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P51572 (BAP31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 135. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B-cell receptor-associated protein 31

Short name=BCR-associated protein 31
Short name=Bap31
Alternative name(s):
6C6-AG tumor-associated antigen
Protein CDM
p28
Gene names
Name:BCAP31
Synonyms:BAP31, DXS1357E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis. Ref.10 Ref.11

Subunit structure

Homodimer and heterodimer with BCAP29. Binds CASP8 (isoform 9)as a complex containing BCAP31, BCAP29, BCL2 and/or BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD immunoglobulins. May interact with ACTG1 and non-muscle myosin II. Interacts with PTPLB. Ref.9 Ref.12 Ref.13

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Note: May shuttle between the ER and the intermediate compartment/cis-Golgi complex. Ref.9 Ref.10

Tissue specificity

Ubiquitous.

Post-translational modification

Cleaved by CASP8 and other caspases.

Involvement in disease

BCAP31 is deleted in the chromosome Xq28 deletion syndrome which involves BCAP31 and the and the promoter region of ABCD1.

Sequence similarities

Belongs to the BCAP29/BCAP31 family.

Ontologies

Keywords
   Biological processApoptosis
ER-Golgi transport
Protein transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

calcium-mediated signaling using intracellular calcium source

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

immune response

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

negative regulation of endoplasmic reticulum calcium ion concentration

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

positive regulation of mitochondrial calcium ion concentration

Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

lipid particle

Inferred from direct assay PubMed 14741744. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51572-1)

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: P51572-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGAEASSSWCPGTALPEERLSVKRASEISGFLGQGSSGEAALDVLTHVLEGAGNKLTSSCGKPSSNRM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 246245B-cell receptor-associated protein 31
PRO_0000142891

Regions

Topological domain2 – 65Lumenal Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 4316Cytoplasmic Potential
Transmembrane44 – 6421Helical; Potential
Topological domain65 – 10238Lumenal Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 246123Cytoplasmic Potential
Motif243 – 2464Di-lysine motif

Sites

Site164 – 1652Cleavage; by caspase-8 Potential
Site238 – 2392Cleavage; by caspase-8 Potential

Natural variations

Alternative sequence11M → MGAEASSSWCPGTALPEERL SVKRASEISGFLGQGSSGEA ALDVLTHVLEGAGNKLTSSC GKPSSNRM in isoform 2.
VSP_043116

Experimental info

Mutagenesis1641D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-238. Ref.11
Mutagenesis2381D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-164. Ref.11
Sequence conflict21S → T in CAA57415. Ref.3
Sequence conflict721K → E in AAH14323. Ref.7
Sequence conflict2081Q → E in CAA57415. Ref.3

Secondary structure

... 246
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: D34367F870D6EB00

FASTA24627,992
        10         20         30         40         50         60 
MSLQWTAVAT FLYAEVFVVL LLCIPFISPK RWQKIFKSRL VELLVSYGNT FFVVLIVILV 

        70         80         90        100        110        120 
LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ RNLYIAGFSL LLSFLLRRLV 

       130        140        150        160        170        180 
TLISQQATLL ASNEAFKKQA ESASEAAKKY MEENDQLKKG AAVDGGKLDV GNAEVKLEEE 

       190        200        210        220        230        240 
NRSLKADLQK LKDELASTKQ KLEKAENQVL AMRKQSEGLT KEYDRLLEEH AKLQAAVDGP 


MDKKEE 

« Hide

Isoform 2 [UniParc].

Checksum: A92BFA18452A46A7
Show »

FASTA31334,752

References

« Hide 'large scale' references
[1]"A new human gene (DXS1357E) with ubiquitous expression, located in Xq28 adjacent to the adrenoleukodystrophy gene."
Mosser J., Sarde C.-O., Vicaire S., Yates J.R., Mandel J.-L.
Genomics 22:469-471(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and characterization of a transmembrane surface antigen in human cells."
Li E., Bestagno M., Burrone O.
Eur. J. Biochem. 238:631-638(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The specificity of association of the IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD transmembrane sequence."
Adachi T., Schamel W.W.A., Kim K.-M., Watanabe T., Becker B., Nielsen P.J., Reth M.
EMBO J. 15:1534-1541(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: B-cell and Promyelocytic leukemia.
[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. expand/collapse author list , 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 2).
Tissue: Stomach and Trachea.
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Lung and Pancreas.
[8]Eichler E.E., Lu F., Shen Y., Muzny D.M., Gibbs R.A., Nelson D.L.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-246.
[9]"p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum."
Ng F.W.H., Nguyen M., Kwan T., Branton P.E., Nicholson D.W., Cromlish J.A., Shore G.C.
J. Cell Biol. 139:327-338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, SUBCELLULAR LOCATION, INTERACTION WITH BCL2; BCL2L1 AND CASP8.
[10]"Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31."
Annaert W.G., Becker B., Kistner U., Reth M., Jahn R.
J. Cell Biol. 139:1397-1410(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-96 AND 205-214, SUBCELLULAR LOCATION, FUNCTION.
[11]"Caspase-resistant BAP31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria."
Nguyen M., Breckenridge D.G., Ducret A., Shore G.C.
Mol. Cell. Biol. 20:6731-6740(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-164 AND ASP-238, ROLE IN APOPTOSIS.
[12]"The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum."
Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C.
Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP8 ISOFORM 9.
[13]"The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B."
Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.
Mol. Cell. Biol. 24:2767-2778(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPLB.
[14]"Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) and DXS1357E: a novel neonatal phenotype similar to peroxisomal biogenesis disorders."
Corzo D., Gibson W., Johnson K., Mitchell G., LePage G., Cox G.F., Casey R., Zeiss C., Tyson H., Cutting G.R., Raymond G.V., Smith K.D., Watkins P.A., Moser A.B., Moser H.W., Steinberg S.J.
Am. J. Hum. Genet. 70:1520-1531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME.
[15]"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
Z31696 mRNA. Translation: CAA83501.1.
X81109 mRNA. Translation: CAA57015.1.
X81817 mRNA. Translation: CAA57415.1.
AK057613 mRNA. Translation: BAG51941.1.
AK125631 mRNA. Translation: BAG54226.1.
U52111 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72818.1.
CH471172 Genomic DNA. Translation: EAW72819.1.
CH471172 Genomic DNA. Translation: EAW72820.1.
CH471172 Genomic DNA. Translation: EAW72821.1.
CH471172 Genomic DNA. Translation: EAW72823.1.
CH471172 Genomic DNA. Translation: EAW72824.1.
CH471172 Genomic DNA. Translation: EAW72825.1.
BC014323 mRNA. Translation: AAH14323.1.
BC065292 mRNA. Translation: AAH65292.1.
U36341 Genomic DNA. Translation: AAA79508.1.
PIRS44279.
RefSeqNP_001132913.1. NM_001139441.1.
NP_001132929.1. NM_001139457.2.
NP_001243376.1. NM_001256447.1.
NP_005736.3. NM_005745.7.
UniGeneHs.522817.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JZLX-ray2.20A/B/C/D168-233[»]
4JZPX-ray2.10A/B168-233[»]
ProteinModelPortalP51572.
SMRP51572. Positions 172-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115437. 40 interactions.
IntActP51572. 22 interactions.
MINTMINT-3018869.
STRING9606.ENSP00000392330.

Protein family/group databases

TCDB3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSiteP51572.

Polymorphism databases

DMDM1705725.

Proteomic databases

PaxDbP51572.
PRIDEP51572.

Protocols and materials databases

DNASU10134.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345046; ENSP00000343458; ENSG00000185825. [P51572-1]
ENST00000441714; ENSP00000405417; ENSG00000185825. [P51572-1]
ENST00000458587; ENSP00000392330; ENSG00000185825. [P51572-2]
ENST00000596601; ENSP00000473146; ENSG00000267977. [P51572-1]
ENST00000597329; ENSP00000472030; ENSG00000267977. [P51572-2]
ENST00000600824; ENSP00000472405; ENSG00000267977. [P51572-1]
GeneID10134.
KEGGhsa:10134.
UCSCuc004fid.3. human. [P51572-2]
uc004fie.2. human. [P51572-1]

Organism-specific databases

CTD10134.
GeneCardsGC0XM152965.
HGNCHGNC:16695. BCAP31.
HPACAB015350.
CAB015424.
HPA003906.
MIM300398. gene.
neXtProtNX_P51572.
Orphanet369942. CADDS.
369939. Severe motor and intellectual disabilities-sensorineural deafness-dystonia syndrome.
PharmGKBPA128394569.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244998.
HOGENOMHOG000204790.
HOVERGENHBG050661.
InParanoidP51572.
KOK14009.
OMAHSMRLFR.
PhylomeDBP51572.
TreeFamTF315310.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP51572.
BgeeP51572.
CleanExHS_BCAP31.
GenevestigatorP51572.

Family and domain databases

InterProIPR008417. Bap31.
[Graphical view]
PANTHERPTHR12701. PTHR12701. 1 hit.
PfamPF05529. Bap31. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCAP31. human.
GeneWikiBCAP31.
GenomeRNAi10134.
NextBio38337.
PMAP-CutDBP51572.
PROP51572.
SOURCESearch...

Entry information

Entry nameBAP31_HUMAN
AccessionPrimary (citable) accession number: P51572
Secondary accession number(s): B3KQ79 expand/collapse secondary AC list , D3DWV5, Q13836, Q96CF0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 135 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

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