPVSAPNPAPPAPAQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTAEL | ||||||
Compositional bias | 1909-1929 | Pro residues | ||||
Sequence: ASAPAPAPTPVSAPNPAPPAP | ||||||
Compositional bias | 1930-1989 | Polar residues | ||||
Sequence: AQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTA | ||||||
Region | 2005-2164 | Disordered | ||||
Sequence: ISKKLGPISPPQPPSVSAWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVVPVLSEKSADKIPEPKEQRQKQPRAGPIKAQKLPDLSPVENKEHKPGPIGKERSLKNRKVKDAQQVEPEGQEKPSPATVRSTDPVTTKETKAVSEM | ||||||
Compositional bias | 2022-2069 | Polar residues | ||||
Sequence: AWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVV | ||||||
Compositional bias | 2077-2091 | Basic and acidic residues | ||||
Sequence: ADKIPEPKEQRQKQP | ||||||
Compositional bias | 2104-2136 | Basic and acidic residues | ||||
Sequence: LSPVENKEHKPGPIGKERSLKNRKVKDAQQVEP | ||||||
Compositional bias | 2143-2164 | Polar residues | ||||
Sequence: SPATVRSTDPVTTKETKAVSEM | ||||||
Region | 2218-2238 | Disordered | ||||
Sequence: LPNTLPLPKRETIQQSSSLTS | ||||||
Region | 2257-2290 | Disordered | ||||
Sequence: WENSPNVREKGSPVTSTAPPIATGVSSSASGPST | ||||||
Compositional bias | 2264-2290 | Polar residues | ||||
Sequence: REKGSPVTSTAPPIATGVSSSASGPST | ||||||
Region | 2317-2341 | Disordered | ||||
Sequence: GAGTYTTSSLSTKSTTTSDPPNICK | ||||||
Region | 2668-2701 | Disordered | ||||
Sequence: DIKPGTPPIAGRSTTPTSSPFRATSTSPNSQSSK | ||||||
Compositional bias | 2677-2701 | Polar residues | ||||
Sequence: AGRSTTPTSSPFRATSTSPNSQSSK | ||||||
Region | 2824-2896 | Disordered | ||||
Sequence: FFSEQQQSKQIGGGKAQKVDSDSSKPPETLTDPPGVCQEKVEEKPPPAPSIATKPVRTGPIKPQAIKTEETKS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q9Y520-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,896
- Mass (Da)316,911
- Last updated2011-07-27 v4
- ChecksumF0E037C36F04CDF9
Q9Y520-2
- Name2
- Differences from canonical
- 1-243: Missing
Q9Y520-3
- Name3
- Differences from canonical
- 2687-2700: PFRATSTSPNSQSS → SGLLLQVRTASPAK
- 2701-2896: Missing
Q9Y520-4
- Name4
- Differences from canonical
- 2732-2810: Missing
Q9Y520-5
- Name5
- Differences from canonical
- 1759-1805: Missing
Q9Y520-6
- Name6
- Differences from canonical
- 2185-2249: Missing
- 2732-2810: Missing
Q9Y520-7
- Name7
- Differences from canonical
- 37-37: T → TVA
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y7F4 | A0A2R8Y7F4_HUMAN | PRRC2C | 910 | ||
A0A2R8Y424 | A0A2R8Y424_HUMAN | PRRC2C | 159 | ||
E7EPN9 | E7EPN9_HUMAN | PRRC2C | 2819 | ||
A0A2R8YET2 | A0A2R8YET2_HUMAN | PRRC2C | 1090 | ||
H7C5N8 | H7C5N8_HUMAN | PRRC2C | 1300 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035244 | 1-243 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035250 | 37 | in isoform 7 | |||
Sequence: T → TVA | ||||||
Compositional bias | 85-99 | Basic and acidic residues | ||||
Sequence: ASKQEQHEEEKTPEV | ||||||
Compositional bias | 122-147 | Polar residues | ||||
Sequence: ASNKQGGQGDGIQVNSQFQQEFPSLQ | ||||||
Compositional bias | 186-211 | Polar residues | ||||
Sequence: GSPSSSDQDEKLPGQDESTAGTSEQN | ||||||
Compositional bias | 297-314 | Basic and acidic residues | ||||
Sequence: LSASELKELDKFDNLDAE | ||||||
Compositional bias | 357-371 | Basic and acidic residues | ||||
Sequence: ASENNENKKETDEVS | ||||||
Compositional bias | 411-427 | Pro residues | ||||
Sequence: KLLAQQHPPPDRQAVPG | ||||||
Compositional bias | 439-645 | Basic and acidic residues | ||||
Sequence: ADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVH | ||||||
Sequence conflict | 454-456 | in Ref. 5; AAH45713 | ||||
Sequence: EIS → GIY | ||||||
Sequence conflict | 561 | in Ref. 5; AAH45713 | ||||
Sequence: Q → P | ||||||
Compositional bias | 671-703 | Polar residues | ||||
Sequence: LPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQ | ||||||
Compositional bias | 704-720 | Pro residues | ||||
Sequence: PSSSTVPPPPHRPLYQP | ||||||
Compositional bias | 906-926 | Polar residues | ||||
Sequence: APQEERISAVESQPSRKRSVS | ||||||
Compositional bias | 954-1058 | Basic and acidic residues | ||||
Sequence: IDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDL | ||||||
Compositional bias | 1059-1084 | Pro residues | ||||
Sequence: PPPPPPPQPPAPIQPQSVPPPIQPEA | ||||||
Compositional bias | 1087-1108 | Polar residues | ||||
Sequence: FPSTETATLAQKPSQDTEKPLE | ||||||
Compositional bias | 1143-1195 | Basic and acidic residues | ||||
Sequence: SKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYS | ||||||
Compositional bias | 1210-1356 | Basic and acidic residues | ||||
Sequence: GGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPG | ||||||
Compositional bias | 1382-1448 | Basic and acidic residues | ||||
Sequence: VPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASK | ||||||
Compositional bias | 1451-1499 | Polar residues | ||||
Sequence: EVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETA | ||||||
Compositional bias | 1501-1519 | Basic and acidic residues | ||||
Sequence: ESSDFNERRERDEKKNADL | ||||||
Compositional bias | 1533-1548 | Basic and acidic residues | ||||
Sequence: PPKREIAKRSFSSQRP | ||||||
Compositional bias | 1549-1565 | Polar residues | ||||
Sequence: VDRQNRRGNNGPPKSGR | ||||||
Compositional bias | 1597-1621 | Polar residues | ||||
Sequence: GVDLINGSSAHHQEGVPNGTGQKNS | ||||||
Compositional bias | 1622-1645 | Basic and acidic residues | ||||
Sequence: KDSTGKKREDPKPGPKKPKEKVDA | ||||||
Compositional bias | 1684-1707 | Basic and acidic residues | ||||
Sequence: VVSKKQQKRLQDEERRKKEEQVIQ | ||||||
Compositional bias | 1708-1748 | Polar residues | ||||
Sequence: VWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPP | ||||||
Compositional bias | 1755-1785 | Polar residues | ||||
Sequence: PPSTSASVPASTSAPLPATLTPVPASTSAPV | ||||||
Alternative sequence | VSP_035245 | 1759-1805 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1909-1929 | Pro residues | ||||
Sequence: ASAPAPAPTPVSAPNPAPPAP | ||||||
Compositional bias | 1930-1989 | Polar residues | ||||
Sequence: AQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTA | ||||||
Sequence conflict | 1940 | in Ref. 9; CAB82345 | ||||
Sequence: V → A | ||||||
Compositional bias | 2022-2069 | Polar residues | ||||
Sequence: AWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVV | ||||||
Compositional bias | 2077-2091 | Basic and acidic residues | ||||
Sequence: ADKIPEPKEQRQKQP | ||||||
Compositional bias | 2104-2136 | Basic and acidic residues | ||||
Sequence: LSPVENKEHKPGPIGKERSLKNRKVKDAQQVEP | ||||||
Compositional bias | 2143-2164 | Polar residues | ||||
Sequence: SPATVRSTDPVTTKETKAVSEM | ||||||
Alternative sequence | VSP_035246 | 2185-2249 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 2264-2290 | Polar residues | ||||
Sequence: REKGSPVTSTAPPIATGVSSSASGPST | ||||||
Sequence conflict | 2443 | in Ref. 10; BAB14056 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2539 | in Ref. 10; BAA90997 | ||||
Sequence: I → V | ||||||
Compositional bias | 2677-2701 | Polar residues | ||||
Sequence: AGRSTTPTSSPFRATSTSPNSQSSK | ||||||
Alternative sequence | VSP_035247 | 2687-2700 | in isoform 3 | |||
Sequence: PFRATSTSPNSQSS → SGLLLQVRTASPAK | ||||||
Alternative sequence | VSP_035248 | 2701-2896 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035249 | 2732-2810 | in isoform 4 and isoform 6 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF488829 EMBL· GenBank· DDBJ | AAO49478.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096857 EMBL· GenBank· DDBJ | CAB51071.1 EMBL· GenBank· DDBJ | mRNA | ||
AL021579 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z98750 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF253978 EMBL· GenBank· DDBJ | AAG44627.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006090 EMBL· GenBank· DDBJ | AAH06090.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC045713 EMBL· GenBank· DDBJ | AAH45713.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC058930 EMBL· GenBank· DDBJ | AAH58930.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AB029019 EMBL· GenBank· DDBJ | BAA83048.2 EMBL· GenBank· DDBJ | mRNA | ||
AL133635 EMBL· GenBank· DDBJ | CAB63759.1 EMBL· GenBank· DDBJ | mRNA | ||
AL162004 EMBL· GenBank· DDBJ | CAB82345.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000190 EMBL· GenBank· DDBJ | BAA90997.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK022492 EMBL· GenBank· DDBJ | BAB14056.1 EMBL· GenBank· DDBJ | mRNA |