UniProtKB - O75925 (PIAS1_HUMAN)
E3 SUMO-protein ligase PIAS1
PIAS1
Functioni
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity).
Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).
By similarity2 PublicationsCaution
: protein sumoylation Pathwayi
This protein is involved in the pathway protein sumoylation, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 351 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 353 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 374 | ZincPROSITE-ProRule annotation | 1 | |
Metal bindingi | 377 | ZincPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 320 – 405 | SP-RING-typePROSITE-ProRule annotationAdd BLAST | 86 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- DNA-binding transcription factor binding Source: Ensembl
- enzyme binding Source: UniProtKB
- SUMO ligase activity Source: UniProtKB
- SUMO transferase activity Source: Reactome
- transcription coregulator activity Source: GO_Central
- transcription corepressor activity Source: ProtInc
- ubiquitin protein ligase binding Source: Ensembl
- zinc ion binding Source: InterPro
GO - Biological processi
- fat cell differentiation Source: Ensembl
- negative regulation of transcription by RNA polymerase II Source: Ensembl
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
- positive regulation of protein sumoylation Source: UniProtKB
- protein sumoylation Source: BHF-UCL
- receptor signaling pathway via JAK-STAT Source: ProtInc
- regulation of cell population proliferation Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
Keywordsi
Molecular function | DNA-binding, Transferase |
Biological process | Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
PathwayCommonsi | O75925 |
Reactomei | R-HSA-3108214, SUMOylation of DNA damage response and repair proteins R-HSA-3232118, SUMOylation of transcription factors R-HSA-3232142, SUMOylation of ubiquitinylation proteins R-HSA-3899300, SUMOylation of transcription cofactors R-HSA-4090294, SUMOylation of intracellular receptors R-HSA-4551638, SUMOylation of chromatin organization proteins R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-877312, Regulation of IFNG signaling |
SignaLinki | O75925 |
SIGNORi | O75925 |
UniPathwayi | UPA00886 |
Names & Taxonomyi
Protein namesi | Recommended name: E3 SUMO-protein ligase PIAS1 (EC:2.3.2.-)Alternative name(s): DEAD/H box-binding protein 1 E3 SUMO-protein transferase PIAS1Curated Gu-binding protein Short name: GBP Protein inhibitor of activated STAT protein 1 RNA helicase II-binding protein |
Gene namesi | Name:PIAS1 Synonyms:DDXBP1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:2752, PIAS1 |
MIMi | 603566, gene |
neXtProti | NX_O75925 |
VEuPathDBi | HostDB:ENSG00000033800 |
Subcellular locationi
Nucleus
- Nucleus speckle 2 Publications
- PML body By similarity
Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.
Nucleus
- nuclear speck Source: UniProtKB-SubCell
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
- PML body Source: UniProtKB-SubCell
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 351 | C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 8554 |
OpenTargetsi | ENSG00000033800 |
PharmGKBi | PA33285 |
Miscellaneous databases
Pharosi | O75925, Tbio |
Genetic variation databases
BioMutai | PIAS1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000218974 | 2 – 651 | E3 SUMO-protein ligase PIAS1Add BLAST | 650 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources | 1 | |
Cross-linki | 40 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 46 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 238 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 453 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 467 | PhosphoserineCombined sources | 1 | |
Modified residuei | 468 | PhosphoserineCombined sources | 1 | |
Modified residuei | 483 | PhosphoserineBy similarity | 1 | |
Modified residuei | 485 | PhosphoserineCombined sources | 1 | |
Modified residuei | 487 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 488 | PhosphoserineCombined sources | 1 | |
Cross-linki | 493 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 503 | PhosphoserineCombined sources | 1 | |
Modified residuei | 510 | PhosphoserineCombined sources | 1 | |
Modified residuei | 522 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | O75925 |
jPOSTi | O75925 |
MassIVEi | O75925 |
MaxQBi | O75925 |
PaxDbi | O75925 |
PeptideAtlasi | O75925 |
PRIDEi | O75925 |
ProteomicsDBi | 3657 50293 [O75925-1] |
PTM databases
iPTMneti | O75925 |
PhosphoSitePlusi | O75925 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000033800, Expressed in bone marrow and 246 other tissues |
ExpressionAtlasi | O75925, baseline and differential |
Genevisiblei | O75925, HS |
Organism-specific databases
HPAi | ENSG00000033800, Low tissue specificity |
Interactioni
Subunit structurei
Interacts with NCOA2 and AR.
Interacts with NR2C1; the interaction promotes its sumoylation (By similarity).
Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation.
Interacts with SP3 (preferentially when SUMO-modified).
Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase.
Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation.
Interacts with PTK2/FAK1; the interaction promotes its sumoylation.
Interacts with DDX5.
Interacts with PML (By similarity).
Interacts with MTA1.
Interacts with SUMO1P1/SUMO5 (PubMed:27211601).
Interacts with PRDM1/Blimp-1 (PubMed:28842558).
By similarity17 Publications(Microbial infection) Interacts with ebolavirus VP35; this interaction mediates the sumoylation of IRF7 and contributes to the viral inhibition of IFN-type I production.
1 PublicationBinary interactionsi
O75925
GO - Molecular functioni
- DNA-binding transcription factor binding Source: Ensembl
- enzyme binding Source: UniProtKB
- ubiquitin protein ligase binding Source: Ensembl
Protein-protein interaction databases
BioGRIDi | 114124, 144 interactors |
CORUMi | O75925 |
DIPi | DIP-5970N |
ELMi | O75925 |
IntActi | O75925, 111 interactors |
MINTi | O75925 |
STRINGi | 9606.ENSP00000249636 |
Miscellaneous databases
RNActi | O75925, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | O75925 |
BMRBi | O75925 |
SMRi | O75925 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O75925 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 11 – 45 | SAPPROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 124 – 288 | PINITPROSITE-ProRule annotationAdd BLAST | 165 | |
Repeati | 520 – 523 | 1 | 4 | |
Repeati | 557 – 560 | 2 | 4 | |
Repeati | 598 – 601 | 3; approximate | 4 | |
Repeati | 612 – 615 | 4; approximate | 4 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 462 – 473 | SUMO1-bindingBy similarityAdd BLAST | 12 | |
Regioni | 465 – 511 | DisorderedSequence analysisAdd BLAST | 47 | |
Regioni | 520 – 615 | 4 X 4 AA repeats of N-T-S-LAdd BLAST | 96 | |
Regioni | 599 – 632 | DisorderedSequence analysisAdd BLAST | 34 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 19 – 23 | LXXLL motif | 5 | |
Motifi | 56 – 64 | Nuclear localization signalSequence analysis | 9 | |
Motifi | 368 – 380 | Nuclear localization signalSequence analysisAdd BLAST | 13 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 480 – 511 | Polar residuesSequence analysisAdd BLAST | 32 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 320 – 405 | SP-RING-typePROSITE-ProRule annotationAdd BLAST | 86 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG2169, Eukaryota |
GeneTreei | ENSGT01030000234539 |
HOGENOMi | CLU_020768_3_0_1 |
InParanoidi | O75925 |
OMAi | CFVSKQM |
OrthoDBi | 1205949at2759 |
PhylomeDBi | O75925 |
TreeFami | TF323787 |
Family and domain databases
Gene3Di | 1.10.720.30, 1 hit 2.60.120.780, 1 hit 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR027227, PIAS1 IPR023321, PINIT IPR038654, PINIT_sf IPR003034, SAP_dom IPR036361, SAP_dom_sf IPR004181, Znf_MIZ IPR013083, Znf_RING/FYVE/PHD |
PANTHERi | PTHR10782:SF11, PTHR10782:SF11, 1 hit |
Pfami | View protein in Pfam PF14324, PINIT, 1 hit PF02891, zf-MIZ, 1 hit |
SMARTi | View protein in SMART SM00513, SAP, 1 hit |
SUPFAMi | SSF68906, SSF68906, 1 hit |
PROSITEi | View protein in PROSITE PS51466, PINIT, 1 hit PS50800, SAP, 1 hit PS51044, ZF_SP_RING, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS
60 70 80 90 100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD
110 120 130 140 150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL
160 170 180 190 200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL
210 220 230 240 250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI
260 270 280 290 300
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK
310 320 330 340 350
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT
360 370 380 390 400
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT
410 420 430 440 450
DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS
460 470 480 490 500
SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH
510 520 530 540 550
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS
560 570 580 590 600
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS
610 620 630 640 650
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL
D
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH3BSI8 | H3BSI8_HUMAN | E3 SUMO-protein ligase PIAS1 | PIAS1 | 160 | Annotation score: | ||
H3BS65 | H3BS65_HUMAN | E3 SUMO-protein ligase PIAS1 | PIAS1 | 64 | Annotation score: | ||
H3BUL7 | H3BUL7_HUMAN | E3 SUMO-protein ligase PIAS1 | PIAS1 | 20 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 119 | E → K in AAC36702 (PubMed:9724754).Curated | 1 | |
Sequence conflicti | 266 – 268 | IVV → MC in AAC36702 (PubMed:9724754).Curated | 3 | |
Sequence conflicti | 613 | S → T in AAB58488 (PubMed:15489334).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056219 | 1 – 7 | MADSAEL → MFTLQDSYV in isoform 2. 1 Publication | 7 | |
Alternative sequenceiVSP_057195 | 312 – 325 | IKEKL…DSEIA → STYDKLISLIQLFC in isoform 3. 1 PublicationAdd BLAST | 14 | |
Alternative sequenceiVSP_057196 | 326 – 651 | Missing in isoform 3. 1 PublicationAdd BLAST | 326 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF077951 mRNA Translation: AAC36702.1 AF167160 mRNA Translation: AAD49722.1 FJ997900 mRNA Translation: ACR77525.1 AK094641 mRNA Translation: BAG52901.1 AK314515 mRNA Translation: BAG37114.1 AC107871 Genomic DNA No translation available. AC135628 Genomic DNA No translation available. BC118587 mRNA Translation: AAI18588.1 BC121797 mRNA Translation: AAI21798.1 U78524 mRNA Translation: AAB58488.1 |
CCDSi | CCDS45290.1 [O75925-1] CCDS81902.1 [O75925-2] |
RefSeqi | NP_001307616.1, NM_001320687.1 [O75925-2] NP_057250.1, NM_016166.2 [O75925-1] XP_016878177.1, XM_017022688.1 [O75925-2] |
Genome annotation databases
Ensembli | ENST00000249636.11; ENSP00000249636.6; ENSG00000033800.14 ENST00000545237.1; ENSP00000438574.1; ENSG00000033800.14 [O75925-2] |
GeneIDi | 8554 |
KEGGi | hsa:8554 |
MANE-Selecti | ENST00000249636.11; ENSP00000249636.6; NM_016166.3; NP_057250.1 |
UCSCi | uc002aqz.4, human [O75925-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF077951 mRNA Translation: AAC36702.1 AF167160 mRNA Translation: AAD49722.1 FJ997900 mRNA Translation: ACR77525.1 AK094641 mRNA Translation: BAG52901.1 AK314515 mRNA Translation: BAG37114.1 AC107871 Genomic DNA No translation available. AC135628 Genomic DNA No translation available. BC118587 mRNA Translation: AAI18588.1 BC121797 mRNA Translation: AAI21798.1 U78524 mRNA Translation: AAB58488.1 |
CCDSi | CCDS45290.1 [O75925-1] CCDS81902.1 [O75925-2] |
RefSeqi | NP_001307616.1, NM_001320687.1 [O75925-2] NP_057250.1, NM_016166.2 [O75925-1] XP_016878177.1, XM_017022688.1 [O75925-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1V66 | NMR | - | A | 1-65 | [»] | |
AlphaFoldDBi | O75925 | |||||
BMRBi | O75925 | |||||
SMRi | O75925 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 114124, 144 interactors |
CORUMi | O75925 |
DIPi | DIP-5970N |
ELMi | O75925 |
IntActi | O75925, 111 interactors |
MINTi | O75925 |
STRINGi | 9606.ENSP00000249636 |
PTM databases
iPTMneti | O75925 |
PhosphoSitePlusi | O75925 |
Genetic variation databases
BioMutai | PIAS1 |
Proteomic databases
EPDi | O75925 |
jPOSTi | O75925 |
MassIVEi | O75925 |
MaxQBi | O75925 |
PaxDbi | O75925 |
PeptideAtlasi | O75925 |
PRIDEi | O75925 |
ProteomicsDBi | 3657 50293 [O75925-1] |
Protocols and materials databases
Antibodypediai | 26284, 368 antibodies from 35 providers |
DNASUi | 8554 |
Genome annotation databases
Ensembli | ENST00000249636.11; ENSP00000249636.6; ENSG00000033800.14 ENST00000545237.1; ENSP00000438574.1; ENSG00000033800.14 [O75925-2] |
GeneIDi | 8554 |
KEGGi | hsa:8554 |
MANE-Selecti | ENST00000249636.11; ENSP00000249636.6; NM_016166.3; NP_057250.1 |
UCSCi | uc002aqz.4, human [O75925-1] |
Organism-specific databases
CTDi | 8554 |
DisGeNETi | 8554 |
GeneCardsi | PIAS1 |
HGNCi | HGNC:2752, PIAS1 |
HPAi | ENSG00000033800, Low tissue specificity |
MIMi | 603566, gene |
neXtProti | NX_O75925 |
OpenTargetsi | ENSG00000033800 |
PharmGKBi | PA33285 |
VEuPathDBi | HostDB:ENSG00000033800 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2169, Eukaryota |
GeneTreei | ENSGT01030000234539 |
HOGENOMi | CLU_020768_3_0_1 |
InParanoidi | O75925 |
OMAi | CFVSKQM |
OrthoDBi | 1205949at2759 |
PhylomeDBi | O75925 |
TreeFami | TF323787 |
Enzyme and pathway databases
UniPathwayi | UPA00886 |
PathwayCommonsi | O75925 |
Reactomei | R-HSA-3108214, SUMOylation of DNA damage response and repair proteins R-HSA-3232118, SUMOylation of transcription factors R-HSA-3232142, SUMOylation of ubiquitinylation proteins R-HSA-3899300, SUMOylation of transcription cofactors R-HSA-4090294, SUMOylation of intracellular receptors R-HSA-4551638, SUMOylation of chromatin organization proteins R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-877312, Regulation of IFNG signaling |
SignaLinki | O75925 |
SIGNORi | O75925 |
Miscellaneous databases
BioGRID-ORCSi | 8554, 78 hits in 1057 CRISPR screens |
ChiTaRSi | PIAS1, human |
EvolutionaryTracei | O75925 |
GeneWikii | PIAS1 |
GenomeRNAii | 8554 |
Pharosi | O75925, Tbio |
PROi | PR:O75925 |
RNActi | O75925, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000033800, Expressed in bone marrow and 246 other tissues |
ExpressionAtlasi | O75925, baseline and differential |
Genevisiblei | O75925, HS |
Family and domain databases
Gene3Di | 1.10.720.30, 1 hit 2.60.120.780, 1 hit 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR027227, PIAS1 IPR023321, PINIT IPR038654, PINIT_sf IPR003034, SAP_dom IPR036361, SAP_dom_sf IPR004181, Znf_MIZ IPR013083, Znf_RING/FYVE/PHD |
PANTHERi | PTHR10782:SF11, PTHR10782:SF11, 1 hit |
Pfami | View protein in Pfam PF14324, PINIT, 1 hit PF02891, zf-MIZ, 1 hit |
SMARTi | View protein in SMART SM00513, SAP, 1 hit |
SUPFAMi | SSF68906, SSF68906, 1 hit |
PROSITEi | View protein in PROSITE PS51466, PINIT, 1 hit PS50800, SAP, 1 hit PS51044, ZF_SP_RING, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PIAS1_HUMAN | |
Accessioni | O75925Primary (citable) accession number: O75925 Secondary accession number(s): B2RB67 Q9UN02 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 5, 2002 |
Last sequence update: | March 5, 2002 | |
Last modified: | May 25, 2022 | |
This is version 208 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families