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Q9UBE0 (SAE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SUMO-activating enzyme subunit 1
Alternative name(s):
Ubiquitin-like 1-activating enzyme E1A
Gene names
Name:SAE1
Synonyms:AOS1, SUA1, UBLE1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.3 Ref.11 Ref.12 Ref.17 Ref.18

Pathway

Protein modification; protein sumoylation.

Subunit structure

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. Ref.1 Ref.2 Ref.3 Ref.11

Subcellular location

Nucleus Ref.11.

Tissue specificity

Expression level increases during S phase and drops in G2 phase (at protein level). Ref.11

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

post-translational protein modification

Traceable author statement. Source: Reactome

protein sumoylation

Inferred from direct assay Ref.18. Source: UniProtKB

protein ubiquitination

Traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.3. Source: UniProtKB

   Molecular_functionATP-dependent protein binding

Inferred from direct assay Ref.3. Source: UniProtKB

enzyme activator activity

Traceable author statement Ref.1. Source: ProtInc

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from direct assay Ref.3. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17PubMed 16189514. Source: IntAct

protein heterodimerization activity

Inferred from physical interaction Ref.18. Source: UniProtKB

ubiquitin activating enzyme activity

Traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBA2Q9UBT23EBI-743154,EBI-718569

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBE0-1)

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.
Isoform 2 (identifier: Q9UBE0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     245-266: VLLKFRTDKGRDPSSDTYEEDS → GTASPRWPQCVRWLEGFWHRKL
     267-346: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UBE0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     245-299: VLLKFRTDKG...DFVRYCFSEM → GPVSAGPSSQ...PTCIPCPLPS
     300-346: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346SUMO-activating enzyme subunit 1
PRO_0000194966
Initiator methionine11Removed; alternate Ref.14
Chain2 – 346345SUMO-activating enzyme subunit 1, N-terminally processed
PRO_0000423290

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14 Ref.16
Modified residue21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processed Ref.14
Modified residue1981N6-acetyllysine By similarity

Natural variations

Alternative sequence245 – 29955VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS in isoform 3.
VSP_045372
Alternative sequence245 – 26622VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2.
VSP_045373
Alternative sequence267 – 34680Missing in isoform 2.
VSP_045374
Alternative sequence300 – 34647Missing in isoform 3.
VSP_045375

Experimental info

Mutagenesis211R → A: Abolishes ATP-dependent activation of SUMO proteins. Ref.18
Mutagenesis24 – 263RLW → AAA: Abolishes ATP-dependent activation of SUMO proteins. Ref.18
Sequence conflict1151I → M in BAG51064. Ref.6
Sequence conflict1581V → A in AAF29104. Ref.4
Sequence conflict178 – 1803KTK → ETD in AAF29104. Ref.4
Sequence conflict1861Q → H in AAF29104. Ref.4
Sequence conflict2731R → G in AAD12785. Ref.1

Secondary structure

......................................................... 346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA34638,450
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 058AD8B9B2A2EEBB
Show »

FASTA26629,811
Isoform 3 [UniParc].

Checksum: 35D1828B2957CCBA
Show »

FASTA29933,063

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[5]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: B-cell.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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] (ISOFORM 1).
Tissue: Colon, Lung and Placenta.
[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, TISSUE SPECIFICITY, 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]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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 UBA2; SUMO1 AND ATP, FUNCTION.
[18]"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 UBA2 AND SUMO1, FUNCTION, MUTAGENESIS OF ARG-21 AND 24-ARG--TRP-26.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090385 mRNA. Translation: AAD12785.2.
AF046025 mRNA. Translation: AAD23902.2.
AF110956 mRNA. Translation: AAD24433.1.
AF161489 mRNA. Translation: AAF29104.1.
AL560234 mRNA. No translation available.
BT007290 mRNA. Translation: AAP35954.1.
AK021978 mRNA. Translation: BAG51064.1.
AK315624 mRNA. Translation: BAG37992.1.
AC008532 Genomic DNA. No translation available.
AC008755 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57461.1.
CH471126 Genomic DNA. Translation: EAW57463.1.
BC000344 mRNA. Translation: AAH00344.1.
BC003611 mRNA. Translation: AAH03611.1.
BC018271 mRNA. Translation: AAH18271.1.
CCDSCCDS12696.1. [Q9UBE0-1]
CCDS54284.1. [Q9UBE0-2]
CCDS54285.1. [Q9UBE0-3]
RefSeqNP_001139185.1. NM_001145713.1. [Q9UBE0-3]
NP_001139186.1. NM_001145714.1. [Q9UBE0-2]
NP_005491.1. NM_005500.2. [Q9UBE0-1]
UniGeneHs.515500.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25A/C1-346[»]
1Y8RX-ray2.75A/D1-346[»]
3KYCX-ray2.45A1-346[»]
3KYDX-ray2.61A1-346[»]
DisProtDP00485.
ProteinModelPortalQ9UBE0.
SMRQ9UBE0. Positions 25-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115366. 38 interactions.
DIPDIP-34587N.
IntActQ9UBE0. 6 interactions.
MINTMINT-1205002.
STRING9606.ENSP00000270225.

Chemistry

BindingDBQ9UBE0.
ChEMBLCHEMBL1615388.

PTM databases

PhosphoSiteQ9UBE0.

Polymorphism databases

DMDM42559897.

Proteomic databases

MaxQBQ9UBE0.
PaxDbQ9UBE0.
PeptideAtlasQ9UBE0.
PRIDEQ9UBE0.

Protocols and materials databases

DNASU10055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270225; ENSP00000270225; ENSG00000142230. [Q9UBE0-1]
ENST00000392776; ENSP00000440818; ENSG00000142230. [Q9UBE0-2]
ENST00000413379; ENSP00000416557; ENSG00000142230. [Q9UBE0-3]
GeneID10055.
KEGGhsa:10055.
UCSCuc002pgc.3. human. [Q9UBE0-1]
uc010ekx.3. human.

Organism-specific databases

CTD10055.
GeneCardsGC19P047634.
HGNCHGNC:30660. SAE1.
HPAHPA041906.
HPA043552.
MIM613294. gene.
neXtProtNX_Q9UBE0.
PharmGKBPA162402387.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000172217.
HOVERGENHBG080782.
InParanoidQ9UBE0.
KOK10684.
OMARTPVDYF.
PhylomeDBQ9UBE0.
TreeFamTF315037.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressQ9UBE0.
BgeeQ9UBE0.
CleanExHS_SAE1.
GenevestigatorQ9UBE0.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamPF00899. ThiF. 1 hit.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SUPFAMSSF69572. SSF69572. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9UBE0.
GeneWikiSAE1.
GenomeRNAi10055.
NextBio37989.
PROQ9UBE0.
SOURCESearch...

Entry information

Entry nameSAE1_HUMAN
AccessionPrimary (citable) accession number: Q9UBE0
Secondary accession number(s): B2RDP5 expand/collapse secondary AC list , B3KMQ2, F5GXX7, G3XAK6, O95717, Q9P020
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 129 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM