Q9Y520 · PRC2C_HUMAN

  • Protein
    Protein PRRC2C
  • Gene
    PRRC2C
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for efficient formation of stress granules.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentmembrane
Molecular FunctionRNA binding
Biological Processhematopoietic progenitor cell differentiation
Biological Processstress granule assembly

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein PRRC2C
  • Alternative names
    • BAT2 domain-containing protein 1
    • HBV X-transactivated gene 2 protein
    • HBV XAg-transactivated protein 2
    • HLA-B-associated transcript 2-like 2
    • Proline-rich and coiled-coil-containing protein 2C

Gene names

    • Name
      PRRC2C
    • Synonyms
      BAT2D1, BAT2L2, KIAA1096, XTP2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9Y520
  • Secondary accessions
    • Q05DM8
    • Q49A39
    • Q6PD54
    • Q9H2N2
    • Q9HA05

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_046290235in dbSNP:rs10913157
Natural variantVAR_046291343in dbSNP:rs36013361
Natural variantVAR_046292468in dbSNP:rs704839
Natural variantVAR_046293906in dbSNP:rs760644
Natural variantVAR_046294959in dbSNP:rs34269512
Natural variantVAR_0462951624in dbSNP:rs235468
Natural variantVAR_0462961771in dbSNP:rs1687056
Natural variantVAR_0462971868in dbSNP:rs3820169
Natural variantVAR_0462981885in dbSNP:rs12025905
Natural variantVAR_0462991924in dbSNP:rs183523
Natural variantVAR_0595842717in dbSNP:rs2421847

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue, cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00003492391-2896UniProtProtein PRRC2C
Modified residue (large scale data)17PRIDEPhosphotyrosine
Modified residue (large scale data)19PRIDEPhosphothreonine
Modified residue (large scale data)21PRIDEPhosphoserine
Modified residue (large scale data)25PRIDEPhosphothreonine
Modified residue27UniProtN6-acetyllysine
Modified residue (large scale data)44PRIDEPhosphoserine
Modified residue (large scale data)159PRIDEPhosphothreonine
Modified residue (large scale data)164PRIDEPhosphotyrosine
Modified residue187UniProtPhosphoserine
Modified residue (large scale data)187PRIDEPhosphoserine
Modified residue (large scale data)189PRIDEPhosphoserine
Modified residue (large scale data)190PRIDEPhosphoserine
Modified residue191UniProtPhosphoserine
Modified residue (large scale data)191PRIDEPhosphoserine
Modified residue242UniProtAsymmetric dimethylarginine; alternate
Modified residue242UniProtOmega-N-methylarginine; alternate
Modified residue255UniProtAsymmetric dimethylarginine
Modified residue266UniProtAsymmetric dimethylarginine
Modified residue279UniProtOmega-N-methylarginine
Modified residue281UniProtOmega-N-methylarginine
Modified residue335UniProtPhosphoserine
Modified residue392UniProtN6-acetyllysine
Modified residue395UniProtPhosphoserine
Modified residue (large scale data)395PRIDEPhosphoserine
Modified residue500UniProtPhosphoserine
Modified residue (large scale data)500PRIDEPhosphoserine
Modified residue (large scale data)633PRIDEPhosphoserine
Modified residue (large scale data)636PRIDEPhosphoserine
Modified residue (large scale data)641PRIDEPhosphothreonine
Modified residue (large scale data)647PRIDEPhosphothreonine
Modified residue (large scale data)653PRIDEPhosphoserine
Modified residue779UniProtPhosphoserine
Modified residue (large scale data)779PRIDEPhosphoserine
Modified residue785UniProtPhosphoserine
Modified residue (large scale data)785PRIDEPhosphoserine
Modified residue (large scale data)799PRIDEPhosphoserine
Modified residue801UniProtPhosphoserine
Modified residue (large scale data)801PRIDEPhosphoserine
Modified residue (large scale data)812PRIDEPhosphotyrosine
Modified residue (large scale data)821PRIDEPhosphothreonine
Modified residue (large scale data)822PRIDEPhosphothreonine
Modified residue (large scale data)834PRIDEPhosphoserine
Modified residue (large scale data)847PRIDEPhosphotyrosine
Modified residue867UniProtPhosphoserine
Modified residue (large scale data)876PRIDEPhosphoserine
Modified residue878UniProtPhosphoserine
Modified residue (large scale data)878PRIDEPhosphoserine
Modified residue (large scale data)887PRIDEPhosphothreonine
Modified residue (large scale data)893PRIDEPhosphoserine
Modified residue (large scale data)917PRIDEPhosphoserine
Modified residue920UniProtPhosphoserine
Modified residue (large scale data)920PRIDEPhosphoserine
Modified residue (large scale data)924PRIDEPhosphoserine
Modified residue (large scale data)926PRIDEPhosphoserine
Modified residue929UniProtPhosphoserine
Modified residue (large scale data)929PRIDEPhosphoserine
Modified residue (large scale data)1013PRIDEPhosphoserine
Modified residue (large scale data)1100PRIDEPhosphoserine
Cross-link1133UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1218PRIDEPhosphotyrosine
Modified residue1242UniProtPhosphoserine
Modified residue (large scale data)1242PRIDEPhosphoserine
Modified residue (large scale data)1244PRIDEPhosphothreonine
Modified residue1246UniProtPhosphoserine
Modified residue (large scale data)1246PRIDEPhosphoserine
Modified residue1248UniProtPhosphoserine
Modified residue (large scale data)1248PRIDEPhosphoserine
Modified residue1249UniProtPhosphoserine
Modified residue (large scale data)1249PRIDEPhosphoserine
Modified residue1263UniProtPhosphoserine
Modified residue (large scale data)1263PRIDEPhosphoserine
Modified residue1265UniProtPhosphothreonine
Modified residue (large scale data)1265PRIDEPhosphothreonine
Modified residue1267UniProtPhosphothreonine
Modified residue (large scale data)1267PRIDEPhosphothreonine
Modified residue (large scale data)1269PRIDEPhosphoserine
Modified residue (large scale data)1274PRIDEPhosphoserine
Modified residue (large scale data)1276PRIDEPhosphoserine
Modified residue (large scale data)1280PRIDEPhosphoserine
Modified residue (large scale data)1476PRIDEPhosphoserine
Modified residue (large scale data)1480PRIDEPhosphothreonine
Modified residue (large scale data)1498PRIDEPhosphothreonine
Modified residue (large scale data)1500PRIDEPhosphoserine
Modified residue (large scale data)1542PRIDEPhosphoserine
Modified residue1544UniProtPhosphoserine
Modified residue (large scale data)1544PRIDEPhosphoserine
Modified residue (large scale data)1545PRIDEPhosphoserine
Modified residue1965UniProtPhosphothreonine
Modified residue (large scale data)1965PRIDEPhosphothreonine
Modified residue (large scale data)1971PRIDEPhosphotyrosine
Modified residue (large scale data)1980PRIDEPhosphothreonine
Modified residue1983UniProtPhosphoserine
Modified residue2013UniProtPhosphoserine
Modified residue (large scale data)2013PRIDEPhosphoserine
Modified residue (large scale data)2029PRIDEPhosphoserine
Modified residue (large scale data)2032PRIDEPhosphoserine
Modified residue (large scale data)2035PRIDEPhosphoserine
Modified residue (large scale data)2036PRIDEPhosphoserine
Modified residue2105UniProtPhosphoserine
Modified residue (large scale data)2105PRIDEPhosphoserine
Modified residue2143UniProtPhosphoserine
Modified residue (large scale data)2143PRIDEPhosphoserine
Modified residue (large scale data)2190PRIDEPhosphotyrosine
Modified residue (large scale data)2192PRIDEPhosphothreonine
Modified residue2260UniProtPhosphoserine
Modified residue (large scale data)2260PRIDEPhosphoserine
Modified residue (large scale data)2665PRIDEPhosphoserine
Modified residue2673UniProtPhosphothreonine
Modified residue (large scale data)2673PRIDEPhosphothreonine
Modified residue (large scale data)2680PRIDEPhosphoserine
Modified residue2682UniProtPhosphothreonine
Modified residue (large scale data)2682PRIDEPhosphothreonine
Modified residue (large scale data)2684PRIDEPhosphothreonine
Modified residue (large scale data)2685PRIDEPhosphoserine
Modified residue2686UniProtPhosphoserine
Modified residue (large scale data)2686PRIDEPhosphoserine
Modified residue (large scale data)2692PRIDEPhosphoserine
Modified residue2694UniProtPhosphoserine
Modified residue (large scale data)2694PRIDEPhosphoserine
Modified residue (large scale data)2707PRIDEPhosphotyrosine
Modified residue2814UniProtOmega-N-methylarginine
Modified residue2823UniProtAsymmetric dimethylarginine; alternate
Modified residue2823UniProtOmega-N-methylarginine; alternate

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Overexpressed in bladder cancer.

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region28-212Disordered
Compositional bias85-99Basic and acidic residues
Compositional bias122-147Polar residues
Compositional bias186-211Polar residues
Region264-729Disordered
Compositional bias297-314Basic and acidic residues
Compositional bias357-371Basic and acidic residues
Compositional bias411-427Pro residues
Compositional bias439-645Basic and acidic residues
Compositional bias671-703Polar residues
Compositional bias704-720Pro residues
Region750-788Disordered
Region804-1118Disordered
Compositional bias906-926Polar residues
Compositional bias954-1058Basic and acidic residues
Coiled coil1020-1046
Compositional bias1059-1084Pro residues
Compositional bias1087-1108Polar residues
Compositional bias1143-1195Basic and acidic residues
Region1143-1647Disordered
Compositional bias1210-1356Basic and acidic residues
Compositional bias1382-1448Basic and acidic residues
Compositional bias1451-1499Polar residues
Compositional bias1501-1519Basic and acidic residues
Compositional bias1533-1548Basic and acidic residues
Compositional bias1549-1565Polar residues
Compositional bias1597-1621Polar residues
Compositional bias1622-1645Basic and acidic residues
Region1670-1785Disordered
Coiled coil1682-1717
Compositional bias1684-1707Basic and acidic residues
Compositional bias1708-1748Polar residues
Compositional bias1755-1785Polar residues
Region1905-1991Disordered
Compositional bias1909-1929Pro residues
Compositional bias1930-1989Polar residues
Region2005-2164Disordered
Compositional bias2022-2069Polar residues
Compositional bias2077-2091Basic and acidic residues
Compositional bias2104-2136Basic and acidic residues
Compositional bias2143-2164Polar residues
Region2218-2238Disordered
Region2257-2290Disordered
Compositional bias2264-2290Polar residues
Region2317-2341Disordered
Region2668-2701Disordered
Compositional bias2677-2701Polar residues
Region2824-2896Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete

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.

  • Length
    2,896
  • Mass (Da)
    316,911
  • Last updated
    2011-07-27 v4
  • Checksum
    F0E037C36F04CDF9
MSEKSGQSTKAKDGKKYATLSLFNTYKGKSLETQKTTARHGLQSLGKVGISRRMPPPANLPSLKAENKGNDPNVNIVPKDGTGWASKQEQHEEEKTPEVPPAQPKPGVAAPPEVAPAPKSWASNKQGGQGDGIQVNSQFQQEFPSLQAAGDQEKKEKETNDDNYGPGPSLRPPNVACWRDGGKAAGSPSSSDQDEKLPGQDESTAGTSEQNDILKVVEKRIACGPPQAKLNGQQAALASQYRAMMPPYMFQQYPRMTYPPLHGPMRFPPSLSETNKGLRGRGPPPSWASEPERPSILSASELKELDKFDNLDAEADEGWAGAQMEVDYTEQLNFSDDDEQGSNSPKENNSEDQGSKASENNENKKETDEVSNTKSSSQIPAQPSVAKVPYGKGPSFNQERGTSSHLPPPPKLLAQQHPPPDRQAVPGRPGPFPSKQQVADEDEIWKQRRRQQSEISAAVERARKRREEEERRMEEQRKAACAEKLKRLDEKLGILEKQPSPEEIREREREKEREREKELEKEQEQEREKEREKDRERQQEKEKELEKEQEKQREMEKERKQEKEKELERQKEKEKELQKMKEQEKECELEKEREKLEEKIEPREPNLEPMVEKQESENSCNKEEEPVFTRQDSNRSEKEATPVVHETEPESGSQPRPAVLSGYFKQFQKSLPPRFQRQQEQMKQQQWQQQQQQGVLPQTVPSQPSSSTVPPPPHRPLYQPMQPHPQHLASMGFDPRWLMMQSYMDPRMMSGRPAMDIPPIHPGMIPPKPLMRRDQMEGSPNSSESFEHIARSARDHAISLSEPRMLWGSDPYPHAEPQQATTPKATEEPEDVRSEAALDQEQITAAYSVEHNQLEAHPKADFIRESSEAQVQKFLSRSVEDVRPHHTDANNQSACFEAPDQKTLSAPQEERISAVESQPSRKRSVSHGSNHTQKPDEQRSEPSAGIPKVTSRCIDSKEPIERPEEKPKKEGFIRSSEGPKPEKVYKSKSETRWGPRPSSNRREEVNDRPVRRSGPIKKPVLRDMKEEREQRKEKEGEKAEKVTEKVVVKPEKTEKKDLPPPPPPPQPPAPIQPQSVPPPIQPEAEKFPSTETATLAQKPSQDTEKPLEPVSTVQVEPAVKTVNQQTMAAPVVKEEKQPEKVISKDLVIERPRPDSRPAVKKESTLPPRTYWKEARERDWFPDQGYRGRGRGEYYSRGRSYRGSYGGRGRGGRGHTRDYPQYRDNKPRAEHIPSGPLRQREESETRSESSDFEVVPKRRRQRGSETDTDSEIHESASDKDSLSKGKLPKREERPENKKPVKPHSSFKPDNHVRIDNRLLEKPYVRDDDKAKPGFLPKGEPTRRGRGGTFRRGGRDPGGRPSRPSTLRRPAYRDNQWNPRQSEVPKPEDGEPPRRHEQFIPIAADKRPPKFERKFDPARERPRRQRPTRPPRQDKPPRFRRLREREAASKSNEVVAVPTNGTVNNVAQEPVNTLGDISGNKTPDLSNQNSSDQANEEWETASESSDFNERRERDEKKNADLNAQTVVKVGENVLPPKREIAKRSFSSQRPVDRQNRRGNNGPPKSGRNFSGPRNERRSGPPSKSGKRGPFDDQPAGTTGVDLINGSSAHHQEGVPNGTGQKNSKDSTGKKREDPKPGPKKPKEKVDALSQFDLNNYASVVIIDDHPEVTVIEDPQSNLNDDGFTEVVSKKQQKRLQDEERRKKEEQVIQVWNKKNANEKGRSQTSKLPPRFAKKQATGIQQAQSSASVPPLASAPLPPSTSASVPASTSAPLPATLTPVPASTSAPVPASTLAPVLASTSAPVPASPLAPVSASASVSASVPASTSAAAITSSSAPASAPAPTPILASVSTPASVTILASASIPILASALASTSAPTPAPAASSPAAPVITAPTIPASAPTASVPLAPASASAPAPAPTPVSAPNPAPPAPAQTQAQTHKPVQNPLQTTSQSSKQPPPSIRLPSAQTPNGTDYVASGKSIQTPQSHGTLTAELWDNKVAPPAVLNDISKKLGPISPPQPPSVSAWNKPLTSFGSAPSSEGAKNGQESGLEIGTDTIQFGAPASNGNENEVVPVLSEKSADKIPEPKEQRQKQPRAGPIKAQKLPDLSPVENKEHKPGPIGKERSLKNRKVKDAQQVEPEGQEKPSPATVRSTDPVTTKETKAVSEMSTEIGTMISVSSAEYGTNAKESVTDYTTPSSSLPNTVATNNTKMEDTLVNNVPLPNTLPLPKRETIQQSSSLTSVPPTTFSLTFKMESARKAWENSPNVREKGSPVTSTAPPIATGVSSSASGPSTANYNSFSSASMPQIPVASVTPTASLSGAGTYTTSSLSTKSTTTSDPPNICKVKPQQLQTSSLPSASHFSQLSCMPSLIAQQQQNPQVYVSQSAAAQIPAFYMDTSHLFNTQHARLAPPSLAQQQGFQPGLSQPTSVQQIPIPIYAPLQGQHQAQLSLGAGPAVSQAQELFSSSLQPYRSQPAFMQSSLSQPSVVLSGTAIHNFPTVQHQELAKAQSGLAFQQTSNTQPIPILYEHQLGQASGLGGSQLIDTHLLQARANLTQASNLYSGQVQQPGQTNFYNTAQSPSALQQVTVPLPASQLSLPNFGSTGQPLIALPQTLQPPLQHTTPQAQAQSLSRPAQVSQPFRGLIPAGTQHSMIATTGKMSEMELKAFGSGIDIKPGTPPIAGRSTTPTSSPFRATSTSPNSQSSKMNSIVYQKQFQSAPATVRMTQPFPTQFAPQILSQPNLVPPLVRAPHTNTFPAPVQRPPMALASQMPPPLTTGLMSHARLPHVARGPCGSLSGVRGNQAQAALKAEQDMKAKQRAEVLQSTQRFFSEQQQSKQIGGGKAQKVDSDSSKPPETLTDPPGVCQEKVEEKPPPAPSIATKPVRTGPIKPQAIKTEETKS

Q9Y520-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9Y520-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9Y520-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9Y520-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9Y520-6

Q9Y520-7

  • Name
    7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8Y7F4A0A2R8Y7F4_HUMANPRRC2C910
A0A2R8Y424A0A2R8Y424_HUMANPRRC2C159
E7EPN9E7EPN9_HUMANPRRC2C2819
A0A2R8YET2A0A2R8YET2_HUMANPRRC2C1090
H7C5N8H7C5N8_HUMANPRRC2C1300

Sequence caution

The sequence AAH06090.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAH45713.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAH58930.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence BAA90997.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0352441-243in isoform 2
Alternative sequenceVSP_03525037in isoform 7
Compositional bias85-99Basic and acidic residues
Compositional bias122-147Polar residues
Compositional bias186-211Polar residues
Compositional bias297-314Basic and acidic residues
Compositional bias357-371Basic and acidic residues
Compositional bias411-427Pro residues
Compositional bias439-645Basic and acidic residues
Sequence conflict454-456in Ref. 5; AAH45713
Sequence conflict561in Ref. 5; AAH45713
Compositional bias671-703Polar residues
Compositional bias704-720Pro residues
Compositional bias906-926Polar residues
Compositional bias954-1058Basic and acidic residues
Compositional bias1059-1084Pro residues
Compositional bias1087-1108Polar residues
Compositional bias1143-1195Basic and acidic residues
Compositional bias1210-1356Basic and acidic residues
Compositional bias1382-1448Basic and acidic residues
Compositional bias1451-1499Polar residues
Compositional bias1501-1519Basic and acidic residues
Compositional bias1533-1548Basic and acidic residues
Compositional bias1549-1565Polar residues
Compositional bias1597-1621Polar residues
Compositional bias1622-1645Basic and acidic residues
Compositional bias1684-1707Basic and acidic residues
Compositional bias1708-1748Polar residues
Compositional bias1755-1785Polar residues
Alternative sequenceVSP_0352451759-1805in isoform 5
Compositional bias1909-1929Pro residues
Compositional bias1930-1989Polar residues
Sequence conflict1940in Ref. 9; CAB82345
Compositional bias2022-2069Polar residues
Compositional bias2077-2091Basic and acidic residues
Compositional bias2104-2136Basic and acidic residues
Compositional bias2143-2164Polar residues
Alternative sequenceVSP_0352462185-2249in isoform 6
Compositional bias2264-2290Polar residues
Sequence conflict2443in Ref. 10; BAB14056
Sequence conflict2539in Ref. 10; BAA90997
Compositional bias2677-2701Polar residues
Alternative sequenceVSP_0352472687-2700in isoform 3
Alternative sequenceVSP_0352482701-2896in isoform 3
Alternative sequenceVSP_0352492732-2810in isoform 4 and isoform 6

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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