Q5T1R4 · ZEP3_HUMAN
- ProteinTranscription factor HIVEP3
- GeneHIVEP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2406 (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 | nucleus | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | skeletal muscle cell differentiation |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence KKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGMGGEMYP; the subsequence GSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILV; and the subsequence VKKEDSKEQPDLPSLAPPSSLPLSETSSRPAKSQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGW show transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameTranscription factor HIVEP3
- Alternative names
Gene names
- Community suggested namesHIVEP3
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5T1R4
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_042910 | 35 | in dbSNP:rs2146315 | |||
Sequence: V → I | ||||||
Natural variant | VAR_042911 | 484 | in a colorectal cancer sample; somatic mutation; dbSNP:rs780211835 | |||
Sequence: V → M | ||||||
Natural variant | VAR_042912 | 575 | in dbSNP:rs2810566 | |||
Sequence: H → R | ||||||
Natural variant | VAR_042913 | 1087 | in dbSNP:rs17363472 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_042914 | 2023 | in dbSNP:rs2483689 | |||
Sequence: A → P | ||||||
Natural variant | VAR_042915 | 2109 | in dbSNP:rs2991344 | |||
Sequence: D → A | ||||||
Natural variant | VAR_042916 | 2272 | in dbSNP:rs11809423 | |||
Sequence: G → R | ||||||
Natural variant | VAR_042917 | 2339 | in dbSNP:rs9439043 | |||
Sequence: T → A | ||||||
Natural variant | VAR_087891 | 2348 | in dbSNP:rs543298786 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,739 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000331627 | 1-2406 | UniProt | Transcription factor HIVEP3 | |||
Sequence: MDPEQSVKGTKKAEGSPRKRLTKGEAIQTSVSSSVPYPGSGTAATQESPAQELLAPQPFPGPSSVLREGSQEKTGQQQKPPKRPPIEASVHISQLPQHPLTPAFMSPGKPEHLLEGSTWQLVDPMRPGPSGSFVAPGLHPQSQLLPSHASIIPPEDLPGVPKVFVPRPSQVSLKPTEEAHKKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGMGGEMYPHGLEMERIPGEEFEEPTEGESTDSEEETSATSGHPAELSPRPKQPLLSSGLYSSGSHSSSHERCSLSQSSTAQSLEDPPPFVEPSSEHPLSHKPEDTHTIKQKLALRLSERKKVIDEQAFLSPGSKGSTESGYFSRSESAEQQVSPPNTNAKSYAEIIFGKCGRIGQRTAMLTATSTQPLLPLSTEDKPSLVPLSVPRTQVIEHITKLITINEAVVDTSEIDSVKPRRSSLSRRSSMESPKSSLYREPLSSHSEKTKPEQSLLSLQHPPSTAPPVPLLRSHSMPSAACTISTPHHPFRGSYSFDDHITDSEALSHSSHVFTSHPRMLKRQPAIELPLGGEYSSEEPGPSSKDTASKPSDEVEPKESELTKKTKKGLKTKGVIYECNICGARYKKRDNYEAHKKYYCSELQIAKPISAGTHTSPEAEKSQIEHEPWSQMMHYKLGTTLELTPLRKRRKEKSLGDEEEPPAFESTKSQFGSPGPSDAARNLPLESTKSPAEPSKSVPSLEGPTGFQPRTPKPGSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESNVSLSGSSRSASFERDDHGKAEAPSPSSDMRPKPLGTHMLTVPSHHPHAREMRRSASEQSPNVSHSAHMTETRSKSFDYGSLSLTGPSAPAPVAPPARVAPPERRKCFLVRQASLSRPPESELEVAPKGRQESEEPQPSSSKPSAKSSLSQISSAATSHGGPPGGKGPGQDRPPLGPTVPYTEALQVFHHPVAQTPLHEKPYLPPPVSLFSFQHLVQHEPGQSPEFFSTQAMSSLLSSPYSMPPLPPSLFQAPPLPLQPTVLHPGQLHLPQLMPHPANIPFRQPPSFLPMPYPTSSALSSGFFLPLQSQFALQLPGDVESHLPQIKTSLAPLATGSAGLSPSTEYSSDIRLPPVAPPASSSAPTSAPPLALPACPDTMVSLVVPVRVQTNMPSYGSAMYTTLSQILVTQSQGSSATVALPKFEEPPSKGTTVCGADVHEVGPGPSGLSEEQSRAFPTPYLRVPVTLPERKGTSLSSESILSLEGSSSTAGGSKRVLSPAGSLELTMETQQQKRVKEEEASKADEKLELVKPCSVVLTSTEDGKRPEKSHLGNQGQGRRELEMLSSLSSDPSDTKEIPPLPHPALSHGTAPGSEALKEYPQPSGKPHRRGLTPLSVKKEDSKEQPDLPSLAPPSSLPLSETSSRPAKSQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGWCISLYNPNLPGVSTKAALSLLRSKQKVSKETYTMATAPHPEAGRLVPSSSRKPRMTEVHLPSLVSPEGQKDLARVEKEEERRGEPEEDAPASQRGEPARIKIFEGGYKSNEEYVYVRGRGRGKYVCEECGIRCKKPSMLKKHIRTHTDVRPYVCKHCHFAFKTKGNLTKHMKSKAHSKKCQETGVLEELEAEEGTSDDLFQDSEGREGSEAVEEHQFSDLEDSDSDSDLDEDEDEDEEESQDELSRPSSEAPPPGPPHALRADSSPILGPQPPDAPASGTEATRGSSVSEAERLTASSCSMSSQSMPGLPWLGPAPLGSVEKDTGSALSYKPVSPRRPWSPSKEAGSRPPLARKHSLTKNDSSPQRCSPAREPQASAPSPPGLHVDPGRGMGALPCGSPRLQLSPLTLCPLGRELAPRAHVLSKLEGTTDPGLPRYSPTRRWSPGQAESPPRSAPPGKWALAGPGSPSAGEHGPGLGLDPRVLFPPAPLPHKLLSRSPETCASPWQKAESRSPSCSPGPAHPLSSRPFSALHDFHGHILARTEENIFSHLPLHSQHLTRAPCPLIPIGGIQMVQARPGAHPTLLPGPTAAWVSGFSGGGSDLTGAREAQERGRWSPTESSSASVSPVAKVSKFTLSSELEGGDYPKERERTGGGPGRPPDWTPHGTGAPAEPTPTHSPCTPPDTLPRPPQGRRAAQSWSPRLESPRAPTNPEPSATPPLDRSSSVGCLAEASARFPARTRNLSGEPRTRQDSPKPSGSGEPRAHPHQPEDRVPPNA | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 720 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 732 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 733 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 739 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 804 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 809 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 811 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 830 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 931 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 993 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1012 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1050 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1964 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2006 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2034 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2067 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2354 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2382 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5T1R4 | SFN P31947 | 5 | EBI-28989979, EBI-476295 | |
BINARY | Q5T1R4 | YWHAG P61981 | 2 | EBI-28989979, EBI-359832 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger, motif, coiled coil, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MDPEQSVKGTKKAEGSPRKRL | ||||||
Region | 1-112 | Disordered | ||||
Sequence: MDPEQSVKGTKKAEGSPRKRLTKGEAIQTSVSSSVPYPGSGTAATQESPAQELLAPQPFPGPSSVLREGSQEKTGQQQKPPKRPPIEASVHISQLPQHPLTPAFMSPGKPEH | ||||||
Compositional bias | 23-52 | Polar residues | ||||
Sequence: KGEAIQTSVSSSVPYPGSGTAATQESPAQE | ||||||
Zinc finger | 192-214 | C2H2-type 1 | ||||
Sequence: YICQYCSRPCAKPSVLQKHIRSH | ||||||
Region | 192-242 | ZAS1 | ||||
Sequence: YICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSH | ||||||
Region | 211-1074 | No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUN | ||||
Sequence: IRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGMGGEMYPHGLEMERIPGEEFEEPTEGESTDSEEETSATSGHPAELSPRPKQPLLSSGLYSSGSHSSSHERCSLSQSSTAQSLEDPPPFVEPSSEHPLSHKPEDTHTIKQKLALRLSERKKVIDEQAFLSPGSKGSTESGYFSRSESAEQQVSPPNTNAKSYAEIIFGKCGRIGQRTAMLTATSTQPLLPLSTEDKPSLVPLSVPRTQVIEHITKLITINEAVVDTSEIDSVKPRRSSLSRRSSMESPKSSLYREPLSSHSEKTKPEQSLLSLQHPPSTAPPVPLLRSHSMPSAACTISTPHHPFRGSYSFDDHITDSEALSHSSHVFTSHPRMLKRQPAIELPLGGEYSSEEPGPSSKDTASKPSDEVEPKESELTKKTKKGLKTKGVIYECNICGARYKKRDNYEAHKKYYCSELQIAKPISAGTHTSPEAEKSQIEHEPWSQMMHYKLGTTLELTPLRKRRKEKSLGDEEEPPAFESTKSQFGSPGPSDAARNLPLESTKSPAEPSKSVPSLEGPTGFQPRTPKPGSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESNVSLSGSSRSASFERDDHGKAEAPSPSSDMRPKPLGTHMLTVPSHHPHAREMRRSASEQSPNVSHSAHMTETRSKSFDYGSLSLTGPSAPAPVAPPARVAPPERRKCFLVRQASLSRPPESELEVAPKGRQESEEPQP | ||||||
Zinc finger | 220-242 | C2H2-type 2 | ||||
Sequence: YPCGPCGFSFKTKSNLYKHRKSH | ||||||
Region | 264-287 | Acidic 1 | ||||
Sequence: EMERIPGEEFEEPTEGESTDSEEE | ||||||
Region | 272-358 | Disordered | ||||
Sequence: EFEEPTEGESTDSEEETSATSGHPAELSPRPKQPLLSSGLYSSGSHSSSHERCSLSQSSTAQSLEDPPPFVEPSSEHPLSHKPEDTH | ||||||
Compositional bias | 306-336 | Polar residues | ||||
Sequence: LLSSGLYSSGSHSSSHERCSLSQSSTAQSLE | ||||||
Region | 377-409 | Disordered | ||||
Sequence: EQAFLSPGSKGSTESGYFSRSESAEQQVSPPNT | ||||||
Compositional bias | 382-409 | Polar residues | ||||
Sequence: SPGSKGSTESGYFSRSESAEQQVSPPNT | ||||||
Region | 481-540 | Disordered | ||||
Sequence: IDSVKPRRSSLSRRSSMESPKSSLYREPLSSHSEKTKPEQSLLSLQHPPSTAPPVPLLRS | ||||||
Region | 597-633 | Disordered | ||||
Sequence: LGGEYSSEEPGPSSKDTASKPSDEVEPKESELTKKTK | ||||||
Compositional bias | 615-633 | Basic and acidic residues | ||||
Sequence: SKPSDEVEPKESELTKKTK | ||||||
Zinc finger | 640-670 | CCHC HIVEP-type | ||||
Sequence: GVIYECNICGARYKKRDNYEAHKKYYCSELQ | ||||||
Region | 677-696 | Disordered | ||||
Sequence: AGTHTSPEAEKSQIEHEPWS | ||||||
Region | 706-1115 | Disordered | ||||
Sequence: TLELTPLRKRRKEKSLGDEEEPPAFESTKSQFGSPGPSDAARNLPLESTKSPAEPSKSVPSLEGPTGFQPRTPKPGSGSESGKERRTTSKEISVIQHTSSFEKSDSLEQPSGLEGEDKPLAQFPSPPPAPHGRSAHSLQPKLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESNVSLSGSSRSASFERDDHGKAEAPSPSSDMRPKPLGTHMLTVPSHHPHAREMRRSASEQSPNVSHSAHMTETRSKSFDYGSLSLTGPSAPAPVAPPARVAPPERRKCFLVRQASLSRPPESELEVAPKGRQESEEPQPSSSKPSAKSSLSQISSAATSHGGPPGGKGPGQDRPPLGPTV | ||||||
Compositional bias | 709-730 | Basic and acidic residues | ||||
Sequence: LTPLRKRRKEKSLGDEEEPPAF | ||||||
Compositional bias | 797-812 | Polar residues | ||||
Sequence: ISVIQHTSSFEKSDSL | ||||||
Compositional bias | 861-884 | Basic and acidic residues | ||||
Sequence: TEEPDRPDTEPEPPPKEPEKTEEF | ||||||
Region | 862-883 | Acidic 2 | ||||
Sequence: EEPDRPDTEPEPPPKEPEKTEE | ||||||
Motif | 903-909 | Nuclear localization signal | ||||
Sequence: PKKKRLR | ||||||
Compositional bias | 914-946 | Polar residues | ||||
Sequence: AQSSGESSFESSVPLSRSPSQESNVSLSGSSRS | ||||||
Compositional bias | 992-1019 | Polar residues | ||||
Sequence: ASEQSPNVSHSAHMTETRSKSFDYGSLS | ||||||
Compositional bias | 1069-1094 | Polar residues | ||||
Sequence: SEEPQPSSSKPSAKSSLSQISSAATS | ||||||
Compositional bias | 1268-1283 | Polar residues | ||||
Sequence: LATGSAGLSPSTEYSS | ||||||
Region | 1268-1303 | Disordered | ||||
Sequence: LATGSAGLSPSTEYSSDIRLPPVAPPASSSAPTSAP | ||||||
Compositional bias | 1406-1430 | Polar residues | ||||
Sequence: KGTSLSSESILSLEGSSSTAGGSKR | ||||||
Region | 1406-1459 | Disordered | ||||
Sequence: KGTSLSSESILSLEGSSSTAGGSKRVLSPAGSLELTMETQQQKRVKEEEASKAD | ||||||
Coiled coil | 1442-1466 | |||||
Sequence: METQQQKRVKEEEASKADEKLELVK | ||||||
Compositional bias | 1445-1459 | Basic and acidic residues | ||||
Sequence: QQQKRVKEEEASKAD | ||||||
Region | 1472-1594 | Disordered | ||||
Sequence: LTSTEDGKRPEKSHLGNQGQGRRELEMLSSLSSDPSDTKEIPPLPHPALSHGTAPGSEALKEYPQPSGKPHRRGLTPLSVKKEDSKEQPDLPSLAPPSSLPLSETSSRPAKSQEGTDSKKVLQ | ||||||
Compositional bias | 1476-1490 | Basic and acidic residues | ||||
Sequence: EDGKRPEKSHLGNQG | ||||||
Compositional bias | 1494-1508 | Polar residues | ||||
Sequence: RELEMLSSLSSDPSD | ||||||
Compositional bias | 1569-1594 | Polar residues | ||||
Sequence: SSLPLSETSSRPAKSQEGTDSKKVLQ | ||||||
Region | 1692-1727 | Disordered | ||||
Sequence: SLVSPEGQKDLARVEKEEERRGEPEEDAPASQRGEP | ||||||
Compositional bias | 1700-1724 | Basic and acidic residues | ||||
Sequence: KDLARVEKEEERRGEPEEDAPASQR | ||||||
Zinc finger | 1754-1776 | C2H2-type 3 | ||||
Sequence: YVCEECGIRCKKPSMLKKHIRTH | ||||||
Region | 1754-1806 | ZAS2 | ||||
Sequence: YVCEECGIRCKKPSMLKKHIRTHTDVRPYVCKHCHFAFKTKGNLTKHMKSKAH | ||||||
Zinc finger | 1782-1806 | C2H2-type 4 | ||||
Sequence: YVCKHCHFAFKTKGNLTKHMKSKAH | ||||||
Region | 1817-1872 | Acidic 3 | ||||
Sequence: EELEAEEGTSDDLFQDSEGREGSEAVEEHQFSDLEDSDSDSDLDEDEDEDEEESQD | ||||||
Region | 1818-2033 | Disordered | ||||
Sequence: ELEAEEGTSDDLFQDSEGREGSEAVEEHQFSDLEDSDSDSDLDEDEDEDEEESQDELSRPSSEAPPPGPPHALRADSSPILGPQPPDAPASGTEATRGSSVSEAERLTASSCSMSSQSMPGLPWLGPAPLGSVEKDTGSALSYKPVSPRRPWSPSKEAGSRPPLARKHSLTKNDSSPQRCSPAREPQASAPSPPGLHVDPGRGMGALPCGSPRLQL | ||||||
Compositional bias | 1829-1848 | Basic and acidic residues | ||||
Sequence: LFQDSEGREGSEAVEEHQFS | ||||||
Compositional bias | 1849-1873 | Acidic residues | ||||
Sequence: DLEDSDSDSDLDEDEDEDEEESQDE | ||||||
Compositional bias | 1910-1937 | Polar residues | ||||
Sequence: TEATRGSSVSEAERLTASSCSMSSQSMP | ||||||
Repeat | 1964-1967 | 1 | ||||
Sequence: SPRR | ||||||
Repeat | 1970-1973 | 2 | ||||
Sequence: SPSK | ||||||
Compositional bias | 1986-2002 | Polar residues | ||||
Sequence: SLTKNDSSPQRCSPARE | ||||||
Repeat | 1993-1996 | 3 | ||||
Sequence: SPQR | ||||||
Repeat | 1998-2001 | 4 | ||||
Sequence: SPAR | ||||||
Region | 2052-2113 | Disordered | ||||
Sequence: LSKLEGTTDPGLPRYSPTRRWSPGQAESPPRSAPPGKWALAGPGSPSAGEHGPGLGLDPRVL | ||||||
Region | 2053-2148 | 6 X 4 AA tandem repeats of S-P-X-[RK] | ||||
Sequence: SKLEGTTDPGLPRYSPTRRWSPGQAESPPRSAPPGKWALAGPGSPSAGEHGPGLGLDPRVLFPPAPLPHKLLSRSPETCASPWQKAESRSPSCSPG | ||||||
Repeat | 2067-2070 | 5 | ||||
Sequence: SPTR | ||||||
Repeat | 2079-2082 | 6 | ||||
Sequence: SPPR | ||||||
Region | 2125-2151 | Disordered | ||||
Sequence: SRSPETCASPWQKAESRSPSCSPGPAH | ||||||
Compositional bias | 2129-2149 | Polar residues | ||||
Sequence: ETCASPWQKAESRSPSCSPGP | ||||||
Region | 2224-2406 | Disordered | ||||
Sequence: GFSGGGSDLTGAREAQERGRWSPTESSSASVSPVAKVSKFTLSSELEGGDYPKERERTGGGPGRPPDWTPHGTGAPAEPTPTHSPCTPPDTLPRPPQGRRAAQSWSPRLESPRAPTNPEPSATPPLDRSSSVGCLAEASARFPARTRNLSGEPRTRQDSPKPSGSGEPRAHPHQPEDRVPPNA | ||||||
Compositional bias | 2244-2262 | Polar residues | ||||
Sequence: WSPTESSSASVSPVAKVSK | ||||||
Compositional bias | 2304-2318 | Pro residues | ||||
Sequence: PTHSPCTPPDTLPRP |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing. Additional isoforms can be generated by alternative splicing or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a premature codon stop.
Q5T1R4-1
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
- SynonymsHIVEP3S
- Length2,406
- Mass (Da)259,465
- Last updated2004-12-21 v1
- ChecksumAFCCFDAF87014A7D
Q5T1R4-2
- Name2
- Differences from canonical
- 2136-2136: Missing
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MDPEQSVKGTKKAEGSPRKRL | ||||||
Compositional bias | 23-52 | Polar residues | ||||
Sequence: KGEAIQTSVSSSVPYPGSGTAATQESPAQE | ||||||
Sequence conflict | 44 | in Ref. 1; AAK01082 | ||||
Sequence: A → P | ||||||
Sequence conflict | 94-95 | in Ref. 1; AAK01082 | ||||
Sequence: QL → HV | ||||||
Sequence conflict | 123 | in Ref. 1; AAK01082 | ||||
Sequence: D → S | ||||||
Sequence conflict | 127 | in Ref. 1; AAK01082 | ||||
Sequence: P → L | ||||||
Sequence conflict | 133-134 | in Ref. 1; AAK01082 | ||||
Sequence: FV → LL | ||||||
Compositional bias | 306-336 | Polar residues | ||||
Sequence: LLSSGLYSSGSHSSSHERCSLSQSSTAQSLE | ||||||
Compositional bias | 382-409 | Polar residues | ||||
Sequence: SPGSKGSTESGYFSRSESAEQQVSPPNT | ||||||
Sequence conflict | 589 | in Ref. 1; AAK01082 | ||||
Sequence: R → P | ||||||
Compositional bias | 615-633 | Basic and acidic residues | ||||
Sequence: SKPSDEVEPKESELTKKTK | ||||||
Compositional bias | 709-730 | Basic and acidic residues | ||||
Sequence: LTPLRKRRKEKSLGDEEEPPAF | ||||||
Compositional bias | 797-812 | Polar residues | ||||
Sequence: ISVIQHTSSFEKSDSL | ||||||
Compositional bias | 861-884 | Basic and acidic residues | ||||
Sequence: TEEPDRPDTEPEPPPKEPEKTEEF | ||||||
Sequence conflict | 901 | in Ref. 1; AAK01082 | ||||
Sequence: L → A | ||||||
Compositional bias | 914-946 | Polar residues | ||||
Sequence: AQSSGESSFESSVPLSRSPSQESNVSLSGSSRS | ||||||
Sequence conflict | 961 | in Ref. 1; AAK01082 | ||||
Sequence: S → D | ||||||
Compositional bias | 992-1019 | Polar residues | ||||
Sequence: ASEQSPNVSHSAHMTETRSKSFDYGSLS | ||||||
Sequence conflict | 1034-1035 | in Ref. 1; AAK01082 | ||||
Sequence: RV → GE | ||||||
Sequence conflict | 1048-1049 | in Ref. 1; AAK01082 | ||||
Sequence: QA → SP | ||||||
Compositional bias | 1069-1094 | Polar residues | ||||
Sequence: SEEPQPSSSKPSAKSSLSQISSAATS | ||||||
Sequence conflict | 1110 | in Ref. 1; AAK01082 | ||||
Sequence: P → A | ||||||
Sequence conflict | 1180 | in Ref. 2; BAB13381 and 5; AAI52564 | ||||
Sequence: P → L | ||||||
Compositional bias | 1268-1283 | Polar residues | ||||
Sequence: LATGSAGLSPSTEYSS | ||||||
Sequence conflict | 1279 | in Ref. 1; AAK01082 | ||||
Sequence: T → Q | ||||||
Compositional bias | 1406-1430 | Polar residues | ||||
Sequence: KGTSLSSESILSLEGSSSTAGGSKR | ||||||
Compositional bias | 1445-1459 | Basic and acidic residues | ||||
Sequence: QQQKRVKEEEASKAD | ||||||
Compositional bias | 1476-1490 | Basic and acidic residues | ||||
Sequence: EDGKRPEKSHLGNQG | ||||||
Compositional bias | 1494-1508 | Polar residues | ||||
Sequence: RELEMLSSLSSDPSD | ||||||
Sequence conflict | 1524 | in Ref. 1; AAK01082 | ||||
Sequence: T → Q | ||||||
Compositional bias | 1569-1594 | Polar residues | ||||
Sequence: SSLPLSETSSRPAKSQEGTDSKKVLQ | ||||||
Compositional bias | 1700-1724 | Basic and acidic residues | ||||
Sequence: KDLARVEKEEERRGEPEEDAPASQR | ||||||
Compositional bias | 1829-1848 | Basic and acidic residues | ||||
Sequence: LFQDSEGREGSEAVEEHQFS | ||||||
Compositional bias | 1849-1873 | Acidic residues | ||||
Sequence: DLEDSDSDSDLDEDEDEDEEESQDE | ||||||
Compositional bias | 1910-1937 | Polar residues | ||||
Sequence: TEATRGSSVSEAERLTASSCSMSSQSMP | ||||||
Compositional bias | 1986-2002 | Polar residues | ||||
Sequence: SLTKNDSSPQRCSPARE | ||||||
Compositional bias | 2129-2149 | Polar residues | ||||
Sequence: ETCASPWQKAESRSPSCSPGP | ||||||
Alternative sequence | VSP_033279 | 2136 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 2244-2262 | Polar residues | ||||
Sequence: WSPTESSSASVSPVAKVSK | ||||||
Compositional bias | 2304-2318 | Pro residues | ||||
Sequence: PTHSPCTPPDTLPRP | ||||||
Sequence conflict | 2376 | in Ref. 1; AAK01082 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF278765 EMBL· GenBank· DDBJ | AAK01082.1 EMBL· GenBank· DDBJ | mRNA | ||
AB046775 EMBL· GenBank· DDBJ | BAB13381.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL445933 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC152563 EMBL· GenBank· DDBJ | AAI52564.1 EMBL· GenBank· DDBJ | mRNA |