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P63166 (SUMO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 1

Short name=SUMO-1
Alternative name(s):
SMT3 homolog 3
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name=Smt3C
Gene names
Name:Sumo1
Synonyms:Smt3c, Smt3h3, Ubl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25 By similarity. Interacts with SAE2, UBE2I, 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 SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains) By similarity. Ref.4 Ref.5

Subcellular location

Nucleus membrane. Nucleus speckle. Cytoplasm. NucleusPML body By similarity. Note: Recruited by BCL11A into the nuclear body. Ref.4 Ref.7

Tissue specificity

Ubiquitous.

Developmental stage

Expressed at E13.5 strongly in the upper lip, primary palate and medial edge epithelia of the secondary palate. At E14.5 expression could be seen in the medial edge epithelial seam. Ref.6

Induction

By hypoxia. Ref.4

Post-translational modification

Cleavage of precursor form by SENP1 or SENP2 is necessary for function By similarity.

Polymeric SUMO1 chains undergo polyubiquitination by RNF4 By similarity.

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Ontologies

Keywords
   Biological processStress response
Ubl conjugation pathway
   Cellular componentCytoplasm
Membrane
Nucleus
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processPML body organization

Inferred from mutant phenotype PubMed 19033381. Source: MGI

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein localization to nuclear pore

Inferred from mutant phenotype PubMed 19033381. Source: MGI

protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.5. Source: MGI

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

nuclear body

Inferred from direct assay Ref.7. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.5PubMed 21931855. Source: MGI

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSUMO ligase activity

Inferred from direct assay PubMed 15122901Ref.5PubMed 18644859. Source: MGI

transcription factor binding

Inferred from physical interaction Ref.5. Source: MGI

ubiquitin protein ligase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ikzf1Q032672EBI-80152,EBI-908572
PTPN1P180312EBI-80152,EBI-968788From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9796Small ubiquitin-related modifier 1
PRO_0000035941
Propeptide98 – 1014 By similarity
PRO_0000035942

Regions

Domain20 – 9778Ubiquitin-like

Sites

Site361Interaction with PIAS2 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine Ref.8
Modified residue91Phosphoserine By similarity
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Sequences

Sequence LengthMass (Da)Tools
P63166 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: 89BE97D2D054FB33

FASTA10111,557
        10         20         30         40         50         60 
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 

        70         80         90        100 
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V 

« Hide

References

« Hide 'large scale' references
[1]"The ubiquitin-homology gene PIC1: characterization of mouse (Pic1) and human (UBL1) genes and pseudogenes."
Howe K., Williamson J., Boddy M.N., Sheer D., Freemont P.S., Solomon E.
Genomics 47:92-100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Kidney, Liver and Thymus.
[3]"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].
Strain: C57BL/6 and FVB/N.
Tissue: Colon and Eye.
[4]"Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1alpha in adult mouse brain and heart in vivo."
Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X., Sjoeland H., Billig H.
FEBS Lett. 569:293-300(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH HIF1A.
[5]"Ikaros SUMOylation: switching out of repression."
Gomez-del Arco P., Koipally J., Georgopoulos K.
Mol. Cell. Biol. 25:2688-2697(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKFZ1.
[6]"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: FUNCTION, DEVELOPMENTAL STAGE.
[7]"BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body."
Kuwata T., Nakamura T.
Genes Cells 13:931-940(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF033353 mRNA. Translation: AAC39959.1.
AK002536 mRNA. Translation: BAB22172.1.
AK011074 mRNA. Translation: BAB27379.1.
AK089081 mRNA. Translation: BAC40739.1.
AK159366 mRNA. Translation: BAE35024.1.
BC082566 mRNA. Translation: AAH82566.1.
BC083158 mRNA. Translation: AAH83158.1.
RefSeqNP_033486.1. NM_009460.2.
UniGeneMm.362118.

3D structure databases

ProteinModelPortalP63166.
SMRP63166. Positions 1-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204420. 30 interactions.
DIPDIP-29278N.
IntActP63166. 7 interactions.
MINTMINT-154756.

PTM databases

PhosphoSiteP63166.

Proteomic databases

PaxDbP63166.
PRIDEP63166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
GeneID22218.
KEGGmmu:22218.
UCSCuc007bdx.1. mouse.

Organism-specific databases

CTD7341.
MGIMGI:1197010. Sumo1.

Phylogenomic databases

eggNOGCOG5227.
GeneTreeENSGT00390000018808.
HOGENOMHOG000207495.
HOVERGENHBG053025.
InParanoidP63166.
KOK12160.
OMAITDNHTP.
OrthoDBEOG76X62R.
PhylomeDBP63166.
TreeFamTF315116.

Gene expression databases

BgeeP63166.
CleanExMM_SUMO1.
GenevestigatorP63166.

Family and domain databases

InterProIPR000626. Ubiquitin-like.
[Graphical view]
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio28734.
PROP63166.
SOURCESearch...

Entry information

Entry nameSUMO1_MOUSE
AccessionPrimary (citable) accession number: P63166
Secondary accession number(s): P55856, Q3TX92, Q93068
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot