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UniProtKB - Q8IUQ4 (SIAH1_HUMAN)

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Protein

E3 ubiquitin-protein ligase SIAH1

Gene

SIAH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins.19 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Enzyme regulationi

Inhibited by interaction with SNCAIP (isoform 2, but not isoform 1). May be inhibited by interaction with PEG10.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi98Zinc 1By similarity1
Metal bindingi105Zinc 1By similarity1
Metal bindingi117Zinc 1By similarity1
Metal bindingi121Zinc 1By similarity1
Metal bindingi128Zinc 21
Metal bindingi135Zinc 21
Metal bindingi147Zinc 21
Metal bindingi152Zinc 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 76RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri93 – 153SIAH-typePROSITE-ProRule annotationAdd BLAST61

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • apoptotic process Source: ProtInc
  • axon guidance Source: Reactome
  • cell cycle Source: UniProtKB-KW
  • cellular protein metabolic process Source: Reactome
  • nervous system development Source: ProtInc
  • neuron apoptotic process Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein catabolic process Source: UniProtKB
  • protein polyubiquitination Source: Reactome
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywordsi

Molecular functionDevelopmental protein, Transferase
Biological processApoptosis, Cell cycle, Differentiation, Spermatogenesis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-373752. Netrin-1 signaling.
R-HSA-977225. Amyloid fiber formation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ8IUQ4.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase SIAH1 (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase SIAH1Curated
Seven in absentia homolog 1
Short name:
Siah-1
Siah-1a
Gene namesi
Name:SIAH1
Synonyms:HUMSIAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:10857. SIAH1.

Subcellular locationi

GO - Cellular componenti

  • beta-catenin destruction complex Source: UniProtKB
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19S → A: Impaired ATM mediated phosphorylation, but normal interaction with HIPK2 and HIPK2 subsequent proteasomal degradation. 1 Publication1
Mutagenesisi19S → D: Reduced interaction with HIPK2 and HIPK2 subsequent proteasomal degradation. 1 Publication1
Mutagenesisi40E → R: Loss of function. 1 Publication1
Mutagenesisi41C → S: Loss of function; when associated with S-44. 1 Publication1
Mutagenesisi44C → S: Loss of function. 2 Publications1
Mutagenesisi55C → A: Loss of function; when associated with A-59 and S-72. 2 Publications1
Mutagenesisi55C → S: Loss of function; when associated with Y-59. 2 Publications1
Mutagenesisi59H → A: Loss of function; when associated with A-55 and S-72. 2 Publications1
Mutagenesisi59H → Y: Loss of function. 2 Publications1
Mutagenesisi66R → L: Decreased activity; when associated with T-68. 1 Publication1
Mutagenesisi68K → T: Decreased activity; when associated with L-66. 1 Publication1
Mutagenesisi72C → S: Loss of function; when associated with A-55 and A-59. 1 Publication1
Mutagenesisi76R → E: Decreased activity. 1 Publication1
Mutagenesisi124R → A in D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-214; A-215; A-231 and A-232. 1
Mutagenesisi142D → A in E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-151. 1
Mutagenesisi151Q → A in E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-142. 1
Mutagenesisi152H → Y: Abolishes ability to degrade DCC. 1 Publication1
Mutagenesisi161 – 162ED → AA in A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-226 and A-237. 2
Mutagenesisi198 – 200KYD → GDG: Impairs CTNNB1 degradation. 1 Publication3
Mutagenesisi202H → Y: No effect. 1 Publication1
Mutagenesisi211L → R: Abolishes ability to degrade DCC. 1 Publication1
Mutagenesisi214 – 215TR → AA in D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-231 and A-232. 2
Mutagenesisi224R → A in C; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-233. 1
Mutagenesisi226E → A in A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-237. 1
Mutagenesisi231 – 232RR → AA in D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-214 and A-215. 2
Mutagenesisi233R → A in C; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-233. 1
Mutagenesisi237E → A in A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-226. 1
Mutagenesisi252M → D or K: Impairs CTNNB1 degradation. 1 Publication1
Mutagenesisi253N → A in B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-265. 1
Mutagenesisi265Q → A in B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-253. 1

Organism-specific databases

DisGeNETi6477.
OpenTargetsiENSG00000196470.
PharmGKBiPA35759.

Polymorphism and mutation databases

BioMutaiSIAH1.
DMDMi46577493.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561631 – 282E3 ubiquitin-protein ligase SIAH1Add BLAST282

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphoserine; by ATM and ATR1 Publication1

Post-translational modificationi

Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal degradation of HIPK2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8IUQ4.
MaxQBiQ8IUQ4.
PaxDbiQ8IUQ4.
PeptideAtlasiQ8IUQ4.
PRIDEiQ8IUQ4.

PTM databases

iPTMnetiQ8IUQ4.
PhosphoSitePlusiQ8IUQ4.

Expressioni

Tissue specificityi

Widely expressed at a low level. Down-regulated in advanced hepatocellular carcinomas.2 Publications

Inductioni

May be induced by p53/TP53, suggesting that it may be required to modulate p53/TP53 response. The relevance of such activity in vivo is however unclear and may not exist.

Gene expression databases

BgeeiENSG00000196470.
CleanExiHS_SIAH1.
ExpressionAtlasiQ8IUQ4. baseline and differential.
GenevisibleiQ8IUQ4. HS.

Organism-specific databases

HPAiCAB018724.

Interactioni

Subunit structurei

Homodimer. Interacts with group 1 glutamate receptors GRM1 and GRM5. Interacts with DAB1, which may inhibit its activity. Interacts with UBE2E2. Interacts with PEG3. Interacts with GAPDH; leading to stabilize SIAH1 (By similarity). Component of some large E3 complex composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with UBE2I. Interacts with alpha-tubulin. Interacts with PEG10, which may inhibit its activity. Interacts with KHDRBS3. Interacts with SNCAIP and HIPK2.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-747107,EBI-747107
Q59GP63EBI-747107,EBI-10243413
AASDHPPTQ9NRN73EBI-747107,EBI-740884
AFF4Q9UHB75EBI-747107,EBI-395282
AFF4Q9UHB7-25EBI-747107,EBI-10261324
AQP1P299723EBI-747107,EBI-745213
ARMC9Q7Z3E5-23EBI-747107,EBI-10256990
ATXN7O152652EBI-747107,EBI-708350
BCL6P411823EBI-747107,EBI-765407
C14orf105Q17R993EBI-747107,EBI-10238351
CAPGP401213EBI-747107,EBI-4291044
CDC23Q9UJX23EBI-747107,EBI-396137
CDC34P494273EBI-747107,EBI-975634
CDK5R1Q8N6193EBI-747107,EBI-10266998
CDK5R1Q8TAM43EBI-747107,EBI-10271838
DDX41Q9UJV93EBI-747107,EBI-1046350
DNAJC15Q9Y5T43EBI-747107,EBI-10329228
DNALI1O146453EBI-747107,EBI-395638
EEF1DP296924EBI-747107,EBI-358607
EXOC3-AS1Q8N2X63EBI-747107,EBI-749333
FAM90A1Q86YD73EBI-747107,EBI-6658203
FLI1Q015433EBI-747107,EBI-2271018
FZD9Q8TAN23EBI-747107,EBI-741016
GDPD5Q8WTR43EBI-747107,EBI-2833203
HIST2H4BP628053EBI-747107,EBI-302023
INHAP051113EBI-11522811,EBI-10194422
KATNAL1Q9BW623EBI-747107,EBI-743591
KCNJ10P785083EBI-747107,EBI-9117877
KIAA0319LQ8IZA03EBI-747107,EBI-5240269
KIAA1217Q5T5P2-63EBI-747107,EBI-10188326
KIAA1683Q9H0B33EBI-747107,EBI-745878
KIF1BO603333EBI-747107,EBI-465633
KIFC3Q9BVG83EBI-747107,EBI-2125614
LACTB2Q53H823EBI-747107,EBI-3943430
MAB21L1Q133943EBI-747107,EBI-10229059
MAPK12P537783EBI-747107,EBI-602406
MAPKBP1O603363EBI-747107,EBI-947402
MOB3CQ70IA83EBI-747107,EBI-9679267
MTIF3Q9H2K03EBI-747107,EBI-3923617
MX1P205913EBI-747107,EBI-929476
MYD88Q998363EBI-747107,EBI-447677
NECTIN2Q926923EBI-747107,EBI-718419
NELFAQ9H3P23EBI-747107,EBI-5461341
NOL6Q9H6R4-43EBI-747107,EBI-10307896
OPRM1P353724EBI-747107,EBI-2624570
OTUB2Q96DC93EBI-747107,EBI-746259
PEG10Q86TG73EBI-747107,EBI-2858265
PFKMP082373EBI-747107,EBI-514788
PHC2Q8IXK05EBI-747107,EBI-713786
POU2AF1Q166332EBI-747107,EBI-943588
Pou2af1Q646935EBI-747107,EBI-943530From Mus musculus.
PRPF31F1T0A53EBI-747107,EBI-10177194
PRPF31Q8WWY33EBI-11522811,EBI-1567797
PRR20CP864795EBI-747107,EBI-10172814
PTPMT1Q8WUK03EBI-747107,EBI-7199479
PUF60Q9UHX17EBI-747107,EBI-1053259
PYGBP112163EBI-747107,EBI-1047231
QRICH1Q2TAL83EBI-747107,EBI-2798044
RAB33AQ140883EBI-747107,EBI-744685
RAD51AP1Q96B013EBI-747107,EBI-1178724
RAD51AP1Q96B01-23EBI-747107,EBI-1178743
RAD54L2Q9Y4B43EBI-747107,EBI-948156
RPS19BP1Q86WX33EBI-747107,EBI-4479407
SDCBPO005603EBI-747107,EBI-727004
SEPT4O43236-62EBI-747107,EBI-4372019
Sh3rf1Q69ZI15EBI-747107,EBI-957380From Mus musculus.
SPATA4Q8NEY33EBI-747107,EBI-7067221
SPATC1LQ9H0A93EBI-747107,EBI-372911
SYT7O435813EBI-747107,EBI-10184345
TBC1D22BQ9NU193EBI-747107,EBI-8787464
TMEM43Q9BTV43EBI-747107,EBI-721293
TOLLIPQ6FIE93EBI-747107,EBI-10249783
TP53BP2Q13625-33EBI-747107,EBI-10175039
TRIM23P364063EBI-747107,EBI-740098
TRIM27P143733EBI-747107,EBI-719493
TRIM7Q9C0293EBI-747107,EBI-2813981
UBE2KP610864EBI-747107,EBI-473850
UPP2O950453EBI-747107,EBI-10191025
UXTQ9UBK93EBI-747107,EBI-357355
WDYHV1Q96HA83EBI-747107,EBI-741158
XP697134EBI-747107,EBI-7088789From Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979).
XIAPP981703EBI-747107,EBI-517127
ZBP1A2RRL93EBI-747107,EBI-10173066
ZCCHC10Q8TBK63EBI-747107,EBI-597063
ZCCHC13Q8WW363EBI-747107,EBI-954111
ZFYVE21Q9BQ243EBI-747107,EBI-2849569
ZMAT3Q9HA383EBI-747107,EBI-2548480
ZNF148Q9UQR13EBI-747107,EBI-2688184
ZNF512BQ96KM63EBI-747107,EBI-1049952

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi112372. 164 interactors.
DIPiDIP-35684N.
IntActiQ8IUQ4. 125 interactors.
MINTiMINT-156060.
STRINGi9606.ENSP00000349156.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi95 – 97Combined sources3
Helixi101 – 103Combined sources3
Beta strandi108 – 110Combined sources3
Helixi111 – 120Combined sources10
Beta strandi122 – 124Combined sources3
Beta strandi130 – 134Combined sources5
Helixi141 – 143Combined sources3
Helixi144 – 151Combined sources8
Beta strandi156 – 167Combined sources12
Beta strandi172 – 184Combined sources13
Beta strandi187 – 197Combined sources11
Beta strandi203 – 213Combined sources11
Helixi215 – 218Combined sources4
Beta strandi221 – 229Combined sources9
Beta strandi232 – 238Combined sources7
Turni243 – 245Combined sources3
Helixi248 – 252Combined sources5
Beta strandi256 – 260Combined sources5
Helixi261 – 267Combined sources7
Beta strandi272 – 281Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A25X-ray2.20A90-282[»]
4C9ZX-ray1.95A/B91-282[»]
4CA1X-ray1.58A/B91-282[»]
4I7BX-ray3.00A/C90-282[»]
4I7CX-ray2.80A/C90-282[»]
4I7DX-ray2.40A/C90-282[»]
4X3GX-ray2.34A/B91-282[»]
ProteinModelPortaliQ8IUQ4.
SMRiQ8IUQ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IUQ4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni90 – 282SBDAdd BLAST193

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity.
The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family.By similarity

Sequence similaritiesi

Belongs to the SINA (Seven in absentia) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 76RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri93 – 153SIAH-typePROSITE-ProRule annotationAdd BLAST61

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3002. Eukaryota.
ENOG410XVP0. LUCA.
GeneTreeiENSGT00390000005434.
HOGENOMiHOG000231487.
HOVERGENiHBG055701.
InParanoidiQ8IUQ4.
KOiK04506.
OMAiEACEFRP.
OrthoDBiEOG091G0BPY.
PhylomeDBiQ8IUQ4.
TreeFamiTF312976.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 2 hits.
InterProiView protein in InterPro
IPR018121. 7-in-absentia-prot_TRAF-dom.
IPR004162. SINA-like.
IPR008974. TRAF-like.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR013010. Znf_SIAH.
PANTHERiPTHR10315. PTHR10315. 1 hit.
PfamiView protein in Pfam
PF03145. Sina. 1 hit.
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IUQ4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSRQTATALP TGTSKCPPSQ RVPALTGTTA SNNDLASLFE CPVCFDYVLP 
        60         70         80         90        100
PILQCQSGHL VCSNCRPKLT CCPTCRGPLG SIRNLAMEKV ANSVLFPCKY 
       110        120        130        140        150
ASSGCEITLP HTEKADHEEL CEFRPYSCPC PGASCKWQGS LDAVMPHLMH 
       160        170        180        190        200
QHKSITTLQG EDIVFLATDI NLPGAVDWVM MQSCFGFHFM LVLEKQEKYD 
       210        220        230        240        250
GHQQFFAIVQ LIGTRKQAEN FAYRLELNGH RRRLTWEATP RSIHEGIATA 
       260        270        280 
IMNSDCLVFD TSIAQLFAEN GNLGINVTIS MC
Length:282
Mass (Da):31,123
Last modified:April 26, 2004 - v2
Checksum:iFA0698D0DC1B0A15
GO
Isoform 2 (identifier: Q8IUQ4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTGKATPPSLYSWRGVLFTCLPAARTRKRKEM

Show »
Length:313
Mass (Da):34,628
Checksum:iBE3085493B0ABEC1
GO
Isoform 3 (identifier: Q8IUQ4-3) [UniParc]FASTAAdd to basket
Also known as: Siah-1S

The sequence of this isoform differs from the canonical sequence as follows:
     193-195: LEK → DLS
     196-282: Missing.

Show »
Length:195
Mass (Da):21,215
Checksum:iB5AB8D4079A7C723
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173P → S in CAE46191 (PubMed:17974005).Curated1
Sequence conflicti245E → G in CAE46191 (PubMed:17974005).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0101661M → MTGKATPPSLYSWRGVLFTC LPAARTRKRKEM in isoform 2. 2 Publications1
Alternative sequenceiVSP_029210193 – 195LEK → DLS in isoform 3. 1 Publication3
Alternative sequenceiVSP_029211196 – 282Missing in isoform 3. 1 PublicationAdd BLAST87

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63295 mRNA. Translation: AAC12950.1.
U76247 mRNA. Translation: AAC51907.1.
AJ400626 Genomic DNA. Translation: CAC35542.1.
EF026094 mRNA. Translation: ABK15529.1.
BX647064 mRNA. Translation: CAE46191.1.
BC035562 mRNA. Translation: AAH35562.1.
BC042550 mRNA. Translation: AAH42550.1.
BC044920 mRNA. Translation: AAH44920.1.
CCDSiCCDS10735.1. [Q8IUQ4-1]
CCDS32444.1. [Q8IUQ4-2]
RefSeqiNP_001006611.1. NM_001006610.1. [Q8IUQ4-2]
NP_003022.3. NM_003031.3. [Q8IUQ4-1]
XP_006721309.1. XM_006721246.1. [Q8IUQ4-1]
XP_011521581.1. XM_011523279.1. [Q8IUQ4-1]
UniGeneiHs.706828.

Genome annotation databases

EnsembliENST00000356721; ENSP00000349156; ENSG00000196470. [Q8IUQ4-2]
ENST00000380006; ENSP00000369343; ENSG00000196470. [Q8IUQ4-1]
ENST00000394725; ENSP00000378214; ENSG00000196470. [Q8IUQ4-1]
ENST00000568007; ENSP00000456421; ENSG00000196470. [Q8IUQ4-1]
GeneIDi6477.
KEGGihsa:6477.
UCSCiuc002efl.4. human. [Q8IUQ4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiSIAH1_HUMAN
AccessioniPrimary (citable) accession number: Q8IUQ4
Secondary accession number(s): A0FKF3
, O43269, Q49A58, Q92880
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 5, 2017
This is version 157 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families