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P63166

- SUMO1_MOUSE

UniProt

P63166 - SUMO1_MOUSE

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Protein
Small ubiquitin-related modifier 1
Gene
Sumo1, Smt3c, Smt3h3, Ubl1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

Sites

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

GO - Molecular functioni

  1. SUMO ligase activity Source: MGI
  2. protein binding Source: IntAct
  3. transcription factor binding Source: MGI
  4. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. PML body organization Source: MGI
  2. negative regulation of DNA binding Source: Ensembl
  3. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  4. negative regulation of transcription, DNA-templated Source: Ensembl
  5. palate development Source: UniProtKB
  6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  7. positive regulation of protein complex assembly Source: Ensembl
  8. protein localization to nuclear pore Source: MGI
  9. protein sumoylation Source: UniProtKB
  10. regulation of transcription, DNA-templated Source: MGI
  11. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_196649. SUMO is proteolytically processed.
REACT_198645. Regulation of IFNG signaling.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Sumo1
Synonyms:Smt3c, Smt3h3, Ubl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1197010. Sumo1.

Subcellular locationi

Nucleus membrane. Nucleus speckle. Cytoplasm. NucleusPML body By similarity
Note: Recruited by BCL11A into the nuclear body.2 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB
  2. cytoplasm Source: UniProtKB-SubCell
  3. dendrite Source: Ensembl
  4. nuclear body Source: UniProtKB
  5. nuclear membrane Source: UniProtKB-SubCell
  6. nuclear speck Source: UniProtKB-SubCell
  7. nucleus Source: MGI
  8. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 9796Small ubiquitin-related modifier 1
PRO_0000035941Add
BLAST
Propeptidei98 – 1014 By similarity
PRO_0000035942

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine1 Publication
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Modified residuei9 – 91Phosphoserine By similarity
Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
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 By similarity.
Polymeric SUMO1 chains undergo polyubiquitination by RNF4 By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63166.
PaxDbiP63166.
PRIDEiP63166.

PTM databases

PhosphoSiteiP63166.

Expressioni

Tissue specificityi

Ubiquitous.

Developmental stagei

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.1 Publication

Inductioni

By hypoxia.1 Publication

Gene expression databases

BgeeiP63166.
CleanExiMM_SUMO1.
GenevestigatoriP63166.

Interactioni

Subunit structurei

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). Interacts with BHLHE40/DEC1 By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ikzf1Q032672EBI-80152,EBI-908572
PTPN1P180312EBI-80152,EBI-968788From a different organism.

Protein-protein interaction databases

BioGridi204420. 31 interactions.
DIPiDIP-29278N.
IntActiP63166. 7 interactions.
MINTiMINT-154756.

Structurei

3D structure databases

ProteinModelPortaliP63166.
SMRiP63166. Positions 1-101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9778Ubiquitin-like
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63166.
KOiK12160.
OMAiITDNHTP.
OrthoDBiEOG76X62R.
PhylomeDBiP63166.
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]

Sequencei

Sequence statusi: Complete.

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

P63166-1 [UniParc]FASTAAdd to Basket

« Hide

MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES    50
YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST 100
V 101
Length:101
Mass (Da):11,557
Last modified:September 27, 2004 - v1
Checksum:i89BE97D2D054FB33
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35586.1.
RefSeqiNP_033486.1. NM_009460.2.
UniGeneiMm.362118.

Genome annotation databases

EnsembliENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
GeneIDi22218.
KEGGimmu:22218.
UCSCiuc007bdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35586.1.
RefSeqi NP_033486.1. NM_009460.2.
UniGenei Mm.362118.

3D structure databases

ProteinModelPortali P63166.
SMRi P63166. Positions 1-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204420. 31 interactions.
DIPi DIP-29278N.
IntActi P63166. 7 interactions.
MINTi MINT-154756.

PTM databases

PhosphoSitei P63166.

Proteomic databases

MaxQBi P63166.
PaxDbi P63166.
PRIDEi P63166.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000091374 ; ENSMUSP00000088935 ; ENSMUSG00000026021 .
GeneIDi 22218.
KEGGi mmu:22218.
UCSCi uc007bdx.1. mouse.

Organism-specific databases

CTDi 7341.
MGIi MGI:1197010. Sumo1.

Phylogenomic databases

eggNOGi COG5227.
GeneTreei ENSGT00390000018808.
HOGENOMi HOG000207495.
HOVERGENi HBG053025.
InParanoidi P63166.
KOi K12160.
OMAi ITDNHTP.
OrthoDBi EOG76X62R.
PhylomeDBi P63166.
TreeFami TF315116.

Enzyme and pathway databases

Reactomei REACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_196649. SUMO is proteolytically processed.
REACT_198645. Regulation of IFNG signaling.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

NextBioi 28734.
PROi P63166.
SOURCEi Search...

Gene expression databases

Bgeei P63166.
CleanExi MM_SUMO1.
Genevestigatori P63166.

Family and domain databases

InterProi IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSUMO1_MOUSE
AccessioniPrimary (citable) accession number: P63166
Secondary accession number(s): P55856, Q3TX92, Q93068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: September 3, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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