SUMO-activating enzyme subunit 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9UBE0 (SAE1_HUMAN)

Last modified June 16, 2009. Version 77. History...

Clusters with 100%, 90%, 50% identity |

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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 1
Alternative name(s):
Ubiquitin-like 1-activating enzyme E1A

Gene names

Name:	SAE1
Synonyms:	AOS1, SUA1, UBLE1A

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	346 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.1 Ref.2 Ref.3 Ref.7 Ref.8 Ref.12
Pathway	Protein modification; protein sumoylation.
Subunit structure	Heterodimer of SAE1 and SAE2. The complex binds SUMO proteins via SAE2. Ref.1 Ref.2 Ref.3 Ref.7
Subcellular location	Nucleus. Ref.7
Tissue specificity	Expression level increases during S phase and drops in G2 phase (at protein level). Ref.7
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10
Sequence similarities	Belongs to the ubiquitin-activating E1 family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Ref.3 Traceable author statement. Source: UniProtKB
Cellular component	nucleus Ref.3 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP-dependent protein binding Ref.3 Inferred from direct assay. Source: UniProtKB enzyme activator activity Ref.1 Traceable author statement. Source: ProtInc ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Ref.3 Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Ref.3 Traceable author statement. Source: UniProtKB ubiquitin activating enzyme activity Ref.3 Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CYP1B1	Q16678	1	EBI-743154,EBI-1055133
FKBP4	Q02790	1	EBI-743154,EBI-1047444
SUMO3	P55854	1	EBI-743154,EBI-474067
UBA2	Q9UBT2	1	EBI-743154,EBI-718569
UBE2I	P63279	1	EBI-743154,EBI-80168

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 346

346

SUMO-activating enzyme subunit 1

PRO_0000194966

Amino acid modifications

Modified residue

185

Phosphoserine Ref.10

Experimental info

Sequence conflict

158

V → A in AAF29104. Ref.4

Sequence conflict

178 – 180

KTK → ETD in AAF29104. Ref.4

Sequence conflict

186

Q → H in AAF29104. Ref.4

Sequence conflict

273

R → G in AAD12785. Ref.1

Secondary structure

346

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9UBE0-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E2B10A69FF2ED746
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FASTA

346

38,450

        10         20         30         40         50         60 
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE IAKNLILAGV 

        70         80         90        100        110        120 
KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ NLNPMVDVKV DTEDIEKKPE 

       130        140        150        160        170        180 
SFFTQFDAVC LTCCSRDVIV KVDQICHKNS IKFFTGDVFG YHGYTFANLG EHEFVEEKTK 

       190        200        210        220        230        240 
VAKVSQGVED GPDTKRAKLD SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY 

       250        260        270        280        290        300 
FLLQVLLKFR TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA 

       310        320        330        340 
PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK

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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], DIMERIZATION, FUNCTION. 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], DIMERIZATION, FUNCTION. 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], PROTEIN SEQUENCE OF 1-11; 109-117 AND 186-193, DIMERIZATION, FUNCTION. Tissue: Cervix carcinoma.
[4]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[5]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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]. Tissue: Colon, Lung and Placenta.
[7]	"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, TISSUE SPECIFICITY, DIMERIZATION, FUNCTION.
[8]	"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.
[9]	"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.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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 SAE2 AND ATP, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAE2; SUMO1 AND ATP, FUNCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF090385 mRNA. Translation: AAD12785.2.
AF046025 mRNA. Translation: AAD23902.2.
AF110956 mRNA. Translation: AAD24433.1.
AF161489 mRNA. Translation: AAF29104.1.
BT007290 mRNA. Translation: AAP35954.1.
BC000344 mRNA. Translation: AAH00344.1.
BC003611 mRNA. Translation: AAH03611.1.
BC018271 mRNA. Translation: AAH18271.1.

IPI

IPI00033130.

RefSeq

NP_005491.1.
NP_057486.1.

UniGene

Hs.515500

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y8Q	X-ray	2.25	A/C	1-346	[»]
1Y8R	X-ray	2.75	A/D	1-346	[»]

DisProt

DP00485.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UBE0. 12 interactions.

PTM databases

PhosphoSite

Q9UBE0.

Proteomic databases

PeptideAtlas

Q9UBE0.

PRIDE

Q9UBE0.

Genome annotation databases

Ensembl

ENSG00000142230. Homo sapiens. [Contig view]

GeneID

10055.

KEGG

hsa:10055.

Organism-specific databases

GeneCards

GC19P052328.

H-InvDB

HIX0015267.

HGNC

HGNC:30660. SAE1.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UBE0.

OMA

Q9UBE0. GSGIVEC.

Gene expression databases

ArrayExpress

Q9UBE0.

Bgee

Q9UBE0.

CleanEx

HS_SAE1.

GermOnline

ENSG00000142230. Homo sapiens.

Family and domain databases

InterPro

IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD_bd.
IPR000011. UBQ-activ_enz_E1-like.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF00899. ThiF. 1 hit.
[Graphical view]

PRINTS

PR01849. UBIQUITINACT.

ProtoNet

Search...

Other Resources

NextBio

37989.

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Entry information

Entry name

SAE1_HUMAN

Accession

Primary (citable) accession number: Q9UBE0
Secondary accession number(s): O95717, Q9P020

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 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

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

Amino acid modifications

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