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P61956

- SUMO2_HUMAN

UniProt

P61956 - SUMO2_HUMAN

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Protein
Small ubiquitin-related modifier 2
Gene
SUMO2, SMT3A, SMT3H2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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.3 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. post-translational protein modification Source: Reactome
  4. protein sumoylation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163725. SUMO is proteolytically processed.
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SUMO2
Synonyms:SMT3A, SMT3H2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11125. SUMO2.

Subcellular locationi

Nucleus. NucleusPML body 3 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111K → R: Abolishes the formation of poly(SUMO) chains. 1 Publication

Organism-specific databases

PharmGKBiPA134914683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Small ubiquitin-related modifier 2
PRO_0000035949Add
BLAST
Propeptidei94 – 952
PRO_0000035950

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei11 – 111N6-acetyllysine; alternate By similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-linki93 – 93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

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.
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61956.
PaxDbiP61956.
PRIDEiP61956.

PTM databases

PhosphoSiteiP61956.

Miscellaneous databases

PMAP-CutDBP61956.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

ArrayExpressiP61956.
BgeeiP61956.
CleanExiHS_SUMO2.
GenevestigatoriP61956.

Organism-specific databases

HPAiCAB037314.

Interactioni

Subunit structurei

Homotrimer Reviewed prediction. 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. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHD3Q128733EBI-473220,EBI-523590
MYBP102423EBI-473220,EBI-298355
PELP1Q8IZL84EBI-473220,EBI-716449
PIAS4Q8N2W93EBI-473220,EBI-473160
Rnf4O888462EBI-473220,EBI-7258907From a different organism.
TANKQ928443EBI-473220,EBI-356349
UBE2IP632796EBI-473220,EBI-80168
USPL1Q5W0Q72EBI-473220,EBI-2513899
uspl1Q6DRC52EBI-473220,EBI-8018150From a different organism.

Protein-protein interaction databases

BioGridi112497. 1259 interactions.
DIPiDIP-29253N.
IntActiP61956. 51 interactions.
MINTiMINT-1373938.
STRINGi9606.ENSP00000405965.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Turni14 – 163
Beta strandi18 – 236
Turni25 – 273
Beta strandi29 – 346
Helixi41 – 5111
Turni55 – 573
Beta strandi59 – 624
Beta strandi65 – 673
Turni73 – 775
Beta strandi82 – 876
Beta strandi90 – 934

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3UINX-ray2.60B14-93[»]
3UIOX-ray2.60B14-93[»]
3ZO5X-ray2.15B16-95[»]
4BKGX-ray2.11A12-93[»]
ProteinModelPortaliP61956.
SMRiP61956. Positions 1-95.

Miscellaneous databases

EvolutionaryTraceiP61956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9580Ubiquitin-like
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5227.
HOVERGENiHBG053025.
KOiK12160.
OMAiQQTGGHC.
PhylomeDBiP61956.
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: P61956-1) [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

MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER   50
QGLSMRQIRF RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY 95
Length:95
Mass (Da):10,871
Last modified:February 22, 2012 - v3
Checksum:iF8F0426849BEF08B
GO
Isoform 2 (identifier: P61956-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-74: Missing.

Show »
Length:71
Mass (Da):8,111
Checksum:i96014B2763D7E899
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161D → N.1 Publication
Corresponds to variant rs17850328 [ dbSNP | Ensembl ].
VAR_047508

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei51 – 7424Missing in isoform 2.
VSP_042351Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BF978876 mRNA. No translation available.
CCDSiCCDS45773.1. [P61956-2]
CCDS45774.1. [P61956-1]
PIRiJC4760.
RefSeqiNP_001005849.1. NM_001005849.1. [P61956-2]
NP_008868.3. NM_006937.3. [P61956-1]
UniGeneiHs.380973.
Hs.546298.

Genome annotation databases

EnsembliENST00000314523; ENSP00000400886; ENSG00000188612. [P61956-2]
ENST00000420826; ENSP00000405965; ENSG00000188612. [P61956-1]
GeneIDi6613.
KEGGihsa:6613.
UCSCiuc002jne.3. human. [P61956-1]
uc002jnf.3. human. [P61956-2]

Polymorphism databases

DMDMi378405233.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
BF978876 mRNA. No translation available.
CCDSi CCDS45773.1. [P61956-2 ]
CCDS45774.1. [P61956-1 ]
PIRi JC4760.
RefSeqi NP_001005849.1. NM_001005849.1. [P61956-2 ]
NP_008868.3. NM_006937.3. [P61956-1 ]
UniGenei Hs.380973.
Hs.546298.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WM2 X-ray 1.60 A 12-89 [» ]
1WM3 X-ray 1.20 A 17-88 [» ]
1WZ0 NMR - A 1-91 [» ]
1Z5Q model - B 15-93 [» ]
2AWT NMR - A 1-95 [» ]
2CKH X-ray 3.20 B 15-93 [» ]
2D07 X-ray 2.10 B 1-93 [» ]
2IO0 X-ray 2.30 B 15-95 [» ]
2IO3 X-ray 3.20 B 15-93 [» ]
2IYD X-ray 3.20 B 15-95 [» ]
2RPQ NMR - A 1-93 [» ]
3UIN X-ray 2.60 B 14-93 [» ]
3UIO X-ray 2.60 B 14-93 [» ]
3ZO5 X-ray 2.15 B 16-95 [» ]
4BKG X-ray 2.11 A 12-93 [» ]
ProteinModelPortali P61956.
SMRi P61956. Positions 1-95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112497. 1259 interactions.
DIPi DIP-29253N.
IntActi P61956. 51 interactions.
MINTi MINT-1373938.
STRINGi 9606.ENSP00000405965.

Chemistry

ChEMBLi CHEMBL2146301.

PTM databases

PhosphoSitei P61956.

Polymorphism databases

DMDMi 378405233.

Proteomic databases

MaxQBi P61956.
PaxDbi P61956.
PRIDEi P61956.

Protocols and materials databases

DNASUi 6613.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314523 ; ENSP00000400886 ; ENSG00000188612 . [P61956-2 ]
ENST00000420826 ; ENSP00000405965 ; ENSG00000188612 . [P61956-1 ]
GeneIDi 6613.
KEGGi hsa:6613.
UCSCi uc002jne.3. human. [P61956-1 ]
uc002jnf.3. human. [P61956-2 ]

Organism-specific databases

CTDi 6613.
GeneCardsi GC17M073163.
H-InvDB HIX0056267.
HGNCi HGNC:11125. SUMO2.
HPAi CAB037314.
MIMi 603042. gene.
neXtProti NX_P61956.
PharmGKBi PA134914683.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5227.
HOVERGENi HBG053025.
KOi K12160.
OMAi QQTGGHC.
PhylomeDBi P61956.
TreeFami TF315116.

Enzyme and pathway databases

Reactomei REACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163725. SUMO is proteolytically processed.
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

Miscellaneous databases

EvolutionaryTracei P61956.
GeneWikii SUMO2.
GenomeRNAii 6613.
NextBioi 25747.
PMAP-CutDB P61956.
PROi P61956.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61956.
Bgeei P61956.
CleanExi HS_SUMO2.
Genevestigatori P61956.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASN-16.
    Tissue: Blood vessel, Bone, Bone marrow, Brain, Lung, Skin 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POLYUBIQUITINATION AT LYS-11 BY RNF4.
  17. "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] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-11.
    Tissue: Cervix carcinoma.
  18. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
    Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
    Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  19. "PolySUMO-binding proteins identified through a string search."
    Sun H., Hunter T.
    J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SIMC1; CASP8AP2; RNF111 AND SOBP.
  20. "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
    Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
    Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT MET-1.
  21. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 9-93, SUBUNIT.
  22. "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.
  23. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-93 CONJUGATED TO TDG.
  24. "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.

Entry informationi

Entry nameiSUMO2_HUMAN
AccessioniPrimary (citable) accession number: P61956
Secondary accession number(s): B2R4I2
, P55855, Q32Q42, Q6IPZ6, Q96HK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: February 22, 2012
Last modified: September 3, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Frequently wrongly assigned as SMT3B in many databases and publications. However, according to initial nomenclature, SUMO2 corresponds to SMT3A (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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