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P61956 (SUMO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 2

Short name=SUMO-2
Alternative name(s):
HSMT3
SMT3 homolog 2
SUMO-3
Sentrin-2
Ubiquitin-like protein SMT3A
Short name=Smt3A
Gene names
Name:SUMO2
Synonyms:SMT3A, SMT3H2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length95 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 that can be covalently attached to proteins as a monomer or as 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 an E3 ligase 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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Ref.7 Ref.15 Ref.16

Subunit structure

Homotrimer Potential. Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Ref.11 Ref.14 Ref.15 Ref.20

Subcellular location

Nucleus. Note: Nuclear bodies. Ref.7 Ref.10

Tissue specificity

Broadly expressed. Ref.7

Post-translational modification

Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Caution

Frequently wrongly assigned as SMT3B in many databases and publications. However, according to initial nomenclature, SUMO2 corresponds to SMT3A (Ref.8).

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.16. Source: UniProtKB

protein sumoylation

Inferred from direct assay. Source: UniProtKB

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionubiquitin protein ligase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9393Small ubiquitin-related modifier 2
PRO_0000035949
Propeptide94 – 952
PRO_0000035950

Regions

Domain16 – 9580Ubiquitin-like

Amino acid modifications

Modified residue111N6-acetyllysine Ref.17
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.9 Ref.16 Ref.18
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-link93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Natural variations

Natural variant161D → N. Ref.6
Corresponds to variant rs17850328 [ dbSNP | Ensembl ].
VAR_047508

Experimental info

Mutagenesis111K → R: Abolishes the formation of poly(SUMO) chains. Ref.9
Sequence conflict551V → M in AAD45399. Ref.1
Sequence conflict551V → M in CAA67897. Ref.2
Sequence conflict551V → M in BAG34779. Ref.3
Sequence conflict551V → M in EAW89249. Ref.5
Sequence conflict551V → M in AAH08450. Ref.6
Sequence conflict551V → M in AAH16775. Ref.6
Sequence conflict551V → M in AAH22340. Ref.6
Sequence conflict551V → M in AAH62713. Ref.6
Sequence conflict551V → M in AAH68465. Ref.6
Sequence conflict551V → M in AAH70159. Ref.6
Sequence conflict551V → M in AAH71645. Ref.6
Sequence conflict551V → M in AAH71646. Ref.6
Sequence conflict551V → M in AAI07854. Ref.6

Secondary structure

............... 95
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61956 [UniParc].

Last modified February 8, 2011. Version 2.
Checksum: E49DF4AF49BEF08B

FASTA9510,839
        10         20         30         40         50         60 
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSVRQIRF 

        70         80         90 
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene."
Mannen H., Tseng H.M., Cho C.L., Li S.S.-L.
Biochem. Biophys. Res. Commun. 222:178-180(1996) [PubMed: 8630065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family."
Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C.
Genomics 40:362-367(1997) [PubMed: 9119407] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-16.
Tissue: Blood vessel, Bone, Bone marrow, Brain, Lung and Testis.
[7]"Characterization of a second member of the sentrin family of ubiquitin-like proteins."
Kamitani T., Kito K., Nguyen H.P., Fukuda-Kamitani T., Yeh E.T.H.
J. Biol. Chem. 273:11349-11353(1998) [PubMed: 9556629] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3."
Saitoh H., Hinchey J.
J. Biol. Chem. 275:6252-6258(2000) [PubMed: 10692421] [Abstract]
Cited for: IDENTIFICATION.
[9]"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
J. Biol. Chem. 276:35368-35374(2001) [PubMed: 11451954] [Abstract]
Cited for: SUMOYLATION AT LYS-11, MUTAGENESIS OF LYS-11.
[10]"Molecular features of human ubiquitin-like SUMO genes and their encoded proteins."
Su H.-L., Li S.S.-L.
Gene 296:65-73(2002) [PubMed: 12383504] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
Biochemistry 42:9959-9969(2003) [PubMed: 12924945] [Abstract]
Cited for: INTERACTION WITH UBE2I.
[12]"A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex."
Reverter D., Lima C.D.
Structure 12:1519-1531(2004) [PubMed: 15296745] [Abstract]
Cited for: CLEAVAGE.
[13]"Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
Xu Z., Au S.W.N.
Biochem. J. 386:325-330(2005) [PubMed: 15487983] [Abstract]
Cited for: CLEAVAGE.
[14]"NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression."
Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G.
Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed: 16567619] [Abstract]
Cited for: INTERACTION WITH PELP1.
[15]"Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25."
Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.
Mol. Cell 30:610-619(2008) [PubMed: 18538659] [Abstract]
Cited for: FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25.
[16]"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
Nat. Cell Biol. 10:538-546(2008) [PubMed: 18408734] [Abstract]
Cited for: FUNCTION, POLYUBIQUITINATION AT LYS-11 BY RNF4.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, MASS SPECTROMETRY.
[18]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed: 20388717] [Abstract]
Cited for: SUMOYLATION AT LYS-11.
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins."
Huang W.-C., Ko T.-P., Li S.S.-L., Wang A.H.-J.
Eur. J. Biochem. 271:4114-4122(2004) [PubMed: 15479240] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 9-93, SUBUNIT.
[21]"Solution structure of human SUMO-2 (SMT3B), a ubiquitin-like protein."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-93.
[22]"Crystal structure of SUMO-3-modified thymine-DNA glycosylase."
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
J. Mol. Biol. 359:137-147(2006) [PubMed: 16626738] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-93 CONJUGATED TO TDG.
[23]"Solution structure of human small ubiquitin-like modifier protein isoform 2 (SUMO-2)."
Chang C.K., Wang Y.H., Chung T.L., Chang C.F., Li S.S.L., Huang T.H.
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-95.
+Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L76416 mRNA. Translation: AAD45399.1.
X99585 mRNA. Translation: CAA67897.1.
AK311837 mRNA. Translation: BAG34779.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89249.1.
BC008450 mRNA. Translation: AAH08450.1.
BC016775 mRNA. Translation: AAH16775.1.
BC022340 mRNA. Translation: AAH22340.1.
BC062713 mRNA. Translation: AAH62713.1.
BC068465 mRNA. Translation: AAH68465.1.
BC070159 mRNA. Translation: AAH70159.1.
BC071645 mRNA. Translation: AAH71645.1.
BC071646 mRNA. Translation: AAH71646.1.
BC107853 mRNA. Translation: AAI07854.1.
IPIIPI00299149.
PIRJC4760.
RefSeqNP_001005849.1. NM_001005849.1.
NP_008868.3. NM_006937.3.
UniGeneHs.380973.
Hs.546298.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WM2X-ray1.60A12-89[»]
1WM3X-ray1.20A17-88[»]
1WZ0NMR-A1-91[»]
1Z5Qmodel-B15-93[»]
2AWTNMR-A1-95[»]
2CKHX-ray3.20B15-93[»]
2D07X-ray2.10B1-93[»]
2IO0X-ray2.30B15-95[»]
2IO3X-ray3.20B15-93[»]
2IYDX-ray3.20B15-95[»]
2RPQNMR-A1-93[»]
ProteinModelPortalP61956.
SMRP61956. Positions 1-95.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29253N.
IntActP61956. 36 interactions.
MINTMINT-1373938.
STRINGP61956.

PTM databases

PhosphoSiteP61956.

Polymorphism databases

DMDM48429130.

Proteomic databases

PRIDEP61956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000420826; ENSP00000405965; ENSG00000188612.
GeneID6613.
KEGGhsa:6613.
UCSCuc002jne.1. human.

Organism-specific databases

CTD6613.
GeneCardsGC17M073163.
H-InvDBHIX0014166.
HIX0056267.
HGNCHGNC:11125. SUMO2.
HPACAB037314.
MIM603042. gene.
neXtProtNX_P61956.
PharmGKBPA134914683.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20741.
GeneTreeENSGT00390000018808.
HOGENOMHBG436396.
HOVERGENHBG053025.
OMATETEHIN.
OrthoDBEOG46HGC8.
PhylomeDBP61956.

Gene expression databases

ArrayExpressP61956.
BgeeP61956.
CleanExHS_SUMO2.
GenevestigatorP61956.
GermOnlineENSG00000188612. Homo sapiens.

Family and domain databases

InterProIPR022617. SUMO.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
KOK12160.
PfamPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio25747.
PMAP-CutDBP61956.
SOURCESearch...

Entry information

Entry nameSUMO2_HUMAN
AccessionPrimary (citable) accession number: P61956
Secondary accession number(s): B2R4I2 expand/collapse secondary AC list , P55855, Q32Q42, Q6IPZ6, Q96HK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: February 8, 2011
Last modified: January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families