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Q04323 (UBXN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UBX domain-containing protein 1
Alternative name(s):
SAPK substrate protein 1
UBA/UBX 33.3 kDa protein
Gene names
Name:UBXN1
Synonyms:SAKS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-binding protein that interacts with the BRCA1-BARD1 heterodimer, and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol.

Subunit structure

Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with HOMER2 By similarity. Interacts directly with VCP. Interacts with BRCA1 and BARD1; interaction takes place when BRCA1 is not autoubiquitinated but is strongly enhanced in the presence of autoubiquitinated BRCA1. Ref.3 Ref.5 Ref.9

Subcellular location

Cytoplasm By similarity.

Domain

The UBA domain specifically recognizes and binds 'Lys-6'-linked polyubiquitin chains. Ref.9

Sequence similarities

Contains 1 UBA domain.

Contains 1 UBX domain.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q04323-1)

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.
Isoform 2 (identifier: Q04323-2)

The sequence of this isoform differs from the canonical sequence as follows:
     283-297: LVPSAVLIVAKKCPS → MAARLETRTRNWGSREACLGKGGMQREGAL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 297296UBX domain-containing protein 1
PRO_0000211023

Regions

Domain2 – 4241UBA
Domain211 – 29383UBX
Region43 – 297255Interaction with BRCA1
Coiled coil87 – 17286 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue1991Phosphoserine Ref.6
Modified residue2001Phosphoserine; by MAPK12 Ref.3
Modified residue2701Phosphoserine Ref.8

Natural variations

Alternative sequence283 – 29715LVPSA…KKCPS → MAARLETRTRNWGSREACLG KGGMQREGAL in isoform 2.
VSP_020367
Natural variant561L → F.
Corresponds to variant rs11543359 [ dbSNP | Ensembl ].
VAR_057370

Experimental info

Mutagenesis131M → T: Abolishes binding to 'Lys-6'-linked polyubiquitin chains and ability to inhibit E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Ref.9
Mutagenesis2191R → A: Does not affect binding to 'Lys-6'-linked polyubiquitin chains and ability to inhibit E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Ref.9
Sequence conflict761G → A in AAA36396. Ref.1
Sequence conflict1481E → AE in AAA36396. Ref.1
Sequence conflict1541K → N in AAA36396. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: E4E0C8BBAC93F2BB

FASTA29733,325
        10         20         30         40         50         60 
MAELTALESL IEMGFPRGRA EKALALTGNQ GIEAAMDWLM EHEDDPDVDE PLETPLGHIL 

        70         80         90        100        110        120 
GREPTSSEQG GLEGSGSAAG EGKPALSEEE RQEQTKRMLE LVAQKQRERE EREEREALER 

       130        140        150        160        170        180 
ERQRRRQGQE LSAARQRLQE DEMRRAAEER RREKAEELAA RQRVREKIER DKAERAKKYG 

       190        200        210        220        230        240 
GSVGSQPPPV APEPGPVPSS PSQEPPTKRE YDQCRIQVRL PDGTSLTQTF RAREQLAAVR 

       250        260        270        280        290 
LYVELHRGEE LGGGQDPVQL LSGFPRRAFS EADMERPLQE LGLVPSAVLI VAKKCPS 

« Hide

Isoform 2 [UniParc].

Checksum: 75C94CB67C03EB78
Show »

FASTA31235,107

References

« Hide 'large scale' references
[1]Pollard K.M.
Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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] (ISOFORMS 1 AND 2).
Tissue: Colon, Placenta and Skin.
[3]"A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs."
McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.
Biochem. J. 384:391-400(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 220-231 AND 276-285, PHOSPHORYLATION AT SER-200, INTERACTION WITH VCP.
[4]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 220-231, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[5]"UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover."
Alexandru G., Graumann J., Smith G.T., Kolawa N.J., Fang R., Deshaies R.J.
Cell 134:804-816(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITIN-BINDING, INTERACTION WITH VCP.
[6]"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-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"The UBXN1 protein associates with autoubiquitinated forms of the BRCA1 tumor suppressor and inhibits its enzymatic function."
Wu-Baer F., Ludwig T., Baer R.
Mol. Cell. Biol. 30:2787-2798(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITIN-BINDING, DOMAIN UBA, INTERACTION WITH BRCA1 AND BARD1, MUTAGENESIS OF MET-13 AND ARG-219.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68864 mRNA. Translation: AAA36396.1.
BC000902 mRNA. Translation: AAH00902.1.
BC001372 mRNA. Translation: AAH01372.1.
BC040129 mRNA. Translation: AAH40129.1.
CCDSCCDS66105.1. [Q04323-1]
CCDS8029.1. [Q04323-2]
PIRS27965.
RefSeqNP_001273006.1. NM_001286077.1. [Q04323-1]
NP_001273007.1. NM_001286078.1.
NP_056937.2. NM_015853.4. [Q04323-2]
XP_005274090.1. XM_005274033.2. [Q04323-2]
UniGeneHs.351296.
Hs.731509.

3D structure databases

ProteinModelPortalQ04323.
SMRQ04323. Positions 2-55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119239. 90 interactions.
DIPDIP-29467N.
IntActQ04323. 30 interactions.
STRING9606.ENSP00000294119.

PTM databases

PhosphoSiteQ04323.

Polymorphism databases

DMDM30923268.

Proteomic databases

MaxQBQ04323.
PaxDbQ04323.
PeptideAtlasQ04323.
PRIDEQ04323.

Protocols and materials databases

DNASU51035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294119; ENSP00000294119; ENSG00000162191. [Q04323-2]
ENST00000301935; ENSP00000303991; ENSG00000162191. [Q04323-1]
GeneID51035.
KEGGhsa:51035.
UCSCuc001nuj.3. human. [Q04323-2]
uc001nul.2. human. [Q04323-1]

Organism-specific databases

CTD51035.
GeneCardsGC11M062477.
H-InvDBHIX0009719.
HGNCHGNC:18402. UBXN1.
HPAHPA012669.
neXtProtNX_Q04323.
PharmGKBPA162408336.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5207.
HOGENOMHOG000188321.
HOVERGENHBG082310.
OMAQWLEDNQ.
OrthoDBEOG7SR4PG.
PhylomeDBQ04323.
TreeFamTF313944.

Gene expression databases

ArrayExpressQ04323.
BgeeQ04323.
CleanExHS_UBXN1.
GenevestigatorQ04323.

Family and domain databases

InterProIPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamPF00627. UBA. 1 hit.
PF00789. UBX. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS50033. UBX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBXN1. human.
GenomeRNAi51035.
NextBio53592.
PROQ04323.

Entry information

Entry nameUBXN1_HUMAN
AccessionPrimary (citable) accession number: Q04323
Secondary accession number(s): Q9BV93, Q9BVV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 114 of the entry and version 2 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM