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Protein

B-cell receptor-associated protein 31

Gene

BCAP31

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8-mediated apoptosis.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei164 – 1652Cleavage; by caspase-8Sequence Analysis
Sitei238 – 2392Cleavage; by caspase-8Sequence Analysis

GO - Biological processi

  • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  • apoptotic process Source: Reactome
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • ER to Golgi vesicle-mediated transport Source: Ensembl
  • intracellular protein transport Source: InterPro
  • negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  • positive regulation of retrograde protein transport, ER to cytosol Source: ParkinsonsUK-UCL
  • programmed cell death Source: Reactome
  • protein localization to endoplasmic reticulum exit site Source: Ensembl
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis, ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Protein family/group databases

TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:BCAP31
Synonyms:BAP31, DXS1357E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:16695. BCAP31.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 65LumenalSequence Analysis
Transmembranei7 – 2721HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 4316CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei44 – 6421HelicalSequence AnalysisAdd
BLAST
Topological domaini65 – 10238LumenalSequence AnalysisAdd
BLAST
Transmembranei103 – 12321HelicalSequence AnalysisAdd
BLAST
Topological domaini124 – 246123CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • clathrin-coated vesicle Source: Ensembl
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi cisterna membrane Source: Ensembl
  • integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  • integral component of plasma membrane Source: UniProtKB
  • lipid particle Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, dystonia, and cerebral hypomyelination (DDCH)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn X-linked recessive mental retardation syndrome characterized by almost no psychomotor development, dysmorphic facial features, sensorineural deafness, dystonia, pyramidal signs, and hypomyelination on brain imaging.

See also OMIM:300475

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-238. 1 Publication
Mutagenesisi238 – 2381D → A: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-164. 1 Publication

Keywords - Diseasei

Deafness, Dystonia, Mental retardation

Organism-specific databases

MIMi300475. phenotype.
Orphaneti369942. CADDS.
369939. Severe motor and intellectual disabilities-sensorineural deafness-dystonia syndrome.
PharmGKBiPA128394569.

Polymorphism and mutation databases

BioMutaiBCAP31.
DMDMi1705725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 246245B-cell receptor-associated protein 31PRO_0000142891Add
BLAST

Post-translational modificationi

Cleaved by CASP8 and other caspases.

Proteomic databases

MaxQBiP51572.
PaxDbiP51572.
PRIDEiP51572.

PTM databases

PhosphoSiteiP51572.

Miscellaneous databases

PMAP-CutDBP51572.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in neurons and discrete endocrine cells.1 Publication

Gene expression databases

BgeeiP51572.
CleanExiHS_BCAP31.
ExpressionAtlasiP51572. baseline and differential.
GenevisibleiP51572. HS.

Organism-specific databases

HPAiCAB015350.
CAB015424.
HPA003906.

Interactioni

Subunit structurei

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 HACD2 (PubMed:15024066).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2P104152EBI-77683,EBI-77694
CASP8Q147903EBI-77683,EBI-78060
CFTRP135693EBI-77683,EBI-349854
DERL1Q9BUN83EBI-77683,EBI-398977
FIS1Q9Y3D68EBI-77683,EBI-3385283
HACD2Q6Y1H24EBI-77683,EBI-530257
SEC61BP604687EBI-77683,EBI-1788819
TRAM1Q156295EBI-77683,EBI-1788852

Protein-protein interaction databases

BioGridi115437. 46 interactions.
IntActiP51572. 23 interactions.
MINTiMINT-3018869.
STRINGi9606.ENSP00000392330.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi170 – 21950Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JZLX-ray2.20A/B/C/D168-233[»]
4JZPX-ray2.10A/B168-233[»]
ProteinModelPortaliP51572.
SMRiP51572. Positions 172-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili165 – 237731 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi243 – 2464Di-lysine motif

Sequence similaritiesi

Belongs to the BCAP29/BCAP31 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG244998.
GeneTreeiENSGT00390000011863.
HOGENOMiHOG000204790.
HOVERGENiHBG050661.
InParanoidiP51572.
KOiK14009.
OMAiLNVEMQH.
PhylomeDBiP51572.
TreeFamiTF315310.

Family and domain databases

InterProiIPR008417. BAP29/BAP31.
[Graphical view]
PANTHERiPTHR12701. PTHR12701. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51572-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLQWTAVAT FLYAEVFVVL LLCIPFISPK RWQKIFKSRL VELLVSYGNT
60 70 80 90 100
FFVVLIVILV LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ
110 120 130 140 150
RNLYIAGFSL LLSFLLRRLV TLISQQATLL ASNEAFKKQA ESASEAAKKY
160 170 180 190 200
MEENDQLKKG AAVDGGKLDV GNAEVKLEEE NRSLKADLQK LKDELASTKQ
210 220 230 240
KLEKAENQVL AMRKQSEGLT KEYDRLLEEH AKLQAAVDGP MDKKEE
Length:246
Mass (Da):27,992
Last modified:January 23, 2007 - v3
Checksum:iD34367F870D6EB00
GO
Isoform 2 (identifier: P51572-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGAEASSSWCPGTALPEERLSVKRASEISGFLGQGSSGEAALDVLTHVLEGAGNKLTSSCGKPSSNRM

Note: No experimental confirmation available.
Show »
Length:313
Mass (Da):34,752
Checksum:iA92BFA18452A46A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → T in CAA57415 (PubMed:8612576).Curated
Sequence conflicti72 – 721K → E in AAH14323 (PubMed:15489334).Curated
Sequence conflicti208 – 2081Q → E in CAA57415 (PubMed:8612576).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGAEASSSWCPGTALPEERL SVKRASEISGFLGQGSSGEA ALDVLTHVLEGAGNKLTSSC GKPSSNRM in isoform 2. 1 PublicationVSP_043116

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14727.1. [P51572-1]
CCDS48191.1. [P51572-2]
PIRiS44279.
RefSeqiNP_001132913.1. NM_001139441.1. [P51572-1]
NP_001132929.1. NM_001139457.2. [P51572-2]
NP_001243376.1. NM_001256447.1. [P51572-1]
NP_005736.3. NM_005745.7. [P51572-1]
UniGeneiHs.522817.

Genome annotation databases

EnsembliENST00000345046; ENSP00000343458; ENSG00000185825.
ENST00000458587; ENSP00000392330; ENSG00000185825. [P51572-2]
GeneIDi10134.
KEGGihsa:10134.
UCSCiuc004fid.3. human. [P51572-2]
uc004fie.2. human. [P51572-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14727.1. [P51572-1]
CCDS48191.1. [P51572-2]
PIRiS44279.
RefSeqiNP_001132913.1. NM_001139441.1. [P51572-1]
NP_001132929.1. NM_001139457.2. [P51572-2]
NP_001243376.1. NM_001256447.1. [P51572-1]
NP_005736.3. NM_005745.7. [P51572-1]
UniGeneiHs.522817.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JZLX-ray2.20A/B/C/D168-233[»]
4JZPX-ray2.10A/B168-233[»]
ProteinModelPortaliP51572.
SMRiP51572. Positions 172-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115437. 46 interactions.
IntActiP51572. 23 interactions.
MINTiMINT-3018869.
STRINGi9606.ENSP00000392330.

Protein family/group databases

TCDBi3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSiteiP51572.

Polymorphism and mutation databases

BioMutaiBCAP31.
DMDMi1705725.

Proteomic databases

MaxQBiP51572.
PaxDbiP51572.
PRIDEiP51572.

Protocols and materials databases

DNASUi10134.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345046; ENSP00000343458; ENSG00000185825.
ENST00000458587; ENSP00000392330; ENSG00000185825. [P51572-2]
GeneIDi10134.
KEGGihsa:10134.
UCSCiuc004fid.3. human. [P51572-2]
uc004fie.2. human. [P51572-1]

Organism-specific databases

CTDi10134.
GeneCardsiGC0XM152965.
HGNCiHGNC:16695. BCAP31.
HPAiCAB015350.
CAB015424.
HPA003906.
MIMi300398. gene.
300475. phenotype.
neXtProtiNX_P51572.
Orphaneti369942. CADDS.
369939. Severe motor and intellectual disabilities-sensorineural deafness-dystonia syndrome.
PharmGKBiPA128394569.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244998.
GeneTreeiENSGT00390000011863.
HOGENOMiHOG000204790.
HOVERGENiHBG050661.
InParanoidiP51572.
KOiK14009.
OMAiLNVEMQH.
PhylomeDBiP51572.
TreeFamiTF315310.

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiBCAP31. human.
GeneWikiiBCAP31.
GenomeRNAii10134.
NextBioi38337.
PMAP-CutDBP51572.
PROiP51572.
SOURCEiSearch...

Gene expression databases

BgeeiP51572.
CleanExiHS_BCAP31.
ExpressionAtlasiP51572. baseline and differential.
GenevisibleiP51572. HS.

Family and domain databases

InterProiIPR008417. BAP29/BAP31.
[Graphical view]
PANTHERiPTHR12701. PTHR12701. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: SUBCELLULAR LOCATION.
  13. "Endoplasmic reticulum membrane-sorting protein of lymphocytes (BAP31) is highly expressed in neurons and discrete endocrine cells."
    Manley H.A., Lennon V.A.
    J. Histochem. Cytochem. 49:1235-1243(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "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.
  15. "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 HACD2.
  16. "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.
  17. "Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated Degradation."
    Wakana Y., Takai S., Nakajima K., Tani K., Yamamoto A., Watson P., Stephens D.J., Hauri H.P., Tagaya M.
    Mol. Biol. Cell 19:1825-1836(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Mutations in BCAP31 cause a severe X-linked phenotype with deafness, dystonia, and central hypomyelination and disorganize the Golgi apparatus."
    Cacciagli P., Sutera-Sardo J., Borges-Correia A., Roux J.C., Dorboz I., Desvignes J.P., Badens C., Delepine M., Lathrop M., Cau P., Levy N., Girard N., Sarda P., Boespflug-Tanguy O., Villard L.
    Am. J. Hum. Genet. 93:579-586(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DDCH.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Structural and biophysical characterization of the cytoplasmic domains of human BAP29 and BAP31."
    Quistgaard E.M., Low C., Moberg P., Guettou F., Maddi K., Nordlund P.
    PLoS ONE 8:E71111-E71111(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 168-233, SUBUNIT, COILED-COIL.

Entry informationi

Entry nameiBAP31_HUMAN
AccessioniPrimary (citable) accession number: P51572
Secondary accession number(s): B3KQ79
, D3DWV5, Q13836, Q96CF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.