Q7Z5J4 · RAI1_HUMAN
- ProteinRetinoic acid-induced protein 1
- GeneRAI1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1906 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | cytoplasm | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Biological Process | circadian regulation of gene expression | |
Biological Process | negative regulation of multicellular organism growth | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | skeletal system development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRetinoic acid-induced protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7Z5J4
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Smith-Magenis syndrome (SMS)
- Note
- DescriptionCharacterized by intellectual disability associated with development and growth delays. Affected persons have characteristic behavioral abnormalities, including self-injurious behaviors and sleep disturbance, and distinct craniofacial and skeletal anomalies.
- See alsoMIM:182290
Natural variants in SMS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_079636 | 758-1906 | missing | in SMS |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051300 | 90 | in dbSNP:rs3803763 | |||
Sequence: G → A | ||||||
Natural variant | VAR_024344 | 165 | in dbSNP:rs11649804 | |||
Sequence: P → T | ||||||
Natural variant | VAR_079636 | 758-1906 | in SMS | |||
Sequence: Missing | ||||||
Natural variant | VAR_051301 | 939 | in dbSNP:rs1759075 | |||
Sequence: Q → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,331 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_0000097159 | 1-1906 | UniProt | Retinoic acid-induced protein 1 | |||
Sequence: MQSFRERCGFHGKQQNYQQTSQETSRLENYRQPSQAGLSCDRQRLLAKDYYNPQPYPSYEGGAGTPSGTAAAVAADKYHRGSKALPTQQGLQGRPAFPGYGVQDSSPYPGRYAGEESLQAWGAPQPPPPQPQPLPAGVAKYDENLMKKTAVPPSRQYAEQGAQVPFRTHSLHVQQPPPPQQPLAYPKLQRQKLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQRVQNLHAYQSGRLSYDQQQQQQQQQQQQQQALQSRHHAQETLHYQNLAKYQHYGQQGQGYCQPDAAVRTPEQYYQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENFPYSQQPLSTGAFPAGITDHSHFMPLLNPSPTDATSSVDTQAGNCKPLQKDKLPENLLSDLSLQSLTALTSQVENISNTVQQLLLSKAAVPQKKGVKNLVSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQEADYLSGSEDPLERSFLYCNQARGSPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDSFQSLHGSLPLDSFSKFVAGERDCPRLLLSALAQEDLASEILGLQEAIGEKADKAWAEAPSLVKDSSKPPFSLENHSACLDSVAKSAWPRPGEPEALPDSLQLDKGGNAKDFSPGLFEDPSVAFATPDPKKTTGPLSFGTKPTLGVPAPDPTTAAFDCFPDTTAASSADSANPFAWPEENLGDACPRWGLHPGELTKGLEQGGKASDGISKGDTHEASACLGFQEEDPPGEKVASLPGDFKQEEVGGVKEEAGGLLQCPEVAKADRWLEDSRHCCSTADFGDLPLLPPTSRKEDLEAEEEYSSLCELLGSPEQRPGMQDPLSPKAPLICTKEEVEEVLDSKAGWGSPCHLSGESVILLGPTVGTESKVQSWFESSLSHMKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRRVHRGLPEAEDSPCRAPVLPKDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTKTQEIFHSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQKEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVLRSRSSSSSNASGNGGDGKEERPEGSPTLFKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGRGLKLEAIVQKITSPSLKKFACKAPGASPGNPLSPSLSDKDRGLKGAGGSPVGVEEGLVNVGTGQKLPTSGADPLCRNPTNRSLKGKLMNSKKLSSTDCFKTEAFTSPEALQPGGTALAPKKRSRKGRAGAHGLSKGPLEKRPYLGPALLLTPRDRASGTQGASEDNSGGGGKKPKMEELGLASQPPEGRPCQPQTRAQKQPGHTNYSSYSKRKRLTRGRAKNTTSSPCKGRAKRRRQQQVLPLDPAEPEIRLKYISSCKRLRSDSRTPAFSPFVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSFSLDAAGASLATLPGGSILQPRPSLPLSSTMHLGPVVSKALSTSCLVCCLCQNPANFKDLGDLCGPYYPEHCLPKKKPKLKEKVRPEGTCEEASLPLERTLKGPECAAAATAGKPPRPDGPADPAKQGPLRTSARGLSRRLQSCYCCDGREDGGEEAAPADKGRKHECSKEAPAEPGGEAQEHWVHEACAVWTGGVYLVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 339 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 345 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 472 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 568 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 578 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 637 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 683 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 696 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 696 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 776 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 805 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 811 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 819 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 846 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 880 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 880 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 892 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 892 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 901 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 901 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 916 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 921 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 924 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1064 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1064 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1068 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1068 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1075 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1076 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1077 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1122 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1136 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1352 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1358 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1360 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1374 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1387 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1394 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1425 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1430 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1431 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1431 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1476 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1533 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1550 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1590 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1616 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7Z5J4 | PIN1 Q13526 | 4 | EBI-743815, EBI-714158 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-261 | Disordered | ||||
Sequence: MQSFRERCGFHGKQQNYQQTSQETSRLENYRQPSQAGLSCDRQRLLAKDYYNPQPYPSYEGGAGTPSGTAAAVAADKYHRGSKALPTQQGLQGRPAFPGYGVQDSSPYPGRYAGEESLQAWGAPQPPPPQPQPLPAGVAKYDENLMKKTAVPPSRQYAEQGAQVPFRTHSLHVQQPPPPQQPLAYPKLQRQKLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQ | ||||||
Compositional bias | 12-39 | Polar residues | ||||
Sequence: GKQQNYQQTSQETSRLENYRQPSQAGLS | ||||||
Compositional bias | 192-261 | Polar residues | ||||
Sequence: KLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQ | ||||||
Region | 273-299 | Disordered | ||||
Sequence: RLSYDQQQQQQQQQQQQQQALQSRHHA | ||||||
Region | 335-370 | Disordered | ||||
Sequence: YQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENF | ||||||
Region | 469-520 | Disordered | ||||
Sequence: VSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQEADYLSG | ||||||
Compositional bias | 471-485 | Polar residues | ||||
Sequence: RTPEQHKSQHCSPEG | ||||||
Compositional bias | 496-514 | Polar residues | ||||
Sequence: PLSEPPSSTPQSTHAEPQE | ||||||
Region | 538-571 | Disordered | ||||
Sequence: SPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDS | ||||||
Region | 656-712 | Disordered | ||||
Sequence: SAWPRPGEPEALPDSLQLDKGGNAKDFSPGLFEDPSVAFATPDPKKTTGPLSFGTKP | ||||||
Region | 937-1299 | Disordered | ||||
Sequence: KVQSWFESSLSHMKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRRVHRGLPEAEDSPCRAPVLPKDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTKTQEIFHSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQKEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVLRSRSSSSSNASGNGGDGKEERPEGSPTLFKRMSSPKKAKPTKGNGEPATKLPPPETPD | ||||||
Compositional bias | 989-1011 | Basic and acidic residues | ||||
Sequence: KEPVPRGKSLRSRRVHRGLPEAE | ||||||
Compositional bias | 1104-1151 | Polar residues | ||||
Sequence: KAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTK | ||||||
Motif | 1160-1177 | Nuclear localization signal | ||||
Sequence: RRRPSEGRLPNCRATKKL | ||||||
Compositional bias | 1184-1198 | Polar residues | ||||
Sequence: PATFKVSSSPQKEGR | ||||||
Motif | 1223-1240 | Nuclear localization signal | ||||
Sequence: KRKSAFMAPVPTKKRNLV | ||||||
Compositional bias | 1239-1255 | Polar residues | ||||
Sequence: LVLRSRSSSSSNASGNG | ||||||
Region | 1344-1570 | Disordered | ||||
Sequence: FACKAPGASPGNPLSPSLSDKDRGLKGAGGSPVGVEEGLVNVGTGQKLPTSGADPLCRNPTNRSLKGKLMNSKKLSSTDCFKTEAFTSPEALQPGGTALAPKKRSRKGRAGAHGLSKGPLEKRPYLGPALLLTPRDRASGTQGASEDNSGGGGKKPKMEELGLASQPPEGRPCQPQTRAQKQPGHTNYSSYSKRKRLTRGRAKNTTSSPCKGRAKRRRQQQVLPLDP | ||||||
Compositional bias | 1407-1427 | Polar residues | ||||
Sequence: SLKGKLMNSKKLSSTDCFKTE | ||||||
Compositional bias | 1513-1534 | Polar residues | ||||
Sequence: GRPCQPQTRAQKQPGHTNYSSY | ||||||
Region | 1613-1637 | Disordered | ||||
Sequence: VVNSPGDAPKPHRKPSSSASSSSSS | ||||||
Region | 1746-1775 | Disordered | ||||
Sequence: AAAATAGKPPRPDGPADPAKQGPLRTSARG | ||||||
Zinc finger | 1780-1835 | C2HC pre-PHD-type | ||||
Sequence: LQSCYCCDGREDGGEEAAPADKGRKHECSKEAPAEPGGEAQEHWVHEACAVWTGGV | ||||||
Region | 1794-1819 | Disordered | ||||
Sequence: EEAAPADKGRKHECSKEAPAEPGGEA | ||||||
Zinc finger | 1855-1903 | PHD-type | ||||
Sequence: MMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q7Z5J4-1
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
- Length1,906
- Mass (Da)203,352
- Last updated2004-07-19 v2
- Checksum8D33A56C33BFE888
Q7Z5J4-2
- Name2
- Differences from canonical
- 207-233: THFPQHSQSFPTSSTYSSSVQGGGQGA → WWAGG
- 407-434: VDTQAGNCKPLQKDKLPENLLSDLSLQS → PAD
- 1415-1479: Missing
- 1803-1821: Missing
- 1856-1906: MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP → HGGTVALAPGDFSLPGLRFASLFQGPSWCDCPVLATSTPSSWSRCVPAAKKPGPPLGAATKDASTPTTTRVPAMQVRARPGTGGHWSPSKQSRGTLPGHSSPNPGPISLFSFPPLLPQQFFYPSVCLDLCWAMPGTWK
Q7Z5J4-3
- Name3
- Differences from canonical
- 1598-1640: FVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSF → LEPSLGAQNPRSGQNAPPAPADARPLCTTRDRRAYSAREQGQR
- 1641-1906: Missing
Q7Z5J4-4
- Name4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 12-39 | Polar residues | ||||
Sequence: GKQQNYQQTSQETSRLENYRQPSQAGLS | ||||||
Compositional bias | 192-261 | Polar residues | ||||
Sequence: KLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQ | ||||||
Alternative sequence | VSP_010995 | 207-233 | in isoform 2 | |||
Sequence: THFPQHSQSFPTSSTYSSSVQGGGQGA → WWAGG | ||||||
Alternative sequence | VSP_010996 | 407-434 | in isoform 2 | |||
Sequence: VDTQAGNCKPLQKDKLPENLLSDLSLQS → PAD | ||||||
Sequence conflict | 440 | in Ref. 2; AAO31738 | ||||
Sequence: S → L | ||||||
Compositional bias | 471-485 | Polar residues | ||||
Sequence: RTPEQHKSQHCSPEG | ||||||
Compositional bias | 496-514 | Polar residues | ||||
Sequence: PLSEPPSSTPQSTHAEPQE | ||||||
Alternative sequence | VSP_010997 | 947-966 | in isoform 4 | |||
Sequence: SHMKPGEEGPDGERAPGDST → YSVYICIHIHIYNIYEDCKC | ||||||
Alternative sequence | VSP_010998 | 967-1906 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 989-1011 | Basic and acidic residues | ||||
Sequence: KEPVPRGKSLRSRRVHRGLPEAE | ||||||
Compositional bias | 1104-1151 | Polar residues | ||||
Sequence: KAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTK | ||||||
Compositional bias | 1184-1198 | Polar residues | ||||
Sequence: PATFKVSSSPQKEGR | ||||||
Compositional bias | 1239-1255 | Polar residues | ||||
Sequence: LVLRSRSSSSSNASGNG | ||||||
Sequence conflict | 1302 | in Ref. 2; AAO31738 | ||||
Sequence: L → F | ||||||
Compositional bias | 1407-1427 | Polar residues | ||||
Sequence: SLKGKLMNSKKLSSTDCFKTE | ||||||
Alternative sequence | VSP_010999 | 1415-1479 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1513 | in Ref. 2; AAO31738 | ||||
Sequence: G → A | ||||||
Compositional bias | 1513-1534 | Polar residues | ||||
Sequence: GRPCQPQTRAQKQPGHTNYSSY | ||||||
Alternative sequence | VSP_011000 | 1598-1640 | in isoform 3 | |||
Sequence: FVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSF → LEPSLGAQNPRSGQNAPPAPADARPLCTTRDRRAYSAREQGQR | ||||||
Alternative sequence | VSP_011001 | 1641-1906 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1682 | in Ref. 5; CAD39144 | ||||
Sequence: T → A | ||||||
Alternative sequence | VSP_011002 | 1803-1821 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011003 | 1856-1906 | in isoform 2 | |||
Sequence: MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP → HGGTVALAPGDFSLPGLRFASLFQGPSWCDCPVLATSTPSSWSRCVPAAKKPGPPLGAATKDASTPTTTRVPAMQVRARPGTGGHWSPSKQSRGTLPGHSSPNPGPISLFSFPPLLPQQFFYPSVCLDLCWAMPGTWK |
Polymorphism
The size of the poly-Gln region may influence the age at onset of spinocerebellar ataxia type 2 (SCA2) (PubMed:10915763).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ271790 EMBL· GenBank· DDBJ | CAC20423.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271791 EMBL· GenBank· DDBJ | CAC20424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY172136 EMBL· GenBank· DDBJ | AAO31738.1 EMBL· GenBank· DDBJ | mRNA | ||
AB058723 EMBL· GenBank· DDBJ | BAB47449.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC021209 EMBL· GenBank· DDBJ | AAH21209.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133649 EMBL· GenBank· DDBJ | CAB63768.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834468 EMBL· GenBank· DDBJ | CAD39127.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834486 EMBL· GenBank· DDBJ | CAD39144.1 EMBL· GenBank· DDBJ | mRNA |