P63166 (SUMO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Sumo1
Synonyms:	Smt3c, Smt3h3, Ubl1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Nucleus › PML 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 process	Stress response Ubl conjugation pathway
Cellular component	Cytoplasm Membrane Nucleus
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	PML body organization Inferred from mutant phenotype PubMed 19033381. Source: MGI negative regulation of DNA binding Inferred from electronic annotation. Source: Compara negative regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara palate development Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of protein complex assembly Inferred from electronic annotation. Source: Compara 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-dependent Inferred from direct assay Ref.5. Source: MGI response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from electronic annotation. Source: Compara nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: Compara
Molecular_function	SUMO ligase activity Inferred from direct assay PubMed 15122901Ref.5PubMed 18644859. Source: MGI ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hif1a	Q61221	6	EBI-80152,EBI-298954
Ikzf1	Q03267	2	EBI-80152,EBI-908572
PTPN1	P18031	2	EBI-80152,EBI-968788	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 97	96	Small ubiquitin-related modifier 1		PRO_0000035941
	Propeptide	98 – 101	4	By similarity		PRO_0000035942
Regions
	Domain	20 – 97	78	Ubiquitin-like
Sites
	Site	36	1	Interaction with PIAS2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	2	1	Phosphoserine Ref.8 Ref.9
	Modified residue	9	1	Phosphoserine By similarity
	Cross-link	7		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
	Cross-link	25		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
	Cross-link	97		Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Sequences

	Sequence		Length	Mass (Da)
	P63166 [UniParc]. Last modified September 27, 2004. Version 1. Checksum: 89BE97D2D054FB33	FASTA	101	11,557
	10 20 30 40 50 60 MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 70 80 90 100 SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V

References

	« Hide 'large scale' referencesShow '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. , 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"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, MASS SPECTROMETRY. 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.
IPI	IPI00124593.
RefSeq	NP_033486.1. NM_009460.2.
UniGene	Mm.362118.
3D structure databases
ProteinModelPortal	P63166.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29278N.
IntAct	P63166. 6 interactions.
MINT	MINT-154756.
PTM databases
PhosphoSite	P63166.
Proteomic databases
PaxDb	P63166.
PRIDE	P63166.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
GeneID	22218.
KEGG	mmu:22218.
UCSC	uc007bdx.1. mouse.
Organism-specific databases
CTD	7341.
MGI	MGI:1197010. Sumo1.
Phylogenomic databases
eggNOG	COG5227.
GeneTree	ENSGT00390000018808.
HOGENOM	HOG000207495.
HOVERGEN	HBG053025.
InParanoid	P63166.
KO	K12160.
OMA	FFQEAKP.
OrthoDB	EOG42JNSX.
Gene expression databases
Bgee	P63166.
CleanEx	MM_SUMO1.
Genevestigator	P63166.
GermOnline	ENSMUSG00000026021. Mus musculus.
Family and domain databases
InterPro	IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF00240. ubiquitin. 1 hit. [Graphical view]
SMART	SM00213. UBQ. 1 hit. [Graphical view]
PROSITE	PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	28734.
SOURCE	Search...

Entry information

Entry name

SUMO1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program