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P51572

- BAP31_HUMAN

UniProt

P51572 - BAP31_HUMAN

Protein

B-cell receptor-associated protein 31

Gene

BCAP31

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 - 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

    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

    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
    9. membrane Source: UniProtKB

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    BCAP31 is deleted in the chromosome Xq28 deletion syndrome which involves BCAP31 and the and the promoter region of ABCD1.1 Publication

    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.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
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 65LumenalSequence Analysis
    Topological domaini28 – 4316CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini65 – 10238LumenalSequence AnalysisAdd
    BLAST
    Topological domaini124 – 246123CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei44 – 6421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei103 – 12321HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    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:
    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]
    ENST00000458587; ENSP00000392330; ENSG00000185825. [P51572-2]
    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 ]
    ENST00000458587 ; ENSP00000392330 ; ENSG00000185825 . [P51572-2 ]
    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

    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.
    20. "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: October 1, 2014
    This is version 141 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