Coatomer subunit beta' - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P35606 (COPB2_HUMAN)

Last modified July 7, 2009. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Coatomer subunit beta'
Alternative name(s):
    Beta'-coat protein
      Short name=Beta'-COP
    p102

Gene names

Name:

COPB2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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	Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle › COPI-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.
Sequence similarities	Contains 9 WD repeats.

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Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane
Domain	Coiled coil Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	COPI coating of Golgi vesicle Inferred from Experiment. Source: Reactome intra-Golgi vesicle-mediated transport Ref.1 Inferred from direct assay. Source: UniProtKB intracellular protein transport Inferred from electronic annotation. Source: InterPro retrograde vesicle-mediated transport, Golgi to ER Traceable author statement. Source: UniProtKB
Cellular component	COPI vesicle coat Ref.1 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ILK	Q13418	1	EBI-1056534,EBI-747644
NDRG1	Q92597	1	EBI-1056534,EBI-716486
TSC22D1	Q15714	1	EBI-1056534,EBI-712609

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 906

905

Coatomer subunit beta'

PRO_0000050912

Regions

Repeat

13 – 52

WD 1

Repeat

55 – 94

WD 2

Repeat

97 – 136

WD 3

Repeat

140 – 180

WD 4

Repeat

183 – 224

WD 5

Repeat

227 – 266

WD 6

Repeat

350 – 388

WD 7

Repeat

390 – 425

WD 8

Repeat

746 – 783

WD 9

Coiled coil

866 – 891

Potential

Amino acid modifications

Modified residue

354

Phosphotyrosine Ref.5

Modified residue

859

Phosphoserine Ref.4 Ref.6 Ref.7 Ref.8

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Sequences

Sequence

Length

Mass (Da)

Tools

P35606-1 [UniParc].

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

906

102,487

        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

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References

	« Hide 'large scale' referencesShow '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: 8335000] [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: 15489334] [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: 12665801] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, MASS SPECTROMETRY.
[6]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, MASS SPECTROMETRY.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X70476 mRNA. Translation: CAA49900.1. BC000326 mRNA. Translation: AAH00326.1.
IPI	IPI00220219.
PIR	S35342.
RefSeq	NP_004757.1.
UniGene	Hs.75724
3D structure databases
HSSP	HSSP built from PDB template 1ERJ based on UniProtKB P16649.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27603N.
IntAct	P35606. 16 interactions.
PTM databases
PhosphoSite	P35606.
Proteomic databases
PeptideAtlas	P35606.
PRIDE	P35606.
Genome annotation databases
Ensembl	ENSG00000184432. Homo sapiens. [Contig view]
GeneID	9276.
KEGG	hsa:9276.
UCSC	uc003etf.2. human.
Organism-specific databases
GeneCards	GC03M140559.
H-InvDB	HIX0022798.
HGNC	HGNC:2232. COPB2.
MIM	606990. gene.
PharmGKB	PA26748.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P35606.
HOVERGEN	P35606.
OMA	P35606. FYDWENT.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	P35606.
Bgee	P35606.
CleanEx	HS_COPB2.
GermOnline	ENSG00000184432. Homo sapiens.
Family and domain databases
InterPro	IPR016453. Coatomer_beta'_subunit. IPR006692. Coatomer_WD-assoc_reg. IPR015943. WD40/YVTN_repeat-like. IPR001680. WD40_repeat. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_region. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF04053. Coatomer_WDAD. 1 hit. PF00400. WD40. 6 hits. [Graphical view]
PIRSF	PIRSF005567. Coatomer_beta'_subunit. 1 hit.
ProDom	PD000018. WD40. 4 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00320. WD40. 6 hits. [Graphical view]
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 5 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34765.
SOURCE	Search...

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Entry information

Entry name

COPB2_HUMAN

Accession

Primary (citable) accession number: P35606

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents