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P51572

- BAP31_HUMAN

UniProt

P51572 - BAP31_HUMAN

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Protein

B-cell receptor-associated protein 31

Gene
BCAP31, BAP31, DXS1357E
Organism
Homo sapiens (Human)
Status
Reviewed - 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-8 Reviewed prediction
Sitei238 – 2392Cleavage; by caspase-8 Reviewed prediction

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  2. apoptotic process Source: Reactome
  3. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. immune response Source: Ensembl
  6. intracellular protein transport Source: InterPro
  7. negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProtKB
  8. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  9. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  10. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  11. positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  12. spermatogenesis Source: Ensembl
  13. vesicle-mediated transport Source: UniProtKB-KW
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: Chromosome X

Organism-specific databases

HGNCiHGNC:16695. BCAP31.

Subcellular locationi

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.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 65Lumenal Reviewed prediction
Transmembranei7 – 2721Helical; Reviewed predictionAdd
BLAST
Topological domaini28 – 4316Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei44 – 6421Helical; Reviewed predictionAdd
BLAST
Topological domaini65 – 10238Lumenal Reviewed predictionAdd
BLAST
Transmembranei103 – 12321Helical; Reviewed predictionAdd
BLAST
Topological domaini124 – 246123Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  4. endoplasmic reticulum membrane Source: Reactome
  5. Golgi membrane Source: Ensembl
  6. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  7. integral component of plasma membrane Source: UniProtKB
  8. lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, dystonia, and cerebral hypomyelination (DDCH) [MIM:300475]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.

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

ArrayExpressiP51572.
BgeeiP51572.
CleanExiHS_BCAP31.
GenevestigatoriP51572.

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 PTPLB.3 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
PTPLBQ6Y1H24EBI-77683,EBI-530257
SEC61BP604687EBI-77683,EBI-1788819
TRAM1Q156295EBI-77683,EBI-1788852

Protein-protein interaction databases

BioGridi115437. 42 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 – 21950

3D structure databases

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

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the BCAP29/BCAP31 family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG244998.
HOGENOMiHOG000204790.
HOVERGENiHBG050661.
InParanoidiP51572.
KOiK14009.
OMAiHSMRLFR.
PhylomeDBiP51572.
TreeFamiTF315310.

Family and domain databases

InterProiIPR008417. BAP29/BAP31.
[Graphical view]
PANTHERiPTHR12701. PTHR12701. 1 hit.
PfamiPF05529. Bap31. 1 hit.
[Graphical view]

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. Align

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

MSLQWTAVAT FLYAEVFVVL LLCIPFISPK RWQKIFKSRL VELLVSYGNT    50
FFVVLIVILV LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ 100
RNLYIAGFSL LLSFLLRRLV TLISQQATLL ASNEAFKKQA ESASEAAKKY 150
MEENDQLKKG AAVDGGKLDV GNAEVKLEEE NRSLKADLQK LKDELASTKQ 200
KLEKAENQVL AMRKQSEGLT KEYDRLLEEH AKLQAAVDGP MDKKEE 246
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGAEASSSWCPGTALPEERL SVKRASEISGFLGQGSSGEA ALDVLTHVLEGAGNKLTSSC GKPSSNRM in isoform 2. VSP_043116

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → T in CAA57415. 1 Publication
Sequence conflicti72 – 721K → E in AAH14323. 1 Publication
Sequence conflicti208 – 2081Q → E in CAA57415. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [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]
GeneIDi10134.
KEGGihsa:10134.
UCSCiuc004fid.3. human. [P51572-2]
uc004fie.2. human. [P51572-1]

Polymorphism databases

DMDMi1705725.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14727.1. [P51572-1 ]
CCDS48191.1. [P51572-2 ]
PIRi S44279.
RefSeqi NP_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 ]
UniGenei Hs.522817.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JZL X-ray 2.20 A/B/C/D 168-233 [» ]
4JZP X-ray 2.10 A/B 168-233 [» ]
ProteinModelPortali P51572.
SMRi P51572. Positions 172-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115437. 42 interactions.
IntActi P51572. 23 interactions.
MINTi MINT-3018869.
STRINGi 9606.ENSP00000392330.

Protein family/group databases

TCDBi 3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

PhosphoSitei P51572.

Polymorphism databases

DMDMi 1705725.

Proteomic databases

MaxQBi P51572.
PaxDbi P51572.
PRIDEi P51572.

Protocols and materials databases

DNASUi 10134.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345046 ; 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 ]
GeneIDi 10134.
KEGGi hsa:10134.
UCSCi uc004fid.3. human. [P51572-2 ]
uc004fie.2. human. [P51572-1 ]

Organism-specific databases

CTDi 10134.
GeneCardsi GC0XM152965.
HGNCi HGNC:16695. BCAP31.
HPAi CAB015350.
CAB015424.
HPA003906.
MIMi 300398. gene.
300475. phenotype.
neXtProti NX_P51572.
Orphaneti 369942. CADDS.
369939. Severe motor and intellectual disabilities-sensorineural deafness-dystonia syndrome.
PharmGKBi PA128394569.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG244998.
HOGENOMi HOG000204790.
HOVERGENi HBG050661.
InParanoidi P51572.
KOi K14009.
OMAi HSMRLFR.
PhylomeDBi P51572.
TreeFami TF315310.

Enzyme and pathway databases

Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSi BCAP31. human.
GeneWikii BCAP31.
GenomeRNAii 10134.
NextBioi 38337.
PMAP-CutDB P51572.
PROi P51572.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51572.
Bgeei P51572.
CleanExi HS_BCAP31.
Genevestigatori P51572.

Family and domain databases

InterProi IPR008417. BAP29/BAP31.
[Graphical view ]
PANTHERi PTHR12701. PTHR12701. 1 hit.
Pfami PF05529. Bap31. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 PTPLB.
  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.

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: September 3, 2014
This is version 140 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

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