Reviewed, UniProtKB/Swiss-Prot P51572 (BAP31_HUMAN)

Names and origin

Protein names

Recommended name:
    B-cell receptor-associated protein 31
Alternative name(s):
    BCR-associated protein Bap31
    p28 Bap31
    Protein CDM
    6C6-AG tumor-associated antigen

Gene names

Name:	BCAP31
Synonyms:	BAP31, DXS1357E

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.8 Ref.9
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.7 Ref.10 Ref.11
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.8 Ref.7
Tissue specificity	Ubiquitous.
Post-translational modification	Cleaved by CASP8 and other caspases.
Involvement in disease	Microdeletions in BCAP31 are involved in the contiguous ABCD1/DXS1375E deletion syndrome (CADDS) [MIM:300475]. Patients manifest profound neonatal hypotonia, subsequent failure to thrive, and cholestatic liver disease.
Sequence similarities	Belongs to the BCAP29/BCAP31 family.

Ontologies

Keywords
Biological process	Apoptosis ER-Golgi transport Protein transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW immune response Non-traceable author statement. Source: UniProtKB intracellular protein transport Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ER-Golgi intermediate compartment membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	receptor binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2	P10415	2	EBI-77683,EBI-77694
BCL2L1	Q07817	1	EBI-77683,EBI-78035
CASP8	Q14790	1	EBI-77683,EBI-78060
CASP8	Q14790-9	1	EBI-77683,EBI-288343
CFTR	P13569	2	EBI-77683,EBI-349854
DERL1	Q9BUN8	1	EBI-77683,EBI-398977
PTPLB	Q6Y1H2	1	EBI-77683,EBI-530257
SEC61B	P60468	3	EBI-77683,EBI-1788819
TRAM1	Q15629	2	EBI-77683,EBI-1788852

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 246	245	B-cell receptor-associated protein 31		PRO_0000142891
Regions
	Topological domain	2 – 6	5	Lumenal Potential
	Transmembrane	7 – 27	21	Potential
	Topological domain	28 – 43	16	Cytoplasmic Potential
	Transmembrane	44 – 64	21	Potential
	Topological domain	65 – 102	38	Lumenal Potential
	Transmembrane	103 – 123	21	Potential
	Topological domain	124 – 246	123	Cytoplasmic Potential
	Motif	243 – 246	4	Di-lysine motif
Sites
	Site	164 – 165	2	Cleavage; by caspase-8 Potential
	Site	238 – 239	2	Cleavage; by caspase-8 Potential
Experimental info
	Mutagenesis	164	1	D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-238. Ref.9
	Mutagenesis	238	1	D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-164. Ref.9
	Sequence conflict	2	1	S → T in CAA57415. Ref.3
	Sequence conflict	72	1	K → E in AAH14323. Ref.5
	Sequence conflict	208	1	Q → E in CAA57415. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P51572-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D34367F870D6EB00	FASTA	246	27,992
	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

References

	« Hide 'large scale' referencesShow '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: 7806238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8706661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8612576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell and Promyelocytic leukemia.
[4]	"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. , 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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 Pancreas.
[6]	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.
[7]	"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: 9334338] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, SUBCELLULAR LOCATION, INTERACTION WITH BCL2; BCL2L1 AND CASP8.
[8]	"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: 9396746] [Abstract] Cited for: PROTEIN SEQUENCE OF 80-96 AND 205-214, SUBCELLULAR LOCATION, FUNCTION.
[9]	"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: 10958671] [Abstract] Cited for: MUTAGENESIS OF ASP-164 AND ASP-238, ROLE IN APOPTOSIS.
[10]	"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: 11917123] [Abstract] Cited for: INTERACTION WITH CASP8 ISOFORM 9.
[11]	"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: 15024066] [Abstract] Cited for: INTERACTION WITH PTPLB.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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: 11992258] [Abstract] Cited for: INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z31696 mRNA. Translation: CAA83501.1. X81109 mRNA. Translation: CAA57015.1. X81817 mRNA. Translation: CAA57415.1. U52111 Genomic DNA. No translation available. BC014323 mRNA. Translation: AAH14323.1. BC065292 mRNA. Translation: AAH65292.1. U36341 Genomic DNA. Translation: AAA79508.1.
IPI	IPI00218200.
PIR	S44279.
RefSeq	NP_001132913.1. NP_005736.3.
UniGene	Hs.522817
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P51572. 13 interactions.
Proteomic databases
PRIDE	P51572.
Genome annotation databases
Ensembl	ENSG00000185825. Homo sapiens. [Contig view]
GeneID	10134.
KEGG	hsa:10134.
UCSC	uc004fid.1. human.
Organism-specific databases
GeneCards	GC0XM152619.
H-InvDB	HIX0017135.
HGNC	HGNC:16695. BCAP31.
HPA	CAB015350. CAB015424. HPA003906.
MIM	300398. gene. 300475. phenotype.
PharmGKB	PA128394569.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P51572.
HOVERGEN	P51572.
OMA	P51572. NDQLKKG.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P51572.
Bgee	P51572.
CleanEx	HS_BCAP31.
GermOnline	ENSG00000185825. Homo sapiens.
Family and domain databases
InterPro	IPR008417. Bap31. [Graphical view]
PANTHER	PTHR12701. Bap31. 1 hit.
Pfam	PF05529. Bap31. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	38337.
PMAP-CutDB	P51572.
SOURCE	Search...

Entry information

Entry name

BAP31_HUMAN

Accession

Primary (citable) accession number: P51572
Secondary accession number(s): Q13836, Q96CF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)