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Q9Z172 (SUMO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 3

Short name=SUMO-3
Alternative name(s):
SMT3 homolog 1
Ubiquitin-like protein SMT3B
Short name=Smt3B
Gene names
Name:Sumo3
Synonyms:Smt3b, Smt3h1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length110 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 which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 By similarity.

Subunit structure

Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with USP25 (via ts SIM domain); the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity By similarity. Interacts with ARNTL/BMAL1. Ref.4

Subcellular location

Cytoplasm By similarity. NucleusPML body Ref.4.

Post-translational modification

Polymeric chains can be formed through Lys-11 cross-linking By similarity.

Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function By similarity.

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z172-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Z172-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MSEEKPK → MTTVLAQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9292Small ubiquitin-related modifier 3
PRO_0000035959
Propeptide93 – 11018 By similarity
PRO_0000035960

Regions

Domain15 – 9278Ubiquitin-like

Amino acid modifications

Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link92Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Natural variations

Alternative sequence1 – 77MSEEKPK → MTTVLAQ in isoform 2.
VSP_021948

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 2950B8B1A3F88DC8

FASTA11012,430
        10         20         30         40         50         60 
MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR 

        70         80         90        100        110 
FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGSASRGSVP TPNRCPDLCY 

« Hide

Isoform 2 [UniParc].

Checksum: C7BD3DAAB055D5F2
Show »

FASTA11012,345

References

« Hide 'large scale' references
[1]"Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes."
Chen A., Mannen H., Li S.S.-L.
Biochem. Mol. Biol. Int. 46:1161-1174(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Bone marrow, Embryo, Kidney, Muellerian duct and Small intestine.
[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] (ISOFORM 1).
[4]"Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex."
Lee J., Lee Y., Lee M.J., Park E., Kang S.H., Chung C.H., Lee K.H., Kim K.
Mol. Cell. Biol. 28:6056-6065(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ARNTL/BMAL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF063847 mRNA. Translation: AAC99333.1.
AK012742 mRNA. Translation: BAB28442.1.
AK013019 mRNA. Translation: BAB28601.1.
AK148306 mRNA. Translation: BAE28469.1.
AK150063 mRNA. Translation: BAE29276.1.
AK150200 mRNA. Translation: BAE29374.1.
AK160169 mRNA. Translation: BAE35670.1.
AK162035 mRNA. Translation: BAE36692.1.
AK167207 mRNA. Translation: BAE39334.1.
AK168988 mRNA. Translation: BAE40788.1.
AK171169 mRNA. Translation: BAE42290.1.
AK170896 mRNA. Translation: BAE42100.1.
BC115488 mRNA. Translation: AAI15489.1.
BC115489 mRNA. Translation: AAI15490.1.
CCDSCCDS23958.1. [Q9Z172-1]
RefSeqNP_064313.1. NM_019929.3. [Q9Z172-1]
XP_006513489.1. XM_006513426.1. [Q9Z172-2]
UniGeneMm.24433.

3D structure databases

ProteinModelPortalQ9Z172.
SMRQ9Z172. Positions 14-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203358. 6 interactions.
IntActQ9Z172. 1 interaction.
MINTMINT-4134935.

PTM databases

PhosphoSiteQ9Z172.

Proteomic databases

PaxDbQ9Z172.
PRIDEQ9Z172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020501; ENSMUSP00000020501; ENSMUSG00000020265. [Q9Z172-1]
ENSMUST00000099538; ENSMUSP00000097136; ENSMUSG00000020265. [Q9Z172-2]
GeneID20610.
KEGGmmu:20610.
UCSCuc007fvy.1. mouse. [Q9Z172-1]
uc007fvz.1. mouse. [Q9Z172-2]

Organism-specific databases

CTD6612.
MGIMGI:1336201. Sumo3.

Phylogenomic databases

eggNOGCOG5227.
GeneTreeENSGT00390000018808.
HOGENOMHOG000207495.
HOVERGENHBG053025.
InParanoidQ9Z172.
KOK12160.
OrthoDBEOG76X62R.
PhylomeDBQ9Z172.
TreeFamTF315116.

Gene expression databases

ArrayExpressQ9Z172.
BgeeQ9Z172.
CleanExMM_SUMO3.
GenevestigatorQ9Z172.

Family and domain databases

InterProIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUMO3. mouse.
NextBio298967.
PROQ9Z172.
SOURCESearch...

Entry information

Entry nameSUMO3_MOUSE
AccessionPrimary (citable) accession number: Q9Z172
Secondary accession number(s): Q14C17, Q3TBL9, Q3UDI5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 100 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