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Q9JIF7

- COPB_MOUSE

UniProt

Q9JIF7 - COPB_MOUSE

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Protein
Coatomer subunit beta
Gene
Copb1, Copb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 By similarity. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.2 Publications

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. intra-Golgi vesicle-mediated transport Source: Ensembl
  2. intracellular protein transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_227904. COPI Mediated Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name:
Beta-COP
Gene namesi
Name:Copb1
Synonyms:Copb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1917599. Copb1.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane By similarity. Endoplasmic reticulum-Golgi intermediate compartment By similarity
Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it By similarity. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm. Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack By similarity. Occasionally present at the trans-side of Golgi, but mainly present at the cis- Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae By similarity. Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles By similarity. Some association with high-density and low-density microsomes and mitochondria/nuclei fraction By similarity. Very little found in plasma membrane fraction By similarity.2 Publications

GO - Cellular componenti

  1. COPI vesicle coat Source: Ensembl
  2. COPI-coated vesicle Source: MGI
  3. Golgi apparatus Source: MGI
  4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 953952Coatomer subunit beta
PRO_0000193834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine By similarity
Modified residuei494 – 4941N6-acetyllysine1 Publication

Post-translational modificationi

Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JIF7.
PaxDbiQ9JIF7.
PRIDEiQ9JIF7.

PTM databases

PhosphoSiteiQ9JIF7.

Expressioni

Tissue specificityi

Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (1 Publication). Ubiquitiously expressed including platelet, liver, heart, spleen, lung and kidney (1 Publication).2 Publications

Gene expression databases

BgeeiQ9JIF7.
CleanExiMM_COPB1.
GenevestigatoriQ9JIF7.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits By similarity. Interacts with CAPN8. Interacts with SCYL1 and PRKCE By similarity. Interacts with COPG1 By similarity. Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes By similarity. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct By similarity. Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 By similarity. Interacts with STX17 By similarity.1 Publication

Protein-protein interaction databases

BioGridi213992. 3 interactions.
DIPiDIP-42642N.
IntActiQ9JIF7. 9 interactions.
MINTiMINT-1489518.
STRINGi10090.ENSMUSP00000033012.

Structurei

3D structure databases

ProteinModelPortaliQ9JIF7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 13136HEAT 1
Add
BLAST
Repeati132 – 16837HEAT 2
Add
BLAST
Repeati240 – 27637HEAT 3
Add
BLAST
Repeati277 – 31438HEAT 4
Add
BLAST
Repeati316 – 35338HEAT 5
Add
BLAST
Repeati396 – 43338HEAT 6
Add
BLAST

Sequence similaritiesi

Contains 6 HEAT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5096.
GeneTreeiENSGT00390000005270.
HOGENOMiHOG000207417.
HOVERGENiHBG005380.
InParanoidiQ3T9Y4.
KOiK17301.
OMAiVHALMEF.
OrthoDBiEOG7ZWD12.
PhylomeDBiQ9JIF7.
TreeFamiTF105737.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
IPR029446. COPB1_appendage_platform_dom.
[Graphical view]
PANTHERiPTHR10635. PTHR10635. 1 hit.
PfamiPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view]
PIRSFiPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q9JIF7-1 [UniParc]FASTAAdd to Basket

« Hide

MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL    50
NGEKLPGLLM TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL 100
VCDAYRKDLQ HPNEFIRGST LRFLCKLKEA ELLEPLMPAI RACLEHRHSY 150
VRRNAVLAIY TIYRNFEHLI PDAPELIHDF LVNEKDASCK RNAFMMLIHA 200
DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS ERARFIRCIY 250
NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 300
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS 350
RNVEELVIVL KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN 400
VIPVLMEFLS DSNEAAAADV LEFVREAIQR FDNLRMLIVE KMLEVFHAIK 450
SVKIYRGALW ILGEYCSTKE DIQSVMTEVR RSLGEIPIVE SEIKKEAGEL 500
KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP PLRGFLLDGD 550
FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 600
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE 650
KLSQKKESEK RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT 700
QRKEAADPLA SKLNKVTQLT GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS 750
DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH DFANIKANVK VASTENGIIF 800
GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF RQMWAEFEWE 850
NKVTVNTNMT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 900
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK 950
TSL 953
Length:953
Mass (Da):107,066
Last modified:October 1, 2000 - v1
Checksum:i4CD5407AD87ACB4B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti757 – 7571T → I in BAE29109. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF231925 mRNA. Translation: AAF76856.1.
AK149828 mRNA. Translation: BAE29109.1.
AK152222 mRNA. Translation: BAE31049.1.
AK161544 mRNA. Translation: BAE36453.1.
AK172214 mRNA. Translation: BAE42886.1.
CH466531 Genomic DNA. Translation: EDL17060.1.
BC030837 mRNA. Translation: AAH30837.1.
CCDSiCCDS21759.1.
RefSeqiNP_203534.1. NM_033370.3.
UniGeneiMm.277024.

Genome annotation databases

EnsembliENSMUST00000033012; ENSMUSP00000033012; ENSMUSG00000030754.
GeneIDi70349.
KEGGimmu:70349.
UCSCiuc009jhx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF231925 mRNA. Translation: AAF76856.1 .
AK149828 mRNA. Translation: BAE29109.1 .
AK152222 mRNA. Translation: BAE31049.1 .
AK161544 mRNA. Translation: BAE36453.1 .
AK172214 mRNA. Translation: BAE42886.1 .
CH466531 Genomic DNA. Translation: EDL17060.1 .
BC030837 mRNA. Translation: AAH30837.1 .
CCDSi CCDS21759.1.
RefSeqi NP_203534.1. NM_033370.3.
UniGenei Mm.277024.

3D structure databases

ProteinModelPortali Q9JIF7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213992. 3 interactions.
DIPi DIP-42642N.
IntActi Q9JIF7. 9 interactions.
MINTi MINT-1489518.
STRINGi 10090.ENSMUSP00000033012.

PTM databases

PhosphoSitei Q9JIF7.

Proteomic databases

MaxQBi Q9JIF7.
PaxDbi Q9JIF7.
PRIDEi Q9JIF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033012 ; ENSMUSP00000033012 ; ENSMUSG00000030754 .
GeneIDi 70349.
KEGGi mmu:70349.
UCSCi uc009jhx.1. mouse.

Organism-specific databases

CTDi 1315.
MGIi MGI:1917599. Copb1.

Phylogenomic databases

eggNOGi COG5096.
GeneTreei ENSGT00390000005270.
HOGENOMi HOG000207417.
HOVERGENi HBG005380.
InParanoidi Q3T9Y4.
KOi K17301.
OMAi VHALMEF.
OrthoDBi EOG7ZWD12.
PhylomeDBi Q9JIF7.
TreeFami TF105737.

Enzyme and pathway databases

Reactomei REACT_227904. COPI Mediated Transport.

Miscellaneous databases

NextBioi 331414.
PROi Q9JIF7.
SOURCEi Search...

Gene expression databases

Bgeei Q9JIF7.
CleanExi MM_COPB1.
Genevestigatori Q9JIF7.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
IPR029446. COPB1_appendage_platform_dom.
[Graphical view ]
PANTHERi PTHR10635. PTHR10635. 1 hit.
Pfami PF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
PF14806. Coatomer_b_Cpla. 1 hit.
[Graphical view ]
PIRSFi PIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMi SSF48371. SSF48371. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and mapping of the mouse Copb gene encoding the beta subunit of the COPI coatomer complex."
    Li W., Elliott R.W., Novak E.K., Swank R.T.
    Somat. Cell Mol. Genet. 25:177-183(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Bone marrow.
  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 and NOD.
    Tissue: Bone marrow, Pituitary and Spleen.
  3. 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].
  4. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. "Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP."
    Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.
    J. Biol. Chem. 281:11214-11224(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAPN8, SUBCELLULAR LOCATION, PTM, TISSUE SPECIFICITY.
  6. "Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA."
    Bi J., Tsai N.P., Lu H.Y., Loh H.H., Wei L.N.
    Proc. Natl. Acad. Sci. U.S.A. 104:13810-13815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: FUNCTION.
  8. "Novel Golgi protein, GoPro49, is a specific dental follicle marker."
    Takatalo M.S., Tummers M., Thesleff I., Roennholm R.
    J. Dent. Res. 88:534-538(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCOPB_MOUSE
AccessioniPrimary (citable) accession number: Q9JIF7
Secondary accession number(s): Q3T9Y4
, Q3TT72, Q3U8G9, Q3UE02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

Keywords - Technical termi

Complete proteome, 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

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