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Protein

Small ubiquitin-related modifier 1

Gene

SUMO1

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

Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei36 – 361Interaction with PIAS2

GO - Molecular functioni

  • ion channel binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • potassium channel regulator activity Source: UniProtKB
  • SUMO transferase activity Source: Ensembl
  • transcription factor binding Source: AgBase
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • cytokine-mediated signaling pathway Source: Reactome
  • DNA repair Source: ProtInc
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of action potential Source: UniProtKB
  • negative regulation of delayed rectifier potassium channel activity Source: UniProtKB
  • negative regulation of DNA binding Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • palate development Source: UniProtKB
  • PML body organization Source: Ensembl
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein complex assembly Source: BHF-UCL
  • post-translational protein modification Source: Reactome
  • protein localization to nuclear pore Source: Ensembl
  • protein sumoylation Source: UniProtKB
  • regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  • regulation of protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000116030-MONOMER.
ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163725. SUMO is proteolytically processed.
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_24980. Regulation of IFNG signaling.
REACT_355174. SUMOylation of DNA damage response and repair proteins.
SignaLinkiP63165.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 1
Short name:
SUMO-1
Alternative name(s):
GAP-modifying protein 1
Short name:
GMP1
SMT3 homolog 3
Sentrin
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name:
Smt3C
Ubiquitin-like protein UBL1
Gene namesi
Name:SUMO1
Synonyms:SMT3C, SMT3H3, UBL1
ORF Names:OK/SW-cl.43
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12502. SUMO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • dendrite Source: Ensembl
  • fibrillar center Source: Ensembl
  • nuclear membrane Source: HPA
  • nuclear pore Source: ProtInc
  • nuclear speck Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • PML body Source: UniProtKB
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Non-syndromic orofacial cleft 10 (OFC10)1 Publication

The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.

Disease descriptionA birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.

See also OMIM:613705

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361F → A: Abolishes binding to PIAS2. 1 Publication

Organism-specific databases

MIMi613705. phenotype.
Orphaneti1991. Cleft lip with or without cleft palate.
PharmGKBiPA37149.

Polymorphism and mutation databases

BioMutaiSUMO1.
DMDMi52783799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 9796Small ubiquitin-related modifier 1PRO_0000035939Add
BLAST
Propeptidei98 – 1014PRO_0000035940

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei2 – 21Phosphoserine5 Publications
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
Modified residuei9 – 91Phosphoserine1 Publication
Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
Cross-linki97 – 97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63165.
PaxDbiP63165.
PRIDEiP63165.

PTM databases

PhosphoSiteiP63165.

Miscellaneous databases

PMAP-CutDBP63165.

Expressioni

Gene expression databases

BgeeiP63165.
CleanExiHS_SUMO1.
ExpressionAtlasiP63165. baseline and differential.
GenevisibleiP63165. HS.

Organism-specific databases

HPAiCAB004269.
HPA056956.

Interactioni

Subunit structurei

Interacts with SAE2, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1. Interacts with Epstein-barr virus BGLF4.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
G2XKQ03EBI-80140,EBI-10175576
Q59GP63EBI-80140,EBI-10243413
ARP102757EBI-80140,EBI-608057
ARKL1Q5BIX23EBI-80140,EBI-10243491
ATF2P153363EBI-80140,EBI-1170906
CARD9Q9H2573EBI-80140,EBI-751319
CCDC67Q05D603EBI-80140,EBI-748597
DAXXQ9UER77EBI-80140,EBI-77321
DNMT3BQ9UBC34EBI-80140,EBI-80125
DTX2Q86UW93EBI-80140,EBI-740376
EDARADDQ8WWZ35EBI-80140,EBI-2949647
EIF4EP067305EBI-80140,EBI-73440
ELK1P194195EBI-80140,EBI-726632
FAM118BQ9BPY33EBI-80140,EBI-726822
FBF1Q8TES7-63EBI-80140,EBI-10244131
FLJ13057Q53SE73EBI-80140,EBI-10172181
FSBPO950733EBI-80140,EBI-1059030
HGSO149643EBI-80140,EBI-740220
HIF1AQ166654EBI-80140,EBI-447269
HNRNPCP079103EBI-80140,EBI-357966
IKBKGQ9Y6K93EBI-80140,EBI-81279
MAPK1IP1LQ8NDC03EBI-80140,EBI-741424
MBD1Q9UIS93EBI-80140,EBI-867196
MYBP102423EBI-80140,EBI-298355
NFKB2Q006532EBI-80140,EBI-307326
PARP1P098742EBI-80140,EBI-355676
PIAS2O759286EBI-80140,EBI-348555
PMLP295903EBI-80140,EBI-295890
PRDM1O75626-22EBI-80140,EBI-7839538
Prdm1Q606363EBI-80140,EBI-7000804From a different organism.
PSIP1O754754EBI-80140,EBI-1801773
RAD54L2Q9Y4B43EBI-80140,EBI-948156
RANGAP1P460605EBI-80140,EBI-396091
RARAP102765EBI-80140,EBI-413374
RHOXF2Q9BQY43EBI-80140,EBI-372094
RWDD3Q9Y3V22EBI-80140,EBI-1549885
SART1O432902EBI-80140,EBI-607761
SATB1Q018262EBI-80140,EBI-743747
SENP1Q9P0U32EBI-80140,EBI-2822935
SOX10P566932EBI-80140,EBI-1167533
SOX2P484313EBI-80140,EBI-6124081
SP100P234976EBI-80140,EBI-751145
TANKQ928448EBI-80140,EBI-356349
TFCP2Q128003EBI-80140,EBI-717422
TRAF4Q9BUZ43EBI-80140,EBI-3650647
UBA2Q9UBT23EBI-80140,EBI-718569
UBE2IP632795EBI-80140,EBI-80168
UBE2IQ7KZS03EBI-80140,EBI-10180829
USPL1Q5W0Q75EBI-80140,EBI-2513899
ZBTB26Q9HCK03EBI-80140,EBI-3918996
ZBTB6Q159163EBI-80140,EBI-7227791
ZCCHC12Q6PEW13EBI-80140,EBI-748373
ZMYM5Q9UJ783EBI-80140,EBI-7228860

Protein-protein interaction databases

BioGridi113188. 1047 interactions.
DIPiDIP-29080N.
IntActiP63165. 124 interactions.
MINTiMINT-137859.
STRINGi9606.ENSP00000376076.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni9 – 113Combined sources
Turni16 – 183Combined sources
Beta strandi22 – 276Combined sources
Beta strandi29 – 313Combined sources
Beta strandi33 – 386Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 5511Combined sources
Helixi59 – 613Combined sources
Beta strandi62 – 665Combined sources
Helixi77 – 804Combined sources
Beta strandi87 – 926Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5RNMR-A1-101[»]
1TGZX-ray2.80B18-97[»]
1WYWX-ray2.10B1-97[»]
1Y8RX-ray2.75C/F1-97[»]
1Z5SX-ray3.01B18-97[»]
2ASQNMR-A1-97[»]
2BF8X-ray2.30B21-97[»]
2G4DX-ray2.80B/D20-97[»]
2IO2X-ray2.90B18-97[»]
2IY0X-ray2.77B20-101[»]
2IY1X-ray2.46B/D20-101[»]
2KQSNMR-A1-97[»]
2LASNMR-A20-97[»]
2MW5NMR-A1-97[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
3RZWX-ray2.15C/D1-97[»]
3UIPX-ray2.29B18-97[»]
4WJNX-ray1.50A17-97[»]
4WJOX-ray1.46A17-97[»]
4WJPX-ray1.70A/C17-97[»]
4WJQX-ray1.35A/C17-97[»]
ProteinModelPortaliP63165.
SMRiP63165. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9778Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63165.
KOiK12160.
OrthoDBiEOG76X62R.
PhylomeDBiP63165.
TreeFamiTF315116.

Family and domain databases

InterProiIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P63165-1) [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
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES
60 70 80 90 100
YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST

V
Length:101
Mass (Da):11,557
Last modified:September 27, 2004 - v1
Checksum:i89BE97D2D054FB33
GO
Isoform 2 (identifier: P63165-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-28: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:76
Mass (Da):8,799
Checksum:i709FCA25A95F9020
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751H → N in AAH66306 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4 – 2825Missing in isoform 2. CuratedVSP_046756Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99586 mRNA. Translation: CAA67898.1.
U61397 mRNA. Translation: AAB40388.1.
U38784 mRNA. Translation: AAC50733.1.
U67122 mRNA. Translation: AAC50996.1.
U72722 mRNA. Translation: AAB40390.1.
U83117 mRNA. Translation: AAB39999.1.
AB062294 mRNA. Translation: BAB93477.1.
BT006632 mRNA. Translation: AAP35278.1.
CR542147 mRNA. Translation: CAG46944.1.
CR542156 mRNA. Translation: CAG46953.1.
AK311840 mRNA. Translation: BAG34782.1.
AC079354 Genomic DNA. Translation: AAY24035.1.
CH471063 Genomic DNA. Translation: EAW70304.1.
CH471063 Genomic DNA. Translation: EAW70307.1.
BC006462 mRNA. Translation: AAH06462.1.
BC053528 mRNA. Translation: AAH53528.1.
BC066306 mRNA. Translation: AAH66306.1.
CCDSiCCDS2352.1. [P63165-1]
CCDS46493.1. [P63165-2]
RefSeqiNP_001005781.1. NM_001005781.1. [P63165-1]
NP_001005782.1. NM_001005782.1. [P63165-2]
NP_003343.1. NM_003352.4. [P63165-1]
UniGeneiHs.81424.

Genome annotation databases

EnsembliENST00000392244; ENSP00000376075; ENSG00000116030. [P63165-2]
ENST00000392245; ENSP00000376076; ENSG00000116030. [P63165-1]
ENST00000392246; ENSP00000376077; ENSG00000116030. [P63165-1]
GeneIDi7341.
KEGGihsa:7341.
UCSCiuc002uyz.1. human. [P63165-1]
uc002uza.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99586 mRNA. Translation: CAA67898.1.
U61397 mRNA. Translation: AAB40388.1.
U38784 mRNA. Translation: AAC50733.1.
U67122 mRNA. Translation: AAC50996.1.
U72722 mRNA. Translation: AAB40390.1.
U83117 mRNA. Translation: AAB39999.1.
AB062294 mRNA. Translation: BAB93477.1.
BT006632 mRNA. Translation: AAP35278.1.
CR542147 mRNA. Translation: CAG46944.1.
CR542156 mRNA. Translation: CAG46953.1.
AK311840 mRNA. Translation: BAG34782.1.
AC079354 Genomic DNA. Translation: AAY24035.1.
CH471063 Genomic DNA. Translation: EAW70304.1.
CH471063 Genomic DNA. Translation: EAW70307.1.
BC006462 mRNA. Translation: AAH06462.1.
BC053528 mRNA. Translation: AAH53528.1.
BC066306 mRNA. Translation: AAH66306.1.
CCDSiCCDS2352.1. [P63165-1]
CCDS46493.1. [P63165-2]
RefSeqiNP_001005781.1. NM_001005781.1. [P63165-1]
NP_001005782.1. NM_001005782.1. [P63165-2]
NP_003343.1. NM_003352.4. [P63165-1]
UniGeneiHs.81424.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5RNMR-A1-101[»]
1TGZX-ray2.80B18-97[»]
1WYWX-ray2.10B1-97[»]
1Y8RX-ray2.75C/F1-97[»]
1Z5SX-ray3.01B18-97[»]
2ASQNMR-A1-97[»]
2BF8X-ray2.30B21-97[»]
2G4DX-ray2.80B/D20-97[»]
2IO2X-ray2.90B18-97[»]
2IY0X-ray2.77B20-101[»]
2IY1X-ray2.46B/D20-101[»]
2KQSNMR-A1-97[»]
2LASNMR-A20-97[»]
2MW5NMR-A1-97[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
3RZWX-ray2.15C/D1-97[»]
3UIPX-ray2.29B18-97[»]
4WJNX-ray1.50A17-97[»]
4WJOX-ray1.46A17-97[»]
4WJPX-ray1.70A/C17-97[»]
4WJQX-ray1.35A/C17-97[»]
ProteinModelPortaliP63165.
SMRiP63165. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113188. 1047 interactions.
DIPiDIP-29080N.
IntActiP63165. 124 interactions.
MINTiMINT-137859.
STRINGi9606.ENSP00000376076.

Chemistry

ChEMBLiCHEMBL2146296.

PTM databases

PhosphoSiteiP63165.

Polymorphism and mutation databases

BioMutaiSUMO1.
DMDMi52783799.

Proteomic databases

MaxQBiP63165.
PaxDbiP63165.
PRIDEiP63165.

Protocols and materials databases

DNASUi7341.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392244; ENSP00000376075; ENSG00000116030. [P63165-2]
ENST00000392245; ENSP00000376076; ENSG00000116030. [P63165-1]
ENST00000392246; ENSP00000376077; ENSG00000116030. [P63165-1]
GeneIDi7341.
KEGGihsa:7341.
UCSCiuc002uyz.1. human. [P63165-1]
uc002uza.1. human.

Organism-specific databases

CTDi7341.
GeneCardsiGC02M203070.
HGNCiHGNC:12502. SUMO1.
HPAiCAB004269.
HPA056956.
MIMi601912. gene.
613705. phenotype.
neXtProtiNX_P63165.
Orphaneti1991. Cleft lip with or without cleft palate.
PharmGKBiPA37149.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63165.
KOiK12160.
OrthoDBiEOG76X62R.
PhylomeDBiP63165.
TreeFamiTF315116.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000116030-MONOMER.
ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163725. SUMO is proteolytically processed.
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_24980. Regulation of IFNG signaling.
REACT_355174. SUMOylation of DNA damage response and repair proteins.
SignaLinkiP63165.

Miscellaneous databases

EvolutionaryTraceiP63165.
GeneWikiiSmall_ubiquitin-related_modifier_1.
GenomeRNAii7341.
NextBioi28734.
PMAP-CutDBP63165.
PROiP63165.
SOURCEiSearch...

Gene expression databases

BgeeiP63165.
CleanExiHS_SUMO1.
ExpressionAtlasiP63165. baseline and differential.
GenevisibleiP63165. HS.

Family and domain databases

InterProiIPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family."
    Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C.
    Genomics 40:362-367(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia."
    Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.
    Oncogene 13:971-982(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Placenta.
  3. "UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins."
    Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K., Chen D.J.
    Genomics 36:271-279(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2."
    Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.
    Cell 88:97-107(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  5. "A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex."
    Matunis M.J., Coutavas E., Blobel G.
    J. Cell Biol. 135:1457-1470(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin."
    Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F., Chang H.M., Yeh E.T.H.
    J. Immunol. 157:4277-4281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  7. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  11. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  14. "Preferential modification of nuclear proteins by a novel ubiquitin-like molecule."
    Kamitani T., Nguyen H.P., Yeh E.T.H.
    J. Biol. Chem. 272:14001-14004(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  15. "Cell cycle regulation of PML modification and ND10 composition."
    Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.
    J. Cell Sci. 112:4581-4588(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif."
    Minty A., Dumont X., Kaghad M., Caput D.
    J. Biol. Chem. 275:36316-36323(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
  17. "Molecular features of human ubiquitin-like SUMO genes and their encoded proteins."
    Su H.-L., Li S.S.-L.
    Gene 296:65-73(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
    Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
    Biochemistry 42:9959-9969(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2I.
  19. "The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML."
    Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O., Everett R.D.
    Exp. Cell Res. 283:36-50(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK2.
  20. "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
    Xu Z., Au S.W.N.
    Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE.
  21. "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
    Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
    Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP2.
  22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Functional modulation of parkin through physical interaction with SUMO-1."
    Um J.W., Chung K.C.
    J. Neurosci. Res. 84:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARK2.
  24. "SUMO1 haploinsufficiency leads to cleft lip and palate."
    Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.
    Science 313:1751-1751(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION, INVOLVEMENT IN OFC10.
  25. "RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia."
    Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M., Silberstein S., Stalla G.K., Holsboer F., Arzt E.
    Cell 131:309-323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2I AND RWDD3.
  26. "Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution."
    Matic I., Macek B., Hilger M., Walther T.C., Mann M.
    J. Proteome Res. 7:4050-4057(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2.
  27. "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25."
    Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.
    Mol. Cell 30:610-619(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25.
  28. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
    Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
    Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  31. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
    Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
    J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-7 AND LYS-25, ACETYLATION AT SER-2.
    Tissue: Cervix carcinoma.
  32. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MTA1.
  35. "SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
    Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
    PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BHLHE40/DEC1.
  36. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  37. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
    Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
    Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  38. "PolySUMO-binding proteins identified through a string search."
    Sun H., Hunter T.
    J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SIMC1; CASP8AP2; RNF111 AND SOBP.
  39. "SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function."
    Li R., Wang L., Liao G., Guzzo C.M., Matunis M.J., Zhu H., Hayward S.D.
    J. Virol. 86:5412-5421(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4.
  40. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  41. "Structure determination of the small ubiquitin-related modifier SUMO-1."
    Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R., Becker J.
    J. Mol. Biol. 280:275-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  42. "A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex."
    Reverter D., Lima C.D.
    Structure 12:1519-1531(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2, CLEAVAGE.
  43. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
    Lois L.M., Lima C.D.
    EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1; SAE2 AND ATP.
  44. "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation."
    Song J., Zhang Z., Hu W., Chen Y.
    J. Biol. Chem. 280:40122-40129(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, MUTAGENESIS OF PHE-36.
  45. "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
    Reverter D., Lima C.D.
    Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I; RANGAP1 AND RANBP2.
  46. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
  48. "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."
    Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.
    Biochem. J. 398:345-352(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
  49. "SUMO protease SENP1 induces isomerization of the scissile peptide bond."
    Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
    Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND SENP1.

Entry informationi

Entry nameiSUMO1_HUMAN
AccessioniPrimary (citable) accession number: P63165
Secondary accession number(s): A8MUS8
, B2R4I5, P55856, Q6FGG0, Q6NZ62, Q93068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: June 24, 2015
This is version 137 of the entry and version 1 of the sequence. [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 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.