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UniProtKB - P63165 (SUMO1_HUMAN)

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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. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). 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. Covalently attached to ZFHX3 (PubMed:24651376).7 Publications

GO - Molecular functioni

  • enzyme binding Source: CAFA
  • glucocorticoid receptor binding Source: CAFA
  • ion channel binding Source: UniProtKB
  • potassium channel regulator activity Source: UniProtKB
  • protein binding, bridging Source: CAFA
  • protein C-terminus binding Source: CAFA
  • protein tag Source: GO_Central
  • RNA binding Source: UniProtKB
  • small protein activating enzyme binding Source: CAFA
  • SUMO transferase activity Source: Reactome
  • transcription corepressor binding Source: CAFA
  • transcription factor binding Source: AgBase
  • ubiquitin protein ligase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • cellular response to cadmium ion Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • DNA repair Source: ProtInc
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • global genome nucleotide-excision repair 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: CAFA
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  • palate development Source: UniProtKB
  • PML body organization Source: Ensembl
  • positive regulation of calcium-transporting ATPase activity Source: Ensembl
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein complex assembly Source: BHF-UCL
  • protein localization to nuclear pore Source: Ensembl
  • protein stabilization Source: UniProtKB
  • protein sumoylation Source: UniProtKB
  • regulation of cardiac muscle cell contraction Source: Ensembl
  • regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  • regulation of protein localization Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Biological processHost-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000116030-MONOMER.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-HSA-3065679. SUMO is proteolytically processed.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-4551638. SUMOylation of chromatin organization proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-877312. Regulation of IFNG signaling.
R-HSA-8866904. Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12502. SUMO1.

Subcellular locationi

  • Nucleus membrane
  • Nucleus speckle
  • Cytoplasm
  • Nucleus › PML body
  • Cell membrane 1 Publication
  • Nucleus 1 Publication

    • Note: Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body.By similarity1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • dendrite Source: Ensembl
  • fibrillar center Source: Ensembl
  • heterochromatin Source: Ensembl
  • nuclear body Source: UniProtKB
  • nuclear membrane Source: HPA
  • nuclear pore Source: ProtInc
  • nuclear speck Source: UniProtKB-SubCell
  • nuclear stress granule Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • PML body Source: UniProtKB
  • SUMO activating enzyme complex Source: CAFA
  • synapse Source: Ensembl
  • XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, 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)DescriptionActionsGraphical viewLength
Mutagenesisi36F → A: Abolishes binding to PIAS2. 1 Publication1

Organism-specific databases

DisGeNETi7341.
MalaCardsiSUMO1.
MIMi613705. phenotype.
OpenTargetsiENSG00000116030.
Orphaneti1991. Cleft lip with or without cleft palate.
PharmGKBiPA37149.

Chemistry databases

ChEMBLiCHEMBL2146296.

Polymorphism and mutation databases

BioMutaiSUMO1.
DMDMi52783799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000359392 – 97Small ubiquitin-related modifier 1Add BLAST96
PropeptideiPRO_000003594098 – 1014

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1 Publication1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei9PhosphoserineCombined sources1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residuei32PhosphoserineCombined sources1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki97Glycyl 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

EPDiP63165.
MaxQBiP63165.
PaxDbiP63165.
PeptideAtlasiP63165.
PRIDEiP63165.
TopDownProteomicsiP63165-1. [P63165-1]

PTM databases

iPTMnetiP63165.
PhosphoSitePlusiP63165.

Miscellaneous databases

PMAP-CutDBiP63165.

Expressioni

Gene expression databases

BgeeiENSG00000116030.
CleanExiHS_SUMO1.
ExpressionAtlasiP63165. baseline and differential.
GenevisibleiP63165. HS.

Organism-specific databases

HPAiCAB004269.
HPA056956.

Interactioni

Subunit structurei

Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (PubMed:19223394). Interacts with SAE2, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. 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 BGLF4.18 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei36Interaction with PIAS21

Binary interactionsi

WithEntry#Exp.IntActNotes
G2XKQ03EBI-80140,EBI-10175576
Q59GP63EBI-80140,EBI-10243413
ARP102757EBI-80140,EBI-608057
ARKL1Q5BIX25EBI-80140,EBI-10243491
ATF2P153365EBI-80140,EBI-1170906
CARD9Q9H2573EBI-80140,EBI-751319
DAXXQ9UER77EBI-80140,EBI-77321
DEUP1Q05D603EBI-80140,EBI-748597
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
HNRNPCP079105EBI-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 Mus musculus.
PSIP1O754754EBI-80140,EBI-1801773
RAD54L2Q9Y4B45EBI-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
SENP1Q9P0U34EBI-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
UBA2Q9UBT25EBI-80140,EBI-718569
UBE2IP632796EBI-80140,EBI-80168
UBE2IQ7KZS03EBI-80140,EBI-10180829
USPL1Q5W0Q75EBI-80140,EBI-2513899
ZBTB26Q9HCK05EBI-80140,EBI-3918996
ZBTB6Q159163EBI-80140,EBI-7227791
ZCCHC12Q6PEW16EBI-80140,EBI-748373
ZMYM5Q9UJ783EBI-80140,EBI-7228860

GO - Molecular functioni

  • enzyme binding Source: CAFA
  • glucocorticoid receptor binding Source: CAFA
  • ion channel binding Source: UniProtKB
  • protein binding, bridging Source: CAFA
  • protein C-terminus binding Source: CAFA
  • small protein activating enzyme binding Source: CAFA
  • transcription corepressor binding Source: CAFA
  • transcription factor binding Source: AgBase
  • ubiquitin protein ligase binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi113188. 168 interactors.
DIPiDIP-29080N.
IntActiP63165. 141 interactors.
MINTiMINT-137859.
STRINGi9606.ENSP00000376076.

Structurei

Secondary structure

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Turni9 – 11Combined sources3
Turni16 – 18Combined sources3
Beta strandi22 – 27Combined sources6
Beta strandi29 – 31Combined sources3
Beta strandi33 – 38Combined sources6
Beta strandi40 – 42Combined sources3
Helixi45 – 55Combined sources11
Helixi59 – 61Combined sources3
Beta strandi62 – 66Combined sources5
Helixi77 – 80Combined sources4
Beta strandi87 – 92Combined sources6
Beta strandi96 – 99Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-A1-101[»]
2MW5NMR-A1-97[»]
2N1ANMR-A1-101[»]
2N1VNMR-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[»]
5AEKX-ray3.00B/D/F/H/J/L/N/P/R/T/V/X20-97[»]
5ELJX-ray1.98B18-97[»]
ProteinModelPortaliP63165.
SMRiP63165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 97Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63165.
KOiK12160.
PhylomeDBiP63165.
TreeFamiTF315116.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiView protein in InterPro
IPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
PfamiView protein in Pfam
PF11976. Rad60-SLD. 1 hit.
SMARTiView protein in SMART
SM00213. UBQ. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiView protein in PROSITE
PS50053. UBIQUITIN_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti75H → N in AAH66306 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0467564 – 28Missing in isoform 2. CuratedAdd BLAST25

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.2. human. [P63165-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

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 nameiSUMO1_HUMAN
AccessioniPrimary (citable) accession number: P63165
Secondary accession number(s): A8MUS8
, B2R4I5, P55856, Q6FGG0, Q6NZ62, Q93068
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 5, 2017
This is version 159 of the entry and version 1 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 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