P22314 (UBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-like modifier-activating enzyme 1

Alternative name(s):
Protein A1S9
Ubiquitin-activating enzyme E1

Gene names

Name:	UBA1
Synonyms:	A1S9T, UBE1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1058 AA.
Sequence status	Complete.
Protein existence	Evidence 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 an ubiquitin-E1 thioester and free AMP.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Monomer By similarity. Interacts with GAN (via BTB domain). Ref.12
Post-translational modification	ISGylated. Ref.10
Involvement in disease	Defects in UBA1 are the cause of spinal muscular atrophy X-linked type 2 (SMAX2) [MIM:301830]; also known as X-linked lethal infantile spinal muscular atrophy, distal X-linked arthrogryposis multiplex congenita or X-linked arthrogryposis type 1 (AMCX1). Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX2 is a lethal infantile form presenting with hypotonia, areflexia, and multiple congenital contractures. Ref.19
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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Disease	Disease mutation Neurodegeneration
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW protein modification process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.12. Source: IntAct small protein activating enzyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAN	Q9H2C0	5	EBI-709688,EBI-764342
UBE2I	P63279	2	EBI-709688,EBI-80168

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1058	1058	Ubiquitin-like modifier-activating enzyme 1		PRO_0000194934
Regions
	Repeat	63 – 199	137	1-1
	Repeat	459 – 611	153	1-2
	Nucleotide binding	478 – 507	30	ATP By similarity
	Region	63 – 611	549	2 approximate repeats
Sites
	Active site	632	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	4	1	Phosphoserine Ref.15
	Modified residue	13	1	Phosphoserine Ref.14
	Modified residue	24	1	Phosphoserine Ref.14
	Modified residue	46	1	Phosphoserine Ref.9 Ref.13 Ref.14 Ref.16
	Modified residue	55	1	Phosphotyrosine Ref.11
	Modified residue	671	1	N6-acetyllysine Ref.17
	Modified residue	800	1	Phosphothreonine Ref.14
	Modified residue	810	1	Phosphoserine Ref.16
	Modified residue	835	1	Phosphoserine Ref.14 Ref.15
	Modified residue	980	1	N6-acetyllysine Ref.17
Natural variations
	Natural variant	447	1	R → H. Corresponds to variant rs2070169 [ dbSNP | Ensembl ].		VAR_043500
	Natural variant	539	1	M → I in SMAX2. Ref.19		VAR_043501
	Natural variant	547	1	S → G in SMAX2. Ref.19		VAR_043502
Experimental info
	Sequence conflict	190	1	D → G in CAA40296. Ref.1
	Sequence conflict	434	1	E → Q in CAA40296. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22314 [UniParc]. Last modified October 25, 2002. Version 3. Checksum: 4B413AAA75FAA562	FASTA	1,058	117,849
	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

References

	« Hide 'large scale' referencesShow '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: 1606621] [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: 1986373] [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: 1871145] [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. , 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: 15772651] [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. , 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: 15489334] [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: 2390975] [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, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 16139798] [Abstract] Cited for: ISGYLATION.
[11]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, MASS SPECTROMETRY.
[12]	"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: 16227972] [Abstract] Cited for: INTERACTION WITH GAN.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-13; SER-24; SER-46; THR-800 AND SER-835, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-835, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-810, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-671 AND LYS-980, MASS SPECTROMETRY.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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: 18179898] [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.
IPI	IPI00645078.
PIR	A38564.
RefSeq	NP_003325.2. NM_003334.3. NP_695012.1. NM_153280.2.
UniGene	Hs.533273.
3D structure databases
ProteinModelPortal	P22314.
SMR	P22314. Positions 47-1057.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22314. 18 interactions.
MINT	MINT-1130980.
STRING	P22314.
PTM databases
PhosphoSite	P22314.
Polymorphism databases
DMDM	24418865.
2D gel databases
REPRODUCTION-2DPAGE	IPI00645078.
Proteomic databases
PeptideAtlas	P22314.
PRIDE	P22314.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335972; ENSP00000338413; ENSG00000130985. ENST00000377351; ENSP00000366568; ENSG00000130985.
GeneID	7317.
KEGG	hsa:7317.
UCSC	uc004dhj.2. human.
Organism-specific databases
CTD	7317.
GeneCards	GC0XP047050.
H-InvDB	HIX0016757.
HGNC	HGNC:12469. UBA1.
HPA	CAB019435. HPA000289.
MIM	301830. phenotype. 314370. gene.
neXtProt	NX_P22314.
Orphanet	1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKB	PA162407527. PA37119.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG356508.
HOVERGEN	HBG054199.
InParanoid	P22314.
OMA	ANGMAKN.
OrthoDB	EOG4QZ7K4.
PhylomeDB	P22314.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P22314.
Bgee	P22314.
CleanEx	HS_UBA1.
Genevestigator	P22314.
GermOnline	ENSG00000130985. Homo sapiens.
Family and domain databases
InterPro	IPR009036. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 4 hits. G3DSA:1.10.3240.10. Ub-like_act_enz_cat_cys_dom. 1 hit.
KO	K03178.
Pfam	PF00899. ThiF. 2 hits. PF09358. UBA_e1_C. 1 hit. PF10585. UBA_e1_thiolCys. 1 hit. PF02134. UBACT. 2 hits. [Graphical view]
PRINTS	PR01849. UBIQUITINACT.
SMART	SM00985. UBA_e1_C. 1 hit. [Graphical view]
SUPFAM	SSF69572. MoeB. 2 hits.
TIGRFAMs	TIGR01408. Ube1. 1 hit.
PROSITE	PS00536. UBIQUITIN_ACTIVAT_1. 1 hit. PS00865. UBIQUITIN_ACTIVAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	28604.
SOURCE	Search...

Entry information

Entry name

UBA1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.