P51572 (BAP31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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 process	Apoptosis ER-Golgi transport Protein transport Transport
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen 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 elevation of cytosolic calcium ion concentration Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB elevation of mitochondrial calcium ion concentration Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB immune response Non-traceable author statement. Source: UniProtKB intracellular protein transport Inferred from electronic annotation. Source: InterPro positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB positive regulation of intrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB reduction of endoplasmic reticulum calcium ion concentration Inferred from mutant phenotype PubMed 21183955. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Compara vesicle-mediated transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome endoplasmic reticulum-Golgi intermediate compartment membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB lipid particle Inferred from direct assay PubMed 14741744. 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
CASP8	Q14790	3	EBI-77683,EBI-78060
CFTR	P13569	3	EBI-77683,EBI-349854
DERL1	Q9BUN8	3	EBI-77683,EBI-398977
FIS1	Q9Y3D6	8	EBI-77683,EBI-3385283
PTPLB	Q6Y1H2	4	EBI-77683,EBI-530257
SEC61B	P60468	7	EBI-77683,EBI-1788819
TRAM1	Q15629	5	EBI-77683,EBI-1788852

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 246	245	B-cell receptor-associated protein 31		PRO_0000142891
Regions
	Topological domain	2 – 6	5	Lumenal Potential
	Transmembrane	7 – 27	21	Helical; Potential
	Topological domain	28 – 43	16	Cytoplasmic Potential
	Transmembrane	44 – 64	21	Helical; Potential
	Topological domain	65 – 102	38	Lumenal Potential
	Transmembrane	103 – 123	21	Helical; 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
Natural variations
	Alternative sequence	1	1	M → MGAEASSSWCPGTALPEERL SVKRASEISGFLGQGSSGEA ALDVLTHVLEGAGNKLTSSC GKPSSNRM in isoform 2.		VSP_043116
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.11
	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.11
	Sequence conflict	2	1	S → T in CAA57415. Ref.3
	Sequence conflict	72	1	K → E in AAH14323. Ref.7
	Sequence conflict	208	1	Q → E in CAA57415. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: A92BFA18452A46A7	FASTA	313	34,752
	10 20 30 40 50 60 MGAEASSSWC PGTALPEERL SVKRASEISG FLGQGSSGEA ALDVLTHVLE GAGNKLTSSC 70 80 90 100 110 120 GKPSSNRMSL QWTAVATFLY AEVFVVLLLC IPFISPKRWQ KIFKSRLVEL LVSYGNTFFV 130 140 150 160 170 180 VLIVILVLLV IDAVREIRKY DDVTEKVNLQ NNPGAMEHFH MKLFRAQRNL YIAGFSLLLS 190 200 210 220 230 240 FLLRRLVTLI SQQATLLASN EAFKKQAESA SEAAKKYMEE NDQLKKGAAV DGGKLDVGNA 250 260 270 280 290 300 EVKLEEENRS LKADLQKLKD ELASTKQKLE KAENQVLAMR KQSEGLTKEY DRLLEEHAKL 310 QAAVDGPMDK KEE

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] [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. , 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. , 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. , 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.
IPI	IPI00218200.
PIR	S44279.
RefSeq	NP_001132913.1. NM_001139441.1. NP_001132929.1. NM_001139457.2. NP_001243376.1. NM_001256447.1. NP_005736.3. NM_005745.7.
UniGene	Hs.522817.
3D structure databases
ProteinModelPortal	P51572.
SMR	P51572. Positions 175-214.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51572. 20 interactions.
MINT	MINT-3018869.
STRING	9606.ENSP00000392330.
Protein family/group databases
TCDB	3.A.5.9.1. general secretory pathway (Sec) family.
PTM databases
PhosphoSite	P51572.
Polymorphism databases
DMDM	1705725.
Proteomic databases
PaxDb	P51572.
PRIDE	P51572.
Protocols and materials databases
DNASU	10134.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000345046; ENSP00000343458; ENSG00000185825. ENST00000441714; ENSP00000405417; ENSG00000185825. ENST00000458587; ENSP00000392330; ENSG00000185825. ENST00000596601; ENSP00000473146; ENSG00000267977. ENST00000597329; ENSP00000472030; ENSG00000267977. ENST00000600824; ENSP00000472405; ENSG00000267977.
GeneID	10134.
KEGG	hsa:10134.
UCSC	uc004fie.2. human.
Organism-specific databases
CTD	10134.
GeneCards	GC0XM152965.
HGNC	HGNC:16695. BCAP31.
HPA	CAB015350. CAB015424. HPA003906.
MIM	300398. gene.
neXtProt	NX_P51572.
PharmGKB	PA128394569.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG244998.
HOGENOM	HOG000204790.
HOVERGEN	HBG050661.
InParanoid	P51572.
KO	K14009.
OMA	SYGNTFF.
OrthoDB	EOG405S2D.
PhylomeDB	P51572.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P51572.
Bgee	P51572.
CleanEx	HS_BCAP31.
Genevestigator	P51572.
GermOnline	ENSG00000185825. Homo sapiens.
Family and domain databases
InterPro	IPR008417. Bap31. [Graphical view]
PANTHER	PTHR12701. PTHR12701. 1 hit.
Pfam	PF05529. Bap31. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BCAP31. human.
GenomeRNAi	10134.
NextBio	38337.
PMAP-CutDB	P51572.
SOURCE	Search...

Entry information

Entry name

BAP31_HUMAN

Accession

Primary (citable) accession number: P51572
Secondary accession number(s): B3KQ79 , D3DWV5, Q13836, Q96CF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.