SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O55029

- COPB2_MOUSE

UniProt

O55029 - COPB2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Coatomer subunit beta'
Gene
Copb2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 By similarity.
This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

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
p102
Gene namesi
Name:Copb2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1354962. Copb2.

Subcellular locationi

Cytoplasmcytosol. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side 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. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi By similarity.1 Publication

GO - Cellular componenti

  1. COPI vesicle coat Source: Ensembl
  2. Golgi apparatus Source: MGI
  3. actin cytoskeleton Source: Ensembl
  4. cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 905904Coatomer subunit beta'
PRO_0000050913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei627 – 6271N6-acetyllysine By similarity
Modified residuei859 – 8591Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO55029.
PaxDbiO55029.
PRIDEiO55029.

PTM databases

PhosphoSiteiO55029.

Expressioni

Gene expression databases

BgeeiO55029.
GenevestigatoriO55029.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1 By similarity.

Protein-protein interaction databases

BioGridi206128. 3 interactions.
IntActiO55029. 6 interactions.
MINTiMINT-1666570.
STRINGi10090.ENSMUSP00000035033.

Structurei

3D structure databases

ProteinModelPortaliO55029.
SMRiO55029. Positions 3-777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 5240WD 1
Add
BLAST
Repeati55 – 9440WD 2
Add
BLAST
Repeati97 – 13640WD 3
Add
BLAST
Repeati140 – 18041WD 4
Add
BLAST
Repeati183 – 22442WD 5
Add
BLAST
Repeati227 – 26640WD 6
Add
BLAST
Repeati350 – 38839WD 7
Add
BLAST
Repeati390 – 42536WD 8
Add
BLAST
Repeati746 – 78338WD 9
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili867 – 89125 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat COPB2 family.
Contains 9 WD repeats.

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00740000115578.
HOGENOMiHOG000163444.
HOVERGENiHBG051076.
InParanoidiO55029.
KOiK17302.
OMAiIAHNPNG.
OrthoDBiEOG78PV85.
PhylomeDBiO55029.
TreeFamiTF300688.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR006692. Coatomer_WD-assoc_reg.
IPR016453. COPB2.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF04053. Coatomer_WDAD. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PIRSFiPIRSF005567. Coatomer_beta'_subunit. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O55029-1 [UniParc]FASTAAdd to Basket

« Hide

MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV    50
KTFEVCDLPV RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD 100
YIRCIAVHPT QPFILTSSDD MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI 150
NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT LEGHEKGVNC IDYYSGGDKP 200
YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE LPIIITGSED 250
GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG 300
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS 350
CEIYPQTIQH NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS 400
SEYAIRESNS IVKIFKNFKE KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY 450
DWENTELIRR IEIQPKHIFW SDSGELVCIA TEESFFILKY LSEKVLAAQE 500
THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV NRLNYYVGGE 550
IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR 600
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ 650
LGELKIAYQL AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL 700
LLATASGNAS MVNKLAEGAE RDGKNNVAFM SYFLQGKLDA CLELLIRTGR 750
LPEAAFLART YLPSQVSRVV KLWRENLSKV NQKAAESLAD PTEYENLFPG 800
LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK GFQPSRPTAQ 850
QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE 900
DILDD 905
Length:905
Mass (Da):102,449
Last modified:August 29, 2001 - v2
Checksum:i5845082CAB10FD12
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti684 – 6841S → H in AAB97760. 1 Publication
Sequence conflicti733 – 7331F → L in AAB97760. 1 Publication
Sequence conflicti839 – 8391A → P in AAB97760. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK088064 mRNA. Translation: BAC40125.1.
AK153352 mRNA. Translation: BAE31926.1.
AF043120 mRNA. Translation: AAB97760.1.
BC006675 mRNA. Translation: AAH06675.1.
CCDSiCCDS40734.1.
RefSeqiNP_056642.1. NM_015827.2.
UniGeneiMm.400464.

Genome annotation databases

EnsembliENSMUST00000035033; ENSMUSP00000035033; ENSMUSG00000032458.
GeneIDi50797.
KEGGimmu:50797.
UCSCiuc009rdm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK088064 mRNA. Translation: BAC40125.1 .
AK153352 mRNA. Translation: BAE31926.1 .
AF043120 mRNA. Translation: AAB97760.1 .
BC006675 mRNA. Translation: AAH06675.1 .
CCDSi CCDS40734.1.
RefSeqi NP_056642.1. NM_015827.2.
UniGenei Mm.400464.

3D structure databases

ProteinModelPortali O55029.
SMRi O55029. Positions 3-777.
ModBasei Search...

Protein-protein interaction databases

BioGridi 206128. 3 interactions.
IntActi O55029. 6 interactions.
MINTi MINT-1666570.
STRINGi 10090.ENSMUSP00000035033.

PTM databases

PhosphoSitei O55029.

Proteomic databases

MaxQBi O55029.
PaxDbi O55029.
PRIDEi O55029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035033 ; ENSMUSP00000035033 ; ENSMUSG00000032458 .
GeneIDi 50797.
KEGGi mmu:50797.
UCSCi uc009rdm.1. mouse.

Organism-specific databases

CTDi 9276.
MGIi MGI:1354962. Copb2.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00740000115578.
HOGENOMi HOG000163444.
HOVERGENi HBG051076.
InParanoidi O55029.
KOi K17302.
OMAi IAHNPNG.
OrthoDBi EOG78PV85.
PhylomeDBi O55029.
TreeFami TF300688.

Enzyme and pathway databases

Reactomei REACT_227904. COPI Mediated Transport.

Miscellaneous databases

NextBioi 307805.
PROi O55029.
SOURCEi Search...

Gene expression databases

Bgeei O55029.
Genevestigatori O55029.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR006692. Coatomer_WD-assoc_reg.
IPR016453. COPB2.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF04053. Coatomer_WDAD. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view ]
PIRSFi PIRSF005567. Coatomer_beta'_subunit. 1 hit.
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 3 hits.
PROSITEi PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 and Thymus.
  2. "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].
  3. Tarsounas M., Moens P.B., Pearlman R.E.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 456-905.
    Tissue: Testis.
  4. Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCOPB2_MOUSE
AccessioniPrimary (citable) accession number: O55029
Secondary accession number(s): Q3U5Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 29, 2001
Last modified: September 3, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Similar proteinsi