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O55029

- COPB2_MOUSE

UniProt

O55029 - COPB2_MOUSE

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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).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

GO - Biological processi

  1. intracellular protein transport Source: InterPro
  2. intra-Golgi vesicle-mediated transport Source: Ensembl
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 1 Publication. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; 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. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi.By similarity

GO - Cellular componenti

  1. COPI vesicle coat Source: Ensembl
  2. Golgi apparatus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei627 – 6271N6-acetyllysineBy similarity
Modified residuei859 – 8591PhosphoserineBy 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. Interacts with JAGN1 (By similarity).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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili867 – 89125Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat COPB2 family.Curated
Contains 9 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00770000120555.
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

        10         20         30         40         50
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV
60 70 80 90 100
KTFEVCDLPV RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD
110 120 130 140 150
YIRCIAVHPT QPFILTSSDD MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI
160 170 180 190 200
NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT LEGHEKGVNC IDYYSGGDKP
210 220 230 240 250
YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE LPIIITGSED
260 270 280 290 300
GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
310 320 330 340 350
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS
360 370 380 390 400
CEIYPQTIQH NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS
410 420 430 440 450
SEYAIRESNS IVKIFKNFKE KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY
460 470 480 490 500
DWENTELIRR IEIQPKHIFW SDSGELVCIA TEESFFILKY LSEKVLAAQE
510 520 530 540 550
THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV NRLNYYVGGE
560 570 580 590 600
IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR
610 620 630 640 650
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ
660 670 680 690 700
LGELKIAYQL AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL
710 720 730 740 750
LLATASGNAS MVNKLAEGAE RDGKNNVAFM SYFLQGKLDA CLELLIRTGR
760 770 780 790 800
LPEAAFLART YLPSQVSRVV KLWRENLSKV NQKAAESLAD PTEYENLFPG
810 820 830 840 850
LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK GFQPSRPTAQ
860 870 880 890 900
QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE

DILDD
Length:905
Mass (Da):102,449
Last modified:August 29, 2001 - v2
Checksum:i5845082CAB10FD12
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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 ENSGT00770000120555.
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: November 26, 2014
This is version 126 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