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Protein

Ubiquitin-associated domain-containing protein 1

Gene

UBAC1

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

Functioni

Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Protein family/group databases

MEROPSiC19.M01.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-associated domain-containing protein 1
Short name:
UBA domain-containing protein 1
Alternative name(s):
E3 ubiquitin-protein ligase subunit KPC2
Glialblastoma cell differentiation-related protein 1
Kip1 ubiquitination-promoting complex protein 2
Gene namesi
Name:UBAC1
Synonyms:GBDR1, KPC2, UBADC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:30221. UBAC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407814.

Polymorphism and mutation databases

BioMutaiUBAC1.
DMDMi74752306.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405Ubiquitin-associated domain-containing protein 1PRO_0000250449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BSL1.
MaxQBiQ9BSL1.
PaxDbiQ9BSL1.
PeptideAtlasiQ9BSL1.
PRIDEiQ9BSL1.

PTM databases

iPTMnetiQ9BSL1.
PhosphoSiteiQ9BSL1.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9BSL1.
CleanExiHS_UBAC1.
GenevisibleiQ9BSL1. HS.

Organism-specific databases

HPAiHPA005651.

Interactioni

Subunit structurei

Component of the KPC complex composed of RNF123/KPC1 and UBAC1/KPC2. Interacts with RNF123 via its N-terminal domain. Interacts with the proteasome via its N-terminal domain.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150384EBI-749370,EBI-724310
HTTP428585EBI-749370,EBI-466029
TRIM2Q9C0404EBI-749370,EBI-749840
TRIM39Q9HCM93EBI-749370,EBI-739510

Protein-protein interaction databases

BioGridi115691. 58 interactions.
DIPiDIP-47279N.
IntActiQ9BSL1. 9 interactions.
STRINGi9606.ENSP00000360821.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi189 – 1913Combined sources
Helixi194 – 20310Combined sources
Helixi207 – 21610Combined sources
Helixi221 – 23010Combined sources
Helixi231 – 2333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAINMR-A172-241[»]
ProteinModelPortaliQ9BSL1.
SMRiQ9BSL1. Positions 172-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BSL1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 9885Ubiquitin-likeAdd
BLAST
Domaini187 – 23145UBA 1PROSITE-ProRule annotationAdd
BLAST
Domaini288 – 32841UBA 2PROSITE-ProRule annotationAdd
BLAST
Domaini353 – 39240STI1Add
BLAST

Sequence similaritiesi

Contains 1 STI1 domain.Curated
Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IHU5. Eukaryota.
ENOG410Y2UN. LUCA.
GeneTreeiENSGT00390000014658.
HOGENOMiHOG000231457.
HOVERGENiHBG053148.
InParanoidiQ9BSL1.
KOiK12174.
OMAiFQAILEN.
OrthoDBiEOG7060QJ.
PhylomeDBiQ9BSL1.
TreeFamiTF324579.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BSL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVQEEKIFA GKVLRLHICA SDGAEWLEEA TEDTSVEKLK ERCLKHCAHG
60 70 80 90 100
SLEDPKSITH HKLIHAASER VLSDARTILE ENIQDQDVLL LIKKRAPSPL
110 120 130 140 150
PKMADVSAEE KKKQDQKAPD KEAILRATAN LPSYNMDRAA VQTNMRDFQT
160 170 180 190 200
ELRKILVSLI EVAQKLLALN PDAVELFKKA NAMLDEDEDE RVDEAALRQL
210 220 230 240 250
TEMGFPENRA TKALQLNHMS VPQAMEWLIE HAEDPTIDTP LPGQAPPEAE
260 270 280 290 300
GATAAASEAA AGASATDEEA RDELTEIFKK IRRKREFRAD ARAVISLMEM
310 320 330 340 350
GFDEKEVIDA LRVNNNQQNA ACEWLLGDRK PSPEELDKGI DPDSPLFQAI
360 370 380 390 400
LDNPVVQLGL TNPKTLLAFE DMLENPLNST QWMNDPETGP VMLQISRIFQ

TLNRT
Length:405
Mass (Da):45,338
Last modified:June 1, 2001 - v1
Checksum:i5FC8EC84A8602CBE
GO

Sequence cautioni

The sequence AAC21559.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441Q → R in AAC21559 (Ref. 4) Curated
Sequence conflicti269 – 2691Missing in AAD51084 (PubMed:10857748).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti374 – 3741E → D.
Corresponds to variant rs11103231 [ dbSNP | Ensembl ].
VAR_027562

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176796 mRNA. Translation: AAD51084.1.
AL355574 Genomic DNA. Translation: CAI14118.1.
BC004967 mRNA. Translation: AAH04967.1.
BC011822 mRNA. Translation: AAH11822.1.
AF068195 mRNA. Translation: AAC21559.1. Different initiation.
CCDSiCCDS35177.1.
RefSeqiNP_057256.2. NM_016172.2.
UniGeneiHs.9194.

Genome annotation databases

EnsembliENST00000371756; ENSP00000360821; ENSG00000130560.
GeneIDi10422.
KEGGihsa:10422.
UCSCiuc004cgt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176796 mRNA. Translation: AAD51084.1.
AL355574 Genomic DNA. Translation: CAI14118.1.
BC004967 mRNA. Translation: AAH04967.1.
BC011822 mRNA. Translation: AAH11822.1.
AF068195 mRNA. Translation: AAC21559.1. Different initiation.
CCDSiCCDS35177.1.
RefSeqiNP_057256.2. NM_016172.2.
UniGeneiHs.9194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAINMR-A172-241[»]
ProteinModelPortaliQ9BSL1.
SMRiQ9BSL1. Positions 172-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115691. 58 interactions.
DIPiDIP-47279N.
IntActiQ9BSL1. 9 interactions.
STRINGi9606.ENSP00000360821.

Protein family/group databases

MEROPSiC19.M01.

PTM databases

iPTMnetiQ9BSL1.
PhosphoSiteiQ9BSL1.

Polymorphism and mutation databases

BioMutaiUBAC1.
DMDMi74752306.

Proteomic databases

EPDiQ9BSL1.
MaxQBiQ9BSL1.
PaxDbiQ9BSL1.
PeptideAtlasiQ9BSL1.
PRIDEiQ9BSL1.

Protocols and materials databases

DNASUi10422.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371756; ENSP00000360821; ENSG00000130560.
GeneIDi10422.
KEGGihsa:10422.
UCSCiuc004cgt.3. human.

Organism-specific databases

CTDi10422.
GeneCardsiUBAC1.
HGNCiHGNC:30221. UBAC1.
HPAiHPA005651.
MIMi608129. gene.
neXtProtiNX_Q9BSL1.
PharmGKBiPA162407814.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHU5. Eukaryota.
ENOG410Y2UN. LUCA.
GeneTreeiENSGT00390000014658.
HOGENOMiHOG000231457.
HOVERGENiHBG053148.
InParanoidiQ9BSL1.
KOiK12174.
OMAiFQAILEN.
OrthoDBiEOG7060QJ.
PhylomeDBiQ9BSL1.
TreeFamiTF324579.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUBAC1. human.
EvolutionaryTraceiQ9BSL1.
GeneWikiiUBAC1.
GenomeRNAii10422.
PROiQ9BSL1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BSL1.
CleanExiHS_UBAC1.
GenevisibleiQ9BSL1. HS.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a glialblastoma cell differentiation factor-related gene mRNA in human microvascular endothelial cells."
    Li C., Rodriguez M., Adamson J.W., Banerjee D.
    Genomics 65:243-252(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Endothelial cell.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Lung and Lymph.
  4. Jin H.L., Hu S.N., Li G.T., Tu C., Zhong N., Yuan J.G., Qiang B.Q.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-405.
    Tissue: Glioblastoma.
  5. "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase."
    Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.
    Nat. Cell Biol. 6:1229-1235(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  6. "Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase."
    Kotoshiba S., Kamura T., Hara T., Ishida N., Nakayama K.
    J. Biol. Chem. 280:17694-17700(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Solution structure of the first UBA domain in the human ubiquitin associated domain containing 1 (UBADC1)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 172-241.

Entry informationi

Entry nameiUBAC1_HUMAN
AccessioniPrimary (citable) accession number: Q9BSL1
Secondary accession number(s): O75500, Q9UMW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 135 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.