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P22314 (UBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Protein A1S9
Ubiquitin-activating enzyme E1
Gene names
Name:UBA1
Synonyms:A1S9T, UBE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1058 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer By similarity. Interacts with GAN (via BTB domain). Ref.11

Post-translational modification

ISGylated. Ref.9

Involvement in disease

Spinal muscular atrophy X-linked 2 (SMAX2) [MIM:301830]: A lethal infantile form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Clinical features include hypotonia, areflexia, and multiple congenital contractures.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q763532EBI-709688,EBI-6248077From a different organism.
GANQ9H2C05EBI-709688,EBI-764342
UBE2IP632792EBI-709688,EBI-80168

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 10581057Ubiquitin-like modifier-activating enzyme 1
PRO_0000194934

Regions

Repeat63 – 1991371-1
Repeat459 – 6111531-2
Nucleotide binding478 – 50730ATP By similarity
Region63 – 6115492 approximate repeats

Sites

Active site6321Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.19
Modified residue131Phosphoserine Ref.12
Modified residue461Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18
Modified residue551Phosphotyrosine By similarity
Modified residue5281N6-succinyllysine By similarity
Modified residue6711N6-acetyllysine Ref.15
Modified residue8001Phosphothreonine Ref.12
Modified residue8101Phosphoserine Ref.14 Ref.16
Modified residue8161Phosphoserine By similarity
Modified residue8201Phosphoserine By similarity
Modified residue8351Phosphoserine Ref.12
Modified residue9801N6-acetyllysine Ref.15

Natural variations

Natural variant4471R → H.
Corresponds to variant rs2070169 [ dbSNP | Ensembl ].
VAR_043500
Natural variant5391M → I in SMAX2. Ref.20
VAR_043501
Natural variant5471S → G in SMAX2. Ref.20
VAR_043502

Experimental info

Sequence conflict1901D → G in CAA40296. Ref.1
Sequence conflict4341E → Q in CAA40296. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22314 [UniParc].

Last modified October 25, 2002. Version 3.
Checksum: 4B413AAA75FAA562

FASTA1,058117,849
        10         20         30         40         50         60 
MSSSPLSKKR RVSGPDPKPG SNCSPAQSVL SEVPSVPTNG MAKNGSEADI DEGLYSRQLY 

        70         80         90        100        110        120 
VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTAQWA DLSSQFYLRE 

       130        140        150        160        170        180 
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSGFQ VVVLTNTPLE DQLRVGEFCH 

       190        200        210        220        230        240 
NRGIKLVVAD TRGLFGQLFC DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH 

       250        260        270        280        290        300 
GFESGDFVSF SEVQGMVELN GNQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 

       310        320        330        340        350        360 
ISFKSLVASL AEPDFVVTDF AKFSRPAQLH IGFQALHQFC AQHGRPPRPR NEEDAAELVA 

       370        380        390        400        410        420 
LAQAVNARAL PAVQQNNLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI 

       430        440        450        460        470        480 
MQWLYFDALE CLPEDKEVLT EDKCLQRQNR YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG 

       490        500        510        520        530        540 
CELLKNFAMI GLGCGEGGEI IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN 

       550        560        570        580        590        600 
PHIRVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT 

       610        620        630        640        650        660 
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA 

       670        680        690        700        710        720 
ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWADCVTWA CHHWHTQYSN 

       730        740        750        760        770        780 
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNPL HLDYVMAAAN LFAQTYGLTG 

       790        800        810        820        830        840 
SQDRAAVATF LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP 

       850        860        870        880        890        900 
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDIPSADR HKSKLIAGKI IPAIATTTAA 

       910        920        930        940        950        960 
VVGLVCLELY KVVQGHRQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV 

       970        980        990       1000       1010       1020 
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS 

      1030       1040       1050 
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR 

« Hide

References

« Hide 'large scale' references
[1]"Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1."
Ayusawa D., Kaneda S., Itoh Y., Yasuda H., Murakami Y., Sugasawa K., Hanaoka F., Seno T.
Cell Struct. Funct. 17:113-122(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1."
Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
Proc. Natl. Acad. Sci. U.S.A. 88:258-262(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 136-158; 369-383; 417-430 AND 559-580.
Tissue: Placenta.
[3]Erratum
Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
Proc. Natl. Acad. Sci. U.S.A. 88:7456-7456(1991) [PubMed] [Europe PMC] [Abstract]
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[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].
Tissue: Lymph.
[7]"Molecular cloning, primary structure and expression of the human X linked A1S9 gene cDNA which complements the ts A1S9 mouse L cell defect in DNA replication."
Zacksenhaus E., Sheinin R.
EMBO J. 9:2923-2929(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-989.
[8]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 559-581 AND 924-944, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[9]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAN.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-46; THR-800 AND SER-835, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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-671 AND LYS-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy."
Ramser J., Ahearn M.E., Lenski C., Yariz K.O., Hellebrand H., von Rhein M., Clark R.D., Schmutzler R.K., Lichtner P., Hoffman E.P., Meindl A., Baumbach-Reardon L.
Am. J. Hum. Genet. 82:188-193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMAX2 ILE-539 AND GLY-547.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56976 mRNA. Translation: CAA40296.1.
M58028 mRNA. Translation: AAA61246.1.
AL513366 Genomic DNA. Translation: CAI41708.1.
CH471164 Genomic DNA. Translation: EAW59290.1.
BC013041 mRNA. Translation: AAH13041.1.
X52897 mRNA. Translation: CAA37078.1.
PIRA38564.
RefSeqNP_003325.2. NM_003334.3.
NP_695012.1. NM_153280.2.
XP_005272707.1. XM_005272650.1.
UniGeneHs.533273.

3D structure databases

ProteinModelPortalP22314.
SMRP22314. Positions 50-1053.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113165. 78 interactions.
DIPDIP-33686N.
IntActP22314. 28 interactions.
MINTMINT-1130980.
STRING9606.ENSP00000338413.

Chemistry

ChEMBLCHEMBL5924.

PTM databases

PhosphoSiteP22314.

Polymorphism databases

DMDM24418865.

2D gel databases

REPRODUCTION-2DPAGEIPI00645078.

Proteomic databases

PaxDbP22314.
PeptideAtlasP22314.
PRIDEP22314.

Protocols and materials databases

DNASU7317.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335972; ENSP00000338413; ENSG00000130985.
ENST00000377351; ENSP00000366568; ENSG00000130985.
ENST00000604887; ENSP00000474569; ENSG00000271310.
ENST00000605619; ENSP00000474757; ENSG00000271310.
GeneID7317.
KEGGhsa:7317.
UCSCuc004dhj.4. human.

Organism-specific databases

CTD7317.
GeneCardsGC0XP047050.
HGNCHGNC:12469. UBA1.
HPACAB019435.
HPA000289.
HPA001506.
MIM301830. phenotype.
314370. gene.
neXtProtNX_P22314.
Orphanet1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKBPA37119.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000167329.
HOVERGENHBG054199.
InParanoidP22314.
KOK03178.
OMAPFFAFSE.
OrthoDBEOG74R1PV.
PhylomeDBP22314.
TreeFamTF300586.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP22314.
BgeeP22314.
CleanExHS_UBA1.
GenevestigatorP22314.

Family and domain databases

Gene3D1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBA1. human.
GeneWikiUBA1.
GenomeRNAi7317.
NextBio28604.
PROP22314.
SOURCESearch...

Entry information

Entry nameUBA1_HUMAN
AccessionPrimary (citable) accession number: P22314
Secondary accession number(s): Q5JRR8, Q96E13
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 25, 2002
Last modified: April 16, 2014
This is version 162 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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