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Protein

Small ubiquitin-related modifier 4

Gene

SUMO4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may modulate protein subcellular localization, stability or activity. Upon oxidative stress, conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. May also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I.3 Publications

GO - Biological processi

  1. protein sumoylation Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 4
Short name:
SUMO-4
Alternative name(s):
Small ubiquitin-like protein 4
Gene namesi
Name:SUMO4
Synonyms:SMT3H4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21181. SUMO4.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

MIMi600320. phenotype.
PharmGKBiPA134979206.

Polymorphism and mutation databases

BioMutaiSUMO4.
DMDMi81175019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Small ubiquitin-related modifier 4PRO_0000042710Add
BLAST
Propeptidei94 – 952By similarityPRO_0000042711

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki93 – 93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

In contrast to SUMO1, SUMO2 and SUMO3, seems to be insensitive to sentrin-specific proteases due to the presence of Pro-90. This may impair processing to mature form and conjugation to substrates.

Keywords - PTMi

Isopeptide bond

Proteomic databases

MaxQBiQ6EEV6.
PaxDbiQ6EEV6.
PRIDEiQ6EEV6.

PTM databases

PhosphoSiteiQ6EEV6.

Expressioni

Tissue specificityi

Expressed mainly in adult and embryonic kidney. Expressed at various levels in immune tissues, with the highest expression in the lymph node and spleen.2 Publications

Gene expression databases

BgeeiQ6EEV6.
CleanExiHS_SUMO4.
GenevestigatoriQ6EEV6.

Organism-specific databases

HPAiHPA042123.
HPA048064.

Interactioni

Subunit structurei

Interacts with SAE2. Covalently attached to a number of proteins (Probable).Curated

Protein-protein interaction databases

BioGridi132223. 97 interactions.
STRINGi9606.ENSP00000318635.

Structurei

3D structure databases

ProteinModelPortaliQ6EEV6.
SMRiQ6EEV6. Positions 17-88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9579Ubiquitin-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.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiQ6EEV6.
KOiK12160.
OrthoDBiEOG76X62R.
PhylomeDBiQ6EEV6.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6EEV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANEKPTEEV KTENNNHINL KVAGQDGSVV QFKIKRQTPL SKLMKAYCEP
60 70 80 90
RGLSMKQIRF RFGGQPISGT DKPAQLEMED EDTIDVFQQP TGGVY
Length:95
Mass (Da):10,685
Last modified:November 8, 2005 - v2
Checksum:i9012CAEE734ED223
GO

Polymorphismi

Variant Val-55 could be associated with insulin-dependent diabetes mellitus 5 (IDDM5) [MIMi:600320].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551M → V May be associated with susceptibility to type 1 diabetes; greater NFKB1 transcriptional activity and IL12B expression. 6 Publications
Corresponds to variant rs237025 [ dbSNP | Ensembl ].
VAR_023740

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY340238 mRNA. Translation: AAR04484.1.
AB205057 Genomic DNA. Translation: BAH05006.1.
AL031133 Genomic DNA. Translation: CAA20019.1.
CH471051 Genomic DNA. Translation: EAW47808.1.
BC130305 mRNA. Translation: AAI30306.1.
CCDSiCCDS34549.1.
RefSeqiNP_001002255.1. NM_001002255.1.
UniGeneiHs.657168.

Genome annotation databases

EnsembliENST00000326669; ENSP00000318635; ENSG00000177688.
GeneIDi387082.
KEGGihsa:387082.
UCSCiuc003qml.3. human.

Polymorphism and mutation databases

BioMutaiSUMO4.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY340238 mRNA. Translation: AAR04484.1.
AB205057 Genomic DNA. Translation: BAH05006.1.
AL031133 Genomic DNA. Translation: CAA20019.1.
CH471051 Genomic DNA. Translation: EAW47808.1.
BC130305 mRNA. Translation: AAI30306.1.
CCDSiCCDS34549.1.
RefSeqiNP_001002255.1. NM_001002255.1.
UniGeneiHs.657168.

3D structure databases

ProteinModelPortaliQ6EEV6.
SMRiQ6EEV6. Positions 17-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132223. 97 interactions.
STRINGi9606.ENSP00000318635.

PTM databases

PhosphoSiteiQ6EEV6.

Polymorphism and mutation databases

BioMutaiSUMO4.
DMDMi81175019.

Proteomic databases

MaxQBiQ6EEV6.
PaxDbiQ6EEV6.
PRIDEiQ6EEV6.

Protocols and materials databases

DNASUi387082.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326669; ENSP00000318635; ENSG00000177688.
GeneIDi387082.
KEGGihsa:387082.
UCSCiuc003qml.3. human.

Organism-specific databases

CTDi387082.
GeneCardsiGC06P149763.
HGNCiHGNC:21181. SUMO4.
HPAiHPA042123.
HPA048064.
MIMi600320. phenotype.
608829. gene.
neXtProtiNX_Q6EEV6.
PharmGKBiPA134979206.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5227.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiQ6EEV6.
KOiK12160.
OrthoDBiEOG76X62R.
PhylomeDBiQ6EEV6.
TreeFamiTF315116.

Miscellaneous databases

GeneWikiiSUMO4.
GenomeRNAii387082.
NextBioi101180.
PROiQ6EEV6.
SOURCEiSearch...

Gene expression databases

BgeeiQ6EEV6.
CleanExiHS_SUMO4.
GenevestigatoriQ6EEV6.

Family and domain databases

InterProiIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 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. "A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus."
    Bohren K.M., Nadkarni V., Song J.H., Gabbay K.H., Owerbach D.
    J. Biol. Chem. 279:27233-27238(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-55, CHARACTERIZATION OF VARIANT VAL-55.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-55, CHARACTERIZATION OF VARIANT VAL-55.
  3. "SUMO4."
    Noso S.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-55.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-55.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-55.
  6. "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], VARIANT VAL-55.
  7. "A proline-90 residue unique to SUMO-4 prevents maturation and sumoylation."
    Owerbach D., McKay E.M., Yeh E.T.H., Gabbay K.H., Bohren K.M.
    Biochem. Biophys. Res. Commun. 337:517-520(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF PROTEOLYTIC CLEAVAGE.
  8. "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress."
    Guo D., Han J., Adam B.-L., Colburn N.H., Wang M.-H., Dong Z., Eizirik D.L., She J.-X., Wang C.-Y.
    Biochem. Biophys. Res. Commun. 337:1308-1318(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: ASSOCIATION OF VARIANT VAL-55 WITH INSULIN-DEPENDENT DIABETES MELLITUS.
  10. "Assessing the validity of the association between the SUMO4 M55V variant and risk of type 1 diabetes."
    Qu H., Bharaj B., Liu X.Q., Curtis J.A., Newhook L.A., Paterson A.D., Hudson T.J., Polychronakos C.
    Nat. Genet. 37:111-112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT VAL-55 WITH INSULIN-DEPENDENT DIABETES MELLITUS.
  11. "Assessing the validity of the association between the SUMO4 M55V variant and risk of type 1 diabetes."
    Park Y., Park S., Kang J., Yang S., Kim D.
    Nat. Genet. 37:112-112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT VAL-55 WITH INSULIN-DEPENDENT DIABETES MELLITUS.

Entry informationi

Entry nameiSUMO4_HUMAN
AccessioniPrimary (citable) accession number: Q6EEV6
Secondary accession number(s): A1L3W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 29, 2015
This is version 95 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.