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Q9UBT2

- SAE2_HUMAN

UniProt

Q9UBT2 - SAE2_HUMAN

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Protein

SUMO-activating enzyme subunit 2

Gene
UBA2, SAE2, UBLE1B, HRIHFB2115
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.6 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481ATP
Binding sitei72 – 721ATP
Metal bindingi158 – 1581Zinc
Metal bindingi161 – 1611Zinc
Active sitei173 – 1731Glycyl thioester intermediate2 Publications
Metal bindingi441 – 4411Zinc
Metal bindingi444 – 4441Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 296ATP
Nucleotide bindingi56 – 594ATP
Nucleotide bindingi95 – 962ATP
Nucleotide bindingi117 – 1226ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme activator activity Source: ProtInc
  3. ligase activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: IntAct
  6. protein heterodimerization activity Source: UniProtKB
  7. SUMO activating enzyme activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. positive regulation of catalytic activity Source: GOC
  3. post-translational protein modification Source: Reactome
  4. protein sumoylation Source: UniProtKB
  5. SMT3-dependent protein catabolic process Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-activating enzyme subunit 2 (EC:6.3.2.-)
Alternative name(s):
Anthracycline-associated resistance ARX
Ubiquitin-like 1-activating enzyme E1B
Ubiquitin-like modifier-activating enzyme 2
Gene namesi
Name:UBA2
Synonyms:SAE2, UBLE1B
ORF Names:HRIHFB2115
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:30661. UBA2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.2 Publications

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. nucleoplasm Source: Reactome
  3. SUMO activating enzyme complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561N → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
Mutagenesisi57 – 571L → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication
Mutagenesisi59 – 591R → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication
Mutagenesisi72 – 721K → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
Mutagenesisi117 – 1171D → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
Mutagenesisi173 – 1731C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi174 – 1741T → A: Slightly reduced enzyme activity. 1 Publication
Mutagenesisi184 – 1841H → Q: No effect on enzyme activity. 1 Publication
Mutagenesisi235 – 2351I → A: Strongly reduced interaction with UBE2I; when associated with A-238. 1 Publication
Mutagenesisi238 – 2381I → A: Strongly reduced interaction with UBE2I; when associated with A-235. 1 Publication
Mutagenesisi484 – 4841Missing: Strongly reduced interaction with UBE2I. 1 Publication
Mutagenesisi485 – 4851G → GGGG: Strongly reduced interaction with UBE2I. 1 Publication

Organism-specific databases

PharmGKBiPA162407583.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640SUMO-activating enzyme subunit 2PRO_0000194968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei271 – 2711N6-acetyllysine; alternate1 Publication
Cross-linki271 – 271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei507 – 5071Phosphoserine1 Publication
Modified residuei592 – 5921Phosphoserine1 Publication
Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei613 – 6131N6-acetyllysine; alternate By similarity
Cross-linki613 – 613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki617 – 617Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki623 – 623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UBT2.
PaxDbiQ9UBT2.
PeptideAtlasiQ9UBT2.
PRIDEiQ9UBT2.

PTM databases

PhosphoSiteiQ9UBT2.

Expressioni

Gene expression databases

ArrayExpressiQ9UBT2.
BgeeiQ9UBT2.
CleanExiHS_UBA2.
GenevestigatoriQ9UBT2.

Organism-specific databases

HPAiHPA041436.

Interactioni

Subunit structurei

Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SAE1Q9UBE03EBI-718569,EBI-743154

Protein-protein interaction databases

BioGridi115365. 61 interactions.
DIPiDIP-35136N.
IntActiQ9UBT2. 5 interactions.
MINTiMINT-1405216.
STRINGi9606.ENSP00000246548.

Structurei

Secondary structure

1
640
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179
Beta strandi19 – 235
Helixi27 – 3913
Beta strandi43 – 486
Helixi54 – 585
Helixi65 – 673
Helixi72 – 8110
Beta strandi88 – 947
Helixi103 – 1064
Beta strandi110 – 1145
Helixi119 – 13214
Beta strandi136 – 1427
Beta strandi145 – 1517
Turni153 – 1553
Beta strandi168 – 1714
Turni172 – 1765
Helixi182 – 19716
Helixi202 – 2043
Helixi213 – 2153
Beta strandi225 – 2273
Beta strandi234 – 2363
Helixi241 – 2466
Helixi251 – 2599
Helixi261 – 2666
Helixi270 – 2723
Beta strandi274 – 2763
Helixi284 – 2896
Helixi308 – 3103
Helixi315 – 33521
Turni337 – 3393
Helixi349 – 36517
Helixi373 – 3819
Helixi388 – 40619
Helixi410 – 4123
Beta strandi414 – 4185
Beta strandi426 – 4338
Turni442 – 4443
Beta strandi445 – 4473
Beta strandi449 – 4546
Turni456 – 4583
Helixi461 – 4666
Helixi467 – 4726
Beta strandi479 – 4868
Beta strandi489 – 4913
Beta strandi493 – 4986
Helixi501 – 5033
Helixi506 – 5094
Beta strandi516 – 5216
Turni522 – 5254
Beta strandi526 – 5349
Beta strandi544 – 5463
Turni609 – 6113
Turni614 – 6196
Helixi620 – 6267
Helixi627 – 6293
Beta strandi636 – 6383

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25B/D1-640[»]
1Y8RX-ray2.75B/E1-640[»]
2PX9NMR-A166-382[»]
3KYCX-ray2.45B1-640[»]
3KYDX-ray2.61B1-549[»]
DisProtiDP00486.
ProteinModelPortaliQ9UBT2.
SMRiQ9UBT2. Positions 4-591, 607-640.

Miscellaneous databases

EvolutionaryTraceiQ9UBT2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000216514.
HOVERGENiHBG060266.
InParanoidiQ9UBT2.
KOiK10685.
OMAiYACLFSK.
OrthoDBiEOG7S7SDB.
PhylomeDBiQ9UBT2.
TreeFamiTF300765.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UBT2-1 [UniParc]FASTAAdd to Basket

« Hide

MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD    50
TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD 100
YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT 150
IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE 200
DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST KEWAKSTGYD 250
PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ 300
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS 350
AMDFVTSAAN LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL 400
EGLKILSGKI DQCRTIFLNK QPNPRKKLLV PCALDPPNPN CYVCASKPEV 450
TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV QIEDGKGTIL ISSEEGETEA 500
NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK DVEFEVVGDA 550
PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN 600
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD 640
Length:640
Mass (Da):71,224
Last modified:February 16, 2004 - v2
Checksum:iC12D15293BBF90EB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti307 – 3071L → R.2 Publications
Corresponds to variant rs1043062 [ dbSNP | Ensembl ].
VAR_017689

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291S → C in AAD12784. 1 Publication
Sequence conflicti229 – 2291S → C in AAD23914. 1 Publication
Sequence conflicti341 – 3411E → G in CAB66839. 1 Publication
Sequence conflicti456 – 4561V → L in BAD92109. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090384 mRNA. Translation: AAD12784.1.
AF079566 mRNA. Translation: AAD23914.1.
AF110957 mRNA. Translation: AAD24434.1.
U35832 mRNA. Translation: AAC99992.1.
AL136905 mRNA. Translation: CAB66839.1.
BT009781 mRNA. Translation: AAP88783.1.
CR456756 mRNA. Translation: CAG33037.1.
BC003153 mRNA. Translation: AAH03153.1.
AB208872 mRNA. Translation: BAD92109.1.
AB015337 mRNA. Translation: BAA34795.1.
CCDSiCCDS12439.1.
PIRiT46936.
RefSeqiNP_005490.1. NM_005499.2.
UniGeneiHs.631580.

Genome annotation databases

EnsembliENST00000246548; ENSP00000246548; ENSG00000126261.
GeneIDi10054.
KEGGihsa:10054.
UCSCiuc002nvk.3. human.

Polymorphism databases

DMDMi42559898.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090384 mRNA. Translation: AAD12784.1 .
AF079566 mRNA. Translation: AAD23914.1 .
AF110957 mRNA. Translation: AAD24434.1 .
U35832 mRNA. Translation: AAC99992.1 .
AL136905 mRNA. Translation: CAB66839.1 .
BT009781 mRNA. Translation: AAP88783.1 .
CR456756 mRNA. Translation: CAG33037.1 .
BC003153 mRNA. Translation: AAH03153.1 .
AB208872 mRNA. Translation: BAD92109.1 .
AB015337 mRNA. Translation: BAA34795.1 .
CCDSi CCDS12439.1.
PIRi T46936.
RefSeqi NP_005490.1. NM_005499.2.
UniGenei Hs.631580.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y8Q X-ray 2.25 B/D 1-640 [» ]
1Y8R X-ray 2.75 B/E 1-640 [» ]
2PX9 NMR - A 166-382 [» ]
3KYC X-ray 2.45 B 1-640 [» ]
3KYD X-ray 2.61 B 1-549 [» ]
DisProti DP00486.
ProteinModelPortali Q9UBT2.
SMRi Q9UBT2. Positions 4-591, 607-640.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115365. 61 interactions.
DIPi DIP-35136N.
IntActi Q9UBT2. 5 interactions.
MINTi MINT-1405216.
STRINGi 9606.ENSP00000246548.

Chemistry

ChEMBLi CHEMBL2095174.

PTM databases

PhosphoSitei Q9UBT2.

Polymorphism databases

DMDMi 42559898.

Proteomic databases

MaxQBi Q9UBT2.
PaxDbi Q9UBT2.
PeptideAtlasi Q9UBT2.
PRIDEi Q9UBT2.

Protocols and materials databases

DNASUi 10054.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000246548 ; ENSP00000246548 ; ENSG00000126261 .
GeneIDi 10054.
KEGGi hsa:10054.
UCSCi uc002nvk.3. human.

Organism-specific databases

CTDi 10054.
GeneCardsi GC19P034919.
HGNCi HGNC:30661. UBA2.
HPAi HPA041436.
MIMi 613295. gene.
neXtProti NX_Q9UBT2.
PharmGKBi PA162407583.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0476.
HOGENOMi HOG000216514.
HOVERGENi HBG060266.
InParanoidi Q9UBT2.
KOi K10685.
OMAi YACLFSK.
OrthoDBi EOG7S7SDB.
PhylomeDBi Q9UBT2.
TreeFami TF300765.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

Miscellaneous databases

ChiTaRSi UBA2. human.
EvolutionaryTracei Q9UBT2.
GeneWikii UBA2.
GenomeRNAii 10054.
NextBioi 37985.
PROi Q9UBT2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBT2.
Bgeei Q9UBT2.
CleanExi HS_UBA2.
Genevestigatori Q9UBT2.

Family and domain databases

Gene3Di 1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view ]
Pfami PF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 2 hits.
PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2."
    Okuma T., Honda R., Ichikawa G., Tsumagari N., Yasuda H.
    Biochem. Biophys. Res. Commun. 254:693-698(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-307.
    Tissue: Cervix carcinoma.
  2. "Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex."
    Gong L., Li B., Millas S., Yeh E.T.H.
    FEBS Lett. 448:185-189(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-307.
    Tissue: Placenta.
  3. "Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1."
    Desterro J.M.P., Rodriguez M.S., Kemp G.D., Hay R.T.
    J. Biol. Chem. 274:10618-10624(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Slapak C., Mizunuma N., Terashima M., Yamauchi T., Kufe D.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "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].
    Tissue: Skin.
  9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-640.
    Tissue: Brain.
  10. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-640.
    Tissue: Fetal brain.
  11. "Expression and regulation of the mammalian SUMO-1 E1 enzyme."
    Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
    FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DIMERIZATION, FUNCTION.
  12. "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: FUNCTION.
  13. "A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
    Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
    Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications."
    Wang J., Lee B., Cai S., Fukui L., Hu W., Chen Y.
    J. Biol. Chem. 284:20340-20348(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2I, FUNCTION, MUTAGENESIS OF ASP-484 AND GLY-485.
  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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity."
    Truong K., Lee T.D., Chen Y.
    J. Biol. Chem. 287:15154-15163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-190; LYS-236; LYS-257; LYS-271 AND LYS-275.
  21. "Sumoylation of SAE2 C terminus regulates SAE nuclear localization."
    Truong K., Lee T.D., Li B., Chen Y.
    J. Biol. Chem. 287:42611-42619(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-611; LYS-613; LYS-617 AND LYS-623.
  22. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
    Lois L.M., Lima C.D.
    EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1; ZINC IONS AND ATP, FUNCTION, SUBUNIT, ACTIVE SITE.
  23. "The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications."
    Wang J., Hu W., Cai S., Lee B., Song J., Chen Y.
    Mol. Cell 27:228-237(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 166-382 IN COMPLEX WITH UBE2I, MUTAGENESIS OF ILE-235 AND ILE-238, FUNCTION, INTERACTION WITH UBE2I.
  24. "Active site remodelling accompanies thioester bond formation in the SUMO E1."
    Olsen S.K., Capili A.D., Lu X., Tan D.S., Lima C.D.
    Nature 463:906-912(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1 AND REACTION INTERMEDIATE, FUNCTION, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF ASN-56; LEU-57; ARG-59; LYS-72; ASP-117; CYS-173; THR-174 AND HIS-184.

Entry informationi

Entry nameiSAE2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBT2
Secondary accession number(s): O95605
, Q59H87, Q6IBP6, Q9NTJ1, Q9UED2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: September 3, 2014
This is version 129 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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