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O55029 (COPB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit beta'
Alternative name(s):
Beta'-coat protein
Short name=Beta'-COP
p102
Gene names
Name:Copb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length905 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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. Ref.4

Sequence similarities

Belongs to the WD repeat COPB2 family.

Contains 9 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 905904Coatomer subunit beta'
PRO_0000050913

Regions

Repeat13 – 5240WD 1
Repeat55 – 9440WD 2
Repeat97 – 13640WD 3
Repeat140 – 18041WD 4
Repeat183 – 22442WD 5
Repeat227 – 26640WD 6
Repeat350 – 38839WD 7
Repeat390 – 42536WD 8
Repeat746 – 78338WD 9
Coiled coil867 – 89125 Potential

Amino acid modifications

Modified residue6271N6-acetyllysine By similarity
Modified residue8591Phosphoserine By similarity

Experimental info

Sequence conflict6841S → H in AAB97760. Ref.3
Sequence conflict7331F → L in AAB97760. Ref.3
Sequence conflict8391A → P in AAB97760. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O55029 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 5845082CAB10FD12

FASTA905102,449
        10         20         30         40         50         60 
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV 

        70         80         90        100        110        120 
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD 

       130        140        150        160        170        180 
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT 

       190        200        210        220        230        240 
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE 

       250        260        270        280        290        300 
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG 

       310        320        330        340        350        360 
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS CEIYPQTIQH 

       370        380        390        400        410        420 
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE 

       430        440        450        460        470        480 
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWENTELIRR IEIQPKHIFW SDSGELVCIA 

       490        500        510        520        530        540 
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV 

       550        560        570        580        590        600 
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR 

       610        620        630        640        650        660 
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL 

       670        680        690        700        710        720 
AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL LLATASGNAS MVNKLAEGAE 

       730        740        750        760        770        780 
RDGKNNVAFM SYFLQGKLDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV 

       790        800        810        820        830        840 
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK 

       850        860        870        880        890        900 
GFQPSRPTAQ QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE 


DILDD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Differential localization of coatomer complex isoforms within the Golgi apparatus."
Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I., Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B., Wieland F.T.
Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK088064 mRNA. Translation: BAC40125.1.
AK153352 mRNA. Translation: BAE31926.1.
AF043120 mRNA. Translation: AAB97760.1.
BC006675 mRNA. Translation: AAH06675.1.
CCDSCCDS40734.1.
RefSeqNP_056642.1. NM_015827.2.
UniGeneMm.400464.

3D structure databases

ProteinModelPortalO55029.
SMRO55029. Positions 3-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206128. 3 interactions.
IntActO55029. 6 interactions.
MINTMINT-1666570.
STRING10090.ENSMUSP00000035033.

PTM databases

PhosphoSiteO55029.

Proteomic databases

MaxQBO55029.
PaxDbO55029.
PRIDEO55029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035033; ENSMUSP00000035033; ENSMUSG00000032458.
GeneID50797.
KEGGmmu:50797.
UCSCuc009rdm.1. mouse.

Organism-specific databases

CTD9276.
MGIMGI:1354962. Copb2.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00740000115578.
HOGENOMHOG000163444.
HOVERGENHBG051076.
InParanoidO55029.
KOK17302.
OMAIAHNPNG.
OrthoDBEOG78PV85.
PhylomeDBO55029.
TreeFamTF300688.

Gene expression databases

BgeeO55029.
GenevestigatorO55029.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR006692. 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]
PfamPF04053. Coatomer_WDAD. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PIRSFPIRSF005567. Coatomer_beta'_subunit. 1 hit.
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 3 hits.
PROSITEPS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307805.
PROO55029.
SOURCESearch...

Entry information

Entry nameCOPB2_MOUSE
AccessionPrimary (citable) accession number: O55029
Secondary accession number(s): Q3U5Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 29, 2001
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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