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Q9Z172

- SUMO3_MOUSE

UniProt

Q9Z172 - SUMO3_MOUSE

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Protein

Small ubiquitin-related modifier 3

Gene
Sumo3, Smt3b, Smt3h1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. SUMO ligase activity Source: MGI

GO - Biological processi

  1. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
  2. protein localization to nucleus Source: MGI
  3. protein sumoylation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 3
Short name:
SUMO-3
Alternative name(s):
SMT3 homolog 1
Ubiquitin-like protein SMT3B
Short name:
Smt3B
Gene namesi
Name:Sumo3
Synonyms:Smt3b, Smt3h1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1336201. Sumo3.

Subcellular locationi

Cytoplasm By similarity. NucleusPML body 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nuclear body Source: MGI
  3. PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9292Small ubiquitin-related modifier 3PRO_0000035959Add
BLAST
Propeptidei93 – 11018 By similarityPRO_0000035960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki92 – 92Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Post-translational modificationi

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.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ9Z172.
PRIDEiQ9Z172.

PTM databases

PhosphoSiteiQ9Z172.

Expressioni

Gene expression databases

ArrayExpressiQ9Z172.
BgeeiQ9Z172.
CleanExiMM_SUMO3.
GenevestigatoriQ9Z172.

Interactioni

Subunit structurei

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/BMAL1.1 Publication

Protein-protein interaction databases

BioGridi203358. 6 interactions.
IntActiQ9Z172. 1 interaction.
MINTiMINT-4134935.

Structurei

3D structure databases

ProteinModelPortaliQ9Z172.
SMRiQ9Z172. Positions 14-88.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9278Ubiquitin-likeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiQ9Z172.
KOiK12160.
OrthoDBiEOG76X62R.
PhylomeDBiQ9Z172.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Z172-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ    50
GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGSASRGSVP 100
TPNRCPDLCY 110
Length:110
Mass (Da):12,430
Last modified:May 1, 1999 - v1
Checksum:i2950B8B1A3F88DC8
GO
Isoform 2 (identifier: Q9Z172-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MSEEKPK → MTTVLAQ

Note: No experimental confirmation available.

Show »
Length:110
Mass (Da):12,345
Checksum:iC7BD3DAAB055D5F2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 77MSEEKPK → MTTVLAQ in isoform 2. VSP_021948

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23958.1. [Q9Z172-1]
RefSeqiNP_064313.1. NM_019929.3. [Q9Z172-1]
XP_006513489.1. XM_006513426.1. [Q9Z172-2]
UniGeneiMm.24433.

Genome annotation databases

EnsembliENSMUST00000020501; ENSMUSP00000020501; ENSMUSG00000020265. [Q9Z172-1]
ENSMUST00000099538; ENSMUSP00000097136; ENSMUSG00000020265. [Q9Z172-2]
GeneIDi20610.
KEGGimmu:20610.
UCSCiuc007fvy.1. mouse. [Q9Z172-1]
uc007fvz.1. mouse. [Q9Z172-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23958.1. [Q9Z172-1 ]
RefSeqi NP_064313.1. NM_019929.3. [Q9Z172-1 ]
XP_006513489.1. XM_006513426.1. [Q9Z172-2 ]
UniGenei Mm.24433.

3D structure databases

ProteinModelPortali Q9Z172.
SMRi Q9Z172. Positions 14-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203358. 6 interactions.
IntActi Q9Z172. 1 interaction.
MINTi MINT-4134935.

PTM databases

PhosphoSitei Q9Z172.

Proteomic databases

PaxDbi Q9Z172.
PRIDEi Q9Z172.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020501 ; ENSMUSP00000020501 ; ENSMUSG00000020265 . [Q9Z172-1 ]
ENSMUST00000099538 ; ENSMUSP00000097136 ; ENSMUSG00000020265 . [Q9Z172-2 ]
GeneIDi 20610.
KEGGi mmu:20610.
UCSCi uc007fvy.1. mouse. [Q9Z172-1 ]
uc007fvz.1. mouse. [Q9Z172-2 ]

Organism-specific databases

CTDi 6612.
MGIi MGI:1336201. Sumo3.

Phylogenomic databases

eggNOGi COG5227.
GeneTreei ENSGT00390000018808.
HOGENOMi HOG000207495.
HOVERGENi HBG053025.
InParanoidi Q9Z172.
KOi K12160.
OrthoDBi EOG76X62R.
PhylomeDBi Q9Z172.
TreeFami TF315116.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi SUMO3. mouse.
NextBioi 298967.
PROi Q9Z172.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z172.
Bgeei Q9Z172.
CleanExi MM_SUMO3.
Genevestigatori Q9Z172.

Family and domain databases

InterProi IPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR10562:SF10. PTHR10562:SF10. 1 hit.
Pfami PF11976. Rad60-SLD. 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. "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.
    , 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.

Entry informationi

Entry nameiSUMO3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z172
Secondary accession number(s): Q14C17, Q3TBL9, Q3UDI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 101 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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