Reviewed, UniProtKB/Swiss-Prot Q9BSL1 (UBAC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin-associated domain-containing protein 1
      Short name=UBA domain-containing protein 1
Alternative name(s):
    E3 ubiquitin-protein ligase subunit KPC2
    Kip1 ubiquitination-promoting complex protein 2
    Glialblastoma cell differentiation-related protein 1

Gene names

Name:	UBAC1
Synonyms:	GBDR1, KPC2, UBADC1

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	405 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.5 Ref.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.5 Ref.6
Subcellular location	Cytoplasm. Ref.5 Ref.1
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Contains 1 STI1 domain. Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Technical term	3D-structure
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DSP	P15924	1	EBI-749370,EBI-355041
EIF4EBP1	Q13541	1	EBI-749370,EBI-74090
IQGAP2	Q13576	1	EBI-749370,EBI-357571
MED7	O43513	1	EBI-749370,EBI-394632
MYH2	Q9UKX2	1	EBI-749370,EBI-1049626
RNF123	Q5XPI4	1	EBI-749370,EBI-1057418

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 405

405

Ubiquitin-associated domain-containing protein 1

PRO_0000250449

Regions

Domain

14 – 98

85

Ubiquitin-like

Domain

187 – 231

45

UBA 1

Domain

288 – 328

41

UBA 2

Domain

353 – 392

40

STI1

Natural variations

Natural variant

374

1

E → D: dbSNP rs11103231.

VAR_027562

Experimental info

Sequence conflict

244

1

Q → R in AAC21559. Ref.4

Sequence conflict

269

1

Missing in AAD51084. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

405

Helix Strand Turn

Details...

Beta strand

189 – 191

3

Helix

194 – 203

10

Helix

207 – 216

10

Helix

221 – 230

10

Helix

231 – 233

3

Sequences

	Sequence		Length	Mass (Da)
	Q9BSL1-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5FC8EC84A8602CBE	FASTA	405	45,338
	10 20 30 40 50 60 MFVQEEKIFA GKVLRLHICA SDGAEWLEEA TEDTSVEKLK ERCLKHCAHG SLEDPKSITH 70 80 90 100 110 120 HKLIHAASER VLSDARTILE ENIQDQDVLL LIKKRAPSPL PKMADVSAEE KKKQDQKAPD 130 140 150 160 170 180 KEAILRATAN LPSYNMDRAA VQTNMRDFQT ELRKILVSLI EVAQKLLALN PDAVELFKKA 190 200 210 220 230 240 NAMLDEDEDE RVDEAALRQL TEMGFPENRA TKALQLNHMS VPQAMEWLIE HAEDPTIDTP 250 260 270 280 290 300 LPGQAPPEAE GATAAASEAA AGASATDEEA RDELTEIFKK IRRKREFRAD ARAVISLMEM 310 320 330 340 350 360 GFDEKEVIDA LRVNNNQQNA ACEWLLGDRK PSPEELDKGI DPDSPLFQAI LDNPVVQLGL 370 380 390 400 TNPKTLLAFE DMLENPLNST QWMNDPETGP VMLQISRIFQ TLNRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10857748] [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: 15164053] [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: 15489334] [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: 15531880] [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: 15746103] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00305442.

RefSeq

NP_057256.2.

UniGene

Hs.9194

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DAI	NMR	-	A	172-241	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BSL1. 11 interactions.

Proteomic databases

PeptideAtlas

Q9BSL1.

PRIDE

Q9BSL1.

Genome annotation databases

Ensembl

ENSG00000130560. Homo sapiens. [Contig view]

GeneID

10422.

KEGG

hsa:10422.

Organism-specific databases

GeneCards

GC09M137965.

HGNC

HGNC:30221. UBAC1.

MIM

608129. gene.

PharmGKB

PA134952947.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9BSL1.

OMA

Q9BSL1. IRRKREF.

Gene expression databases

ArrayExpress

Q9BSL1.

Bgee

Q9BSL1.

CleanEx

HS_UBAC1.

GermOnline

ENSG00000130560. Homo sapiens.

Family and domain databases

InterPro

IPR006636. STI1_HS_bd.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]

Pfam

PF00627. UBA. 2 hits.
[Graphical view]

SMART

SM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
[Graphical view]

PROSITE

PS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

39500.

SOURCE

Search...

Entry information

Entry name

UBAC1_HUMAN

Accession

Primary (citable) accession number: Q9BSL1
Secondary accession number(s): O75500, Q9UMW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)