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P35606 (COPB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity.

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 By similarity. 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.

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 Ref.3
Chain2 – 906905Coatomer subunit beta'
PRO_0000050912

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 coil866 – 89126 Potential

Amino acid modifications

Modified residue6271N6-acetyllysine Ref.9
Modified residue8591Phosphoserine Ref.6 Ref.8 Ref.10 Ref.12

Sequences

Sequence LengthMass (Da)Tools
P35606 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 824BB63BEFAA53F6

FASTA906102,487
        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 GDAEIKDGER LPLAVKDMGS CEIYPQTIQH 

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

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

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

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

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

       670        680        690        700        710        720 
AVEAESEQKW KQLAELAISK CQFGLAQECL HHAQDYGGLL LLATASGNAN MVNKLAEGAE 

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

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

       850        860        870        880        890        900 
DFQPSRSTAQ QELDGKPASP TPVIVASHTA NKEEKSLLEL EVDLDNLELE DIDTTDINLD 


EDILDD 

« Hide

References

« Hide 'large scale' references
[1]"A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins."
Harrison-Lavoie K.J., Lewis V.A., Hynes G.M., Collison K.S., Nutland E., Willison K.R.
EMBO J. 12:2847-2853(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Lung.
[3]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9.
Tissue: Platelet.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70476 mRNA. Translation: CAA49900.1.
BC000326 mRNA. Translation: AAH00326.1.
CCDSCCDS3108.1.
PIRS35342.
RefSeqNP_004757.1. NM_004766.2.
UniGeneHs.681616.

3D structure databases

ProteinModelPortalP35606.
SMRP35606. Positions 3-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114693. 32 interactions.
DIPDIP-27603N.
IntActP35606. 13 interactions.
MINTMINT-5000992.
STRING9606.ENSP00000329419.

PTM databases

PhosphoSiteP35606.

Polymorphism databases

DMDM544076.

Proteomic databases

MaxQBP35606.
PaxDbP35606.
PeptideAtlasP35606.
PRIDEP35606.

Protocols and materials databases

DNASU9276.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333188; ENSP00000329419; ENSG00000184432.
GeneID9276.
KEGGhsa:9276.
UCSCuc003etf.4. human.

Organism-specific databases

CTD9276.
GeneCardsGC03M139076.
HGNCHGNC:2232. COPB2.
HPAHPA036867.
MIM606990. gene.
neXtProtNX_P35606.
PharmGKBPA26748.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000163444.
HOVERGENHBG051076.
InParanoidP35606.
KOK17302.
OMAIAHNPNG.
OrthoDBEOG78PV85.
PhylomeDBP35606.
TreeFamTF300688.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
SignaLinkP35606.

Gene expression databases

ArrayExpressP35606.
BgeeP35606.
CleanExHS_COPB2.
GenevestigatorP35606.

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

ChiTaRSCOPB2. human.
GeneWikiCOPB2.
GenomeRNAi9276.
NextBio34765.
PROP35606.
SOURCESearch...

Entry information

Entry nameCOPB2_HUMAN
AccessionPrimary (citable) accession number: P35606
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM