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Protein

Ubiquitin-like modifier-activating enzyme 5

Gene

UBA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E1-like enzyme which activates UFM1 and SUMO2.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831ATP; via amide nitrogen1 Publication
Binding sitei104 – 1041ATP1 Publication
Binding sitei127 – 1271ATP1 Publication
Binding sitei150 – 1501ATP1 Publication
Binding sitei184 – 1841ATP1 Publication
Metal bindingi226 – 2261Zinc1 Publication
Metal bindingi229 – 2291Zinc1 Publication
Active sitei250 – 2501Glycyl thioester intermediate1 Publication
Metal bindingi303 – 3031Zinc1 Publication
Metal bindingi308 – 3081Zinc1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. UFM1 activating enzyme activity Source: UniProtKB

GO - Biological processi

  1. protein polyufmylation Source: UniProtKB
  2. protein ufmylation Source: UniProtKB
  3. regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  4. response to endoplasmic reticulum stress Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 5
Short name:
Ubiquitin-activating enzyme 5
Alternative name(s):
ThiFP1
UFM1-activating enzyme
Ubiquitin-activating enzyme E1 domain-containing protein 1
Gene namesi
Name:UBA5
Synonyms:UBE1DC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:23230. UBA5.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Localizes mainly in cytoplasm, while it mainly localizes to the nucleus in presence of SUMO2.

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: GO_Central
  3. intracellular membrane-bounded organelle Source: HPA
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501C → S: Forms a stable intermediate complex. 1 Publication

Organism-specific databases

PharmGKBiPA162407661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Ubiquitin-like modifier-activating enzyme 5PRO_0000194970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9GZZ9.
PaxDbiQ9GZZ9.
PRIDEiQ9GZZ9.

PTM databases

PhosphoSiteiQ9GZZ9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9GZZ9.
CleanExiHS_UBA5.
ExpressionAtlasiQ9GZZ9. baseline and differential.
GenevestigatoriQ9GZZ9.

Organism-specific databases

HPAiHPA017235.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951662EBI-747805,EBI-712001
GABARAPL1Q9H0R82EBI-747805,EBI-746969
GABARAPL2P6052010EBI-747805,EBI-720116
MAP1LC3BQ9GZQ82EBI-747805,EBI-373144
MAP1LC3CQ9BXW42EBI-747805,EBI-2603996

Protein-protein interaction databases

BioGridi122964. 56 interactions.
IntActiQ9GZZ9. 37 interactions.
MINTiMINT-1475093.
STRINGi9606.ENSP00000348565.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi70 – 734Combined sources
Beta strandi75 – 795Combined sources
Helixi83 – 9513Combined sources
Beta strandi98 – 1036Combined sources
Helixi120 – 1223Combined sources
Helixi127 – 13812Combined sources
Beta strandi142 – 1476Combined sources
Helixi154 – 16613Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi176 – 1805Combined sources
Helixi185 – 19814Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi211 – 2199Combined sources
Turni221 – 2233Combined sources
Beta strandi229 – 2313Combined sources
Helixi247 – 27428Combined sources
Beta strandi281 – 2866Combined sources
Turni287 – 2904Combined sources
Helixi306 – 31712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GUCX-ray2.25A/B57-329[»]
3H8VX-ray2.00A/B57-329[»]
ProteinModelPortaliQ9GZZ9.
SMRiQ9GZZ9. Positions 43-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GZZ9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family. UBA5 subfamily.Sequence Analysis

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00570000079161.
HOGENOMiHOG000256352.
HOVERGENiHBG056496.
InParanoidiQ9GZZ9.
KOiK12164.
OMAiTWFESGV.
OrthoDBiEOG7N63MX.
PhylomeDBiQ9GZZ9.
TreeFamiTF314168.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR029752. D-isomer_DH_CS1.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9GZZ9-1) [UniParc]FASTAAdd to basket

Also known as: UBE1DC1A

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.

« Hide

        10         20         30         40         50
MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS
60 70 80 90 100
NPYSRLMALK RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL
110 120 130 140 150
LLFDYDKVEL ANMNRLFFQP HQAGLSKVQA AEHTLRNINP DVLFEVHNYN
160 170 180 190 200
ITTVENFQHF MDRISNGGLE EGKPVDLVLS CVDNFEARMT INTACNELGQ
210 220 230 240 250
TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID EKTLKREGVC
260 270 280 290 300
AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
310 320 330 340 350
PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS
360 370 380 390 400
EEELKNFSGP VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK

MKNM
Length:404
Mass (Da):44,863
Last modified:March 1, 2001 - v1
Checksum:i02F0F64FEAA1E880
GO
Isoform 2 (identifier: Q9GZZ9-2) [UniParc]FASTAAdd to basket

Also known as: UBE1DC1B

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Show »
Length:348
Mass (Da):38,537
Checksum:i127B3CB48EB035B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031N → S in BAB55199 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 2. CuratedVSP_038528Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB154406 mRNA. Translation: BAD15375.1.
AY253672 mRNA. Translation: AAP79600.1.
AL136757 mRNA. Translation: CAB66691.1.
AK026904 mRNA. Translation: BAB15587.1.
AK027563 mRNA. Translation: BAB55199.1.
AC020632 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79192.1.
CH471052 Genomic DNA. Translation: EAW79189.1.
CH471052 Genomic DNA. Translation: EAW79191.1.
BC009737 mRNA. Translation: AAH09737.1.
CCDSiCCDS3076.1. [Q9GZZ9-1]
CCDS3077.1. [Q9GZZ9-2]
RefSeqiNP_079094.1. NM_024818.3. [Q9GZZ9-1]
NP_938143.1. NM_198329.2. [Q9GZZ9-2]
XP_005247844.1. XM_005247787.2. [Q9GZZ9-2]
UniGeneiHs.170737.

Genome annotation databases

EnsembliENST00000264991; ENSP00000264991; ENSG00000081307. [Q9GZZ9-2]
ENST00000356232; ENSP00000348565; ENSG00000081307. [Q9GZZ9-1]
ENST00000494238; ENSP00000418807; ENSG00000081307. [Q9GZZ9-2]
GeneIDi79876.
KEGGihsa:79876.
UCSCiuc003epa.4. human. [Q9GZZ9-1]

Polymorphism databases

DMDMi74733510.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB154406 mRNA. Translation: BAD15375.1.
AY253672 mRNA. Translation: AAP79600.1.
AL136757 mRNA. Translation: CAB66691.1.
AK026904 mRNA. Translation: BAB15587.1.
AK027563 mRNA. Translation: BAB55199.1.
AC020632 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79192.1.
CH471052 Genomic DNA. Translation: EAW79189.1.
CH471052 Genomic DNA. Translation: EAW79191.1.
BC009737 mRNA. Translation: AAH09737.1.
CCDSiCCDS3076.1. [Q9GZZ9-1]
CCDS3077.1. [Q9GZZ9-2]
RefSeqiNP_079094.1. NM_024818.3. [Q9GZZ9-1]
NP_938143.1. NM_198329.2. [Q9GZZ9-2]
XP_005247844.1. XM_005247787.2. [Q9GZZ9-2]
UniGeneiHs.170737.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GUCX-ray2.25A/B57-329[»]
3H8VX-ray2.00A/B57-329[»]
ProteinModelPortaliQ9GZZ9.
SMRiQ9GZZ9. Positions 43-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122964. 56 interactions.
IntActiQ9GZZ9. 37 interactions.
MINTiMINT-1475093.
STRINGi9606.ENSP00000348565.

Chemistry

BindingDBiQ9GZZ9.
ChEMBLiCHEMBL2016429.

PTM databases

PhosphoSiteiQ9GZZ9.

Polymorphism databases

DMDMi74733510.

Proteomic databases

MaxQBiQ9GZZ9.
PaxDbiQ9GZZ9.
PRIDEiQ9GZZ9.

Protocols and materials databases

DNASUi79876.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264991; ENSP00000264991; ENSG00000081307. [Q9GZZ9-2]
ENST00000356232; ENSP00000348565; ENSG00000081307. [Q9GZZ9-1]
ENST00000494238; ENSP00000418807; ENSG00000081307. [Q9GZZ9-2]
GeneIDi79876.
KEGGihsa:79876.
UCSCiuc003epa.4. human. [Q9GZZ9-1]

Organism-specific databases

CTDi79876.
GeneCardsiGC03P132373.
HGNCiHGNC:23230. UBA5.
HPAiHPA017235.
MIMi610552. gene.
neXtProtiNX_Q9GZZ9.
PharmGKBiPA162407661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00570000079161.
HOGENOMiHOG000256352.
HOVERGENiHBG056496.
InParanoidiQ9GZZ9.
KOiK12164.
OMAiTWFESGV.
OrthoDBiEOG7N63MX.
PhylomeDBiQ9GZZ9.
TreeFamiTF314168.

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ9GZZ9.
GeneWikiiUBE1DC1.
GenomeRNAii79876.
NextBioi69659.
PROiQ9GZZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZZ9.
CleanExiHS_UBA5.
ExpressionAtlasiQ9GZZ9. baseline and differential.
GenevestigatoriQ9GZZ9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR029752. D-isomer_DH_CS1.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier."
    Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N., Ueno T., Kominami E., Natsume T., Tanaka K.
    EMBO J. 23:1977-1986(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-250.
  2. "Isolation and characterization of ubiquitin-activating enzyme E1-domain containing 1, UBE1DC1."
    Dou T., Gu S., Liu J., Chen F., Zeng L., Guo L., Xie Y., Mao Y.
    Mol. Biol. Rep. 32:265-271(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: TestisImported.
  4. "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.
    , 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] (ISOFORM 1).
    Tissue: ColonImported and TeratocarcinomaImported.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: LungImported.
  8. "UBE1DC1, an ubiquitin-activating enzyme, activates two different ubiquitin-like proteins."
    Zheng M., Gu X., Zheng D., Yang Z., Li F., Zhao J., Xie Y., Ji C., Mao Y.
    J. Cell. Biochem. 104:2324-2334(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme."
    Bacik J.P., Walker J.R., Ali M., Schimmer A.D., Dhe-Paganon S.
    J. Biol. Chem. 285:20273-20280(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP AND ZINC, FUNCTION, ACTIVE SITE.

Entry informationi

Entry nameiUBA5_HUMAN
AccessioniPrimary (citable) accession number: Q9GZZ9
Secondary accession number(s): A6NJL3, D3DNC8, Q96ST1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.