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Protein

B-cell receptor-associated protein 31

Gene

Bcap31

Organism
Mus musculus (Mouse)
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.2 Publications

Sites

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

GO - Molecular functioni

  • MHC class I protein binding Source: MGI
  • protein complex binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_277640. Apoptotic cleavage of cellular proteins.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell receptor-associated protein 31
Short name:
BCR-associated protein 31
Short name:
Bap31
Alternative name(s):
p28
Gene namesi
Name:Bcap31
Synonyms:Bap31
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1350933. 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 – 245122CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 245244B-cell receptor-associated protein 31PRO_0000142892Add
BLAST

Post-translational modificationi

Cleaved by CASP8 and other caspases.By similarity

Proteomic databases

MaxQBiQ61335.
PaxDbiQ61335.
PRIDEiQ61335.

PTM databases

PhosphoSiteiQ61335.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

CleanExiMM_BCAP31.
GenevisibleiQ61335. MM.

Interactioni

Subunit structurei

Homodimer and heterodimer with BCAP29. Binds CASP8 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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ61335. 4 interactions.
MINTiMINT-1797765.
STRINGi10090.ENSMUSP00000002091.

Structurei

3D structure databases

ProteinModelPortaliQ61335.
SMRiQ61335. Positions 178-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili165 – 23672By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi242 – 2454Di-lysine motif

Sequence similaritiesi

Belongs to the BCAP29/BCAP31 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG244998.
GeneTreeiENSGT00390000011863.
HOGENOMiHOG000204790.
HOVERGENiHBG050661.
InParanoidiQ61335.
KOiK14009.
OMAiLNVEMQH.
OrthoDBiEOG7B5WXD.
TreeFamiTF315310.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q61335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQWTTVAT FLYAEVFAVL LLCIPFISPK RWQKVFKSRL VELVVTYGNT
60 70 80 90 100
FFVVLIVILV LLVIDAVREI LKYDDVTEKV NLQNNPGAME HFHMKLFRAQ
110 120 130 140 150
RNLYIAGFSL LLSFLLRRLV TLISQQATLL ASNEAFKKQA ESASEAAKKY
160 170 180 190 200
MEENDQLKKG AAEDGDKLDI GNTEMKLEEN KSLKNDLRKL KDELASTKKK
210 220 230 240
LEKAENEALA MQKQSEGLTK EYDRLLEEHA KLQASVRGPS VKKEE
Length:245
Mass (Da):27,957
Last modified:October 3, 2012 - v4
Checksum:iA8C53B7A04E06C97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281S → Y in BAB25427 (PubMed:16141072).Curated
Sequence conflicti108 – 1081F → L in CAA57414 (PubMed:8612576).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81816 mRNA. Translation: CAA57414.1.
AK008043 mRNA. Translation: BAB25427.1.
AK011500 mRNA. Translation: BAB27660.1.
AL805924 Genomic DNA. Translation: CAM21061.1.
CH466650 Genomic DNA. Translation: EDL29886.1.
BC002106 mRNA. Translation: AAH02106.1.
CCDSiCCDS30209.1.
PIRiS71116.
RefSeqiNP_036190.2. NM_012060.4.
XP_006528111.1. XM_006528048.2.
XP_011245902.1. XM_011247600.1.
UniGeneiMm.17.

Genome annotation databases

EnsembliENSMUST00000002091; ENSMUSP00000002091; ENSMUSG00000002015.
GeneIDi27061.
KEGGimmu:27061.
UCSCiuc009tmj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81816 mRNA. Translation: CAA57414.1.
AK008043 mRNA. Translation: BAB25427.1.
AK011500 mRNA. Translation: BAB27660.1.
AL805924 Genomic DNA. Translation: CAM21061.1.
CH466650 Genomic DNA. Translation: EDL29886.1.
BC002106 mRNA. Translation: AAH02106.1.
CCDSiCCDS30209.1.
PIRiS71116.
RefSeqiNP_036190.2. NM_012060.4.
XP_006528111.1. XM_006528048.2.
XP_011245902.1. XM_011247600.1.
UniGeneiMm.17.

3D structure databases

ProteinModelPortaliQ61335.
SMRiQ61335. Positions 178-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61335. 4 interactions.
MINTiMINT-1797765.
STRINGi10090.ENSMUSP00000002091.

PTM databases

PhosphoSiteiQ61335.

Proteomic databases

MaxQBiQ61335.
PaxDbiQ61335.
PRIDEiQ61335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002091; ENSMUSP00000002091; ENSMUSG00000002015.
GeneIDi27061.
KEGGimmu:27061.
UCSCiuc009tmj.1. mouse.

Organism-specific databases

CTDi10134.
MGIiMGI:1350933. Bcap31.

Phylogenomic databases

eggNOGiNOG244998.
GeneTreeiENSGT00390000011863.
HOGENOMiHOG000204790.
HOVERGENiHBG050661.
InParanoidiQ61335.
KOiK14009.
OMAiLNVEMQH.
OrthoDBiEOG7B5WXD.
TreeFamiTF315310.

Enzyme and pathway databases

ReactomeiREACT_277640. Apoptotic cleavage of cellular proteins.
REACT_339401. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiBcap31. mouse.
NextBioi305025.
PROiQ61335.
SOURCEiSearch...

Gene expression databases

CleanExiMM_BCAP31.
GenevisibleiQ61335. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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], PROTEIN SEQUENCE OF 2-11, INTERACTION WITH BCAP29 AND IGD, TISSUE SPECIFICITY.
    Tissue: Plasmacytoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  6. "Two new proteins preferentially associated with membrane immunoglobulin D."
    Kim K.-M., Adachi T., Nielsen P.J., Terashima M., Lamers M.C., Koehler G., Reth M.
    EMBO J. 13:3793-3800(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 150-157; 168-180; 205-213; 214-220; 221-231 AND 232-242, INTERACTION WITH BCAP29 AND IGD.
  7. "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: FUNCTION, INTERACTION WITH VAMP3.
  8. "Bap29/31 influences the intracellular traffic of MHC class I molecules."
    Paquet M.E., Cohen-Doyle M., Shore G.C., Williams D.B.
    J. Immunol. 172:7548-7555(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiBAP31_MOUSE
AccessioniPrimary (citable) accession number: Q61335
Secondary accession number(s): A2ALM8, Q9D0E9, Q9D8G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 3, 2012
Last modified: July 22, 2015
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.