SUMO-activating enzyme subunit 2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9UBT2 (SAE2_HUMAN)

Last modified June 16, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    SUMO-activating enzyme subunit 2
    EC=6.3.2.-
Alternative name(s):
    Ubiquitin-like 1-activating enzyme E1B
    Anthracycline-associated resistance ARX

Gene names

Name:	UBA2
Synonyms:	SAE2, UBLE1B
ORF Names:	HRIHFB2115

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	The dimeric enzyme acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2. Ref.11 Ref.12 Ref.16
Pathway	Protein modification; protein sumoylation.
Subunit structure	Heterodimer of SAE1 and SAE2. The complex binds SUMO proteins via SAE2. Ref.11
Subcellular location	Nucleus. Ref.11
Sequence similarities	Belongs to the ubiquitin-activating E1 family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein modification process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme activator activity Ref.3 Traceable author statement. Source: ProtInc ligase activity Inferred from electronic annotation. Source: UniProtKB-KW small protein activating enzyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAE1	Q9UBE0	1	EBI-718569,EBI-743154
UBE2I	P63279	1	EBI-718569,EBI-80168

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 640

640

SUMO-activating enzyme subunit 2

PRO_0000194968

Regions

Nucleotide binding

27 – 51

ATP By similarity

Sites

Active site

173

Glycyl thioester intermediate Probable

Amino acid modifications

Modified residue

592

Phosphoserine Ref.14

Natural variations

Natural variant

307

L → R: dbSNP rs1043062. Ref.1 Ref.2

VAR_017689

Experimental info

Sequence conflict

229

S → C in AAD12784. Ref.1

Sequence conflict

229

S → C in AAD23914. Ref.2

Sequence conflict

341

E → G in CAB66839. Ref.5

Sequence conflict

456

V → L in BAD92109. Ref.9

Secondary structure

640

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9UBT2-1 [UniParc].

Last modified February 16, 2004. Version 2.
Checksum: C12D15293BBF90EB
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FASTA

640

71,224

        10         20         30         40         50         60 
MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ 

        70         80         90        100        110        120 
FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA 

       130        140        150        160        170        180 
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS 

       190        200        210        220        230        240 
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST 

       250        260        270        280        290        300 
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ 

       310        320        330        340        350        360 
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN 

       370        380        390        400        410        420 
LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK 

       430        440        450        460        470        480 
QPNPRKKLLV PCALDPPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV 

       490        500        510        520        530        540 
QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK 

       550        560        570        580        590        600 
DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN 

       610        620        630        640 
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9920803] [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: 10217437] [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: 10187858] [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]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] 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: 15489334] [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: 9853615] [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: 11481243] [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: 11451954] [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: 16620772] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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: 15660128] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SAE1 AND ATP, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1 AND ATP, FUNCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

IPI

IPI00023234.

PIR

T46936.

RefSeq

NP_005490.1.

UniGene

Hs.631580

3D structure databases

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	[»]

DisProt

DP00486.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UBT2. 8 interactions.

PTM databases

PhosphoSite

Q9UBT2.

Proteomic databases

PeptideAtlas

Q9UBT2.

PRIDE

Q9UBT2.

Genome annotation databases

Ensembl

ENSG00000126261. Homo sapiens. [Contig view]

GeneID

10054.

KEGG

hsa:10054.

Organism-specific databases

GeneCards

GC19P039611.

H-InvDB

HIX0015011.

HGNC

HGNC:30661. UBA2.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UBT2.

OMA

Q9UBT2. WEPMEAE.

Gene expression databases

ArrayExpress

Q9UBT2.

Bgee

Q9UBT2.

CleanEx

HS_UBA2.

GermOnline

ENSG00000126261. Homo sapiens.

Family and domain databases

InterPro

IPR000594. ThiF_NAD_FAD_bd.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]

Pfam

PF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]

PROSITE

PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

37985.

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Entry information

Entry name

SAE2_HUMAN

Accession

Primary (citable) accession number: Q9UBT2
Secondary accession number(s): O95605

Q9UED2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	February 16, 2004
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 19

Human chromosome 19: 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents