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Protein

Small ubiquitin-related modifier 1

Gene

Sumo1

Organism
Mus musculus (Mouse)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei36 – 361Interaction with PIAS2By similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. SUMO transferase activity Source: MGI
  3. transcription factor binding Source: AgBase
  4. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of DNA binding Source: MGI
  2. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  3. negative regulation of transcription, DNA-templated Source: MGI
  4. palate development Source: UniProtKB
  5. PML body organization Source: MGI
  6. positive regulation of calcium-transporting ATPase activity Source: BHF-UCL
  7. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  8. positive regulation of protein complex assembly Source: MGI
  9. protein localization to nuclear pore Source: MGI
  10. protein sumoylation Source: UniProtKB
  11. regulation of calcium ion transmembrane transport Source: BHF-UCL
  12. regulation of cardiac muscle cell contraction Source: BHF-UCL
  13. regulation of protein stability Source: BHF-UCL
  14. regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_289967. Regulation of IFNG signaling.
REACT_304803. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_304847. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_343238. SUMO is proteolytically processed.

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 Componenti: 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 9796Small ubiquitin-related modifier 1PRO_0000035941Add
BLAST
Propeptidei98 – 1014By similarityPRO_0000035942

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21Phosphoserine1 Publication
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
Modified residuei9 – 91PhosphoserineBy 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. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi204420. 33 interactions.
DIPiDIP-29278N.
IntActiP63166. 7 interactions.
MINTiMINT-154756.

Structurei

3D structure databases

ProteinModelPortaliP63166.
SMRiP63166. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

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.
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

        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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP63166.
SMRiP63166. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204420. 33 interactions.
DIPiDIP-29278N.
IntActiP63166. 7 interactions.
MINTiMINT-154756.

PTM databases

PhosphoSiteiP63166.

Proteomic databases

MaxQBiP63166.
PaxDbiP63166.
PRIDEiP63166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7341.
MGIiMGI:1197010. Sumo1.

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63166.
KOiK12160.
OMAiITDNHTP.
OrthoDBiEOG76X62R.
PhylomeDBiP63166.
TreeFamiTF315116.

Enzyme and pathway databases

ReactomeiREACT_289967. Regulation of IFNG signaling.
REACT_304803. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_304847. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_343238. SUMO is proteolytically processed.

Miscellaneous databases

NextBioi28734.
PROiP63166.
SOURCEiSearch...

Gene expression databases

BgeeiP63166.
CleanExiMM_SUMO1.
GenevestigatoriP63166.

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. "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(1997) [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(2004) [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(2003) [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(2003) [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(2005) [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(2007) [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(2008) [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: April 1, 2015
This is version 111 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

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.