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P35606

- COPB2_HUMAN

UniProt

P35606 - COPB2_HUMAN

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Protein

Coatomer subunit beta'

Gene

COPB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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 By similarity. Interacts with JAGN1.By similarity1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. COPI coating of Golgi vesicle Source: Reactome
  2. intracellular protein transport Source: InterPro
  3. intra-Golgi vesicle-mediated transport Source: UniProtKB
  4. membrane organization Source: Reactome
  5. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
SignaLinkiP35606.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit beta'
Alternative name(s):
Beta'-coat protein
Short name:
Beta'-COP
p102
Gene namesi
Name:COPB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:2232. COPB2.

Subcellular locationi

Cytoplasmcytosol By similarity. 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: UniProtKB
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26748.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 906905Coatomer subunit beta'PRO_0000050912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei627 – 6271N6-acetyllysine1 Publication
Modified residuei859 – 8591Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35606.
PaxDbiP35606.
PeptideAtlasiP35606.
PRIDEiP35606.

PTM databases

PhosphoSiteiP35606.

Expressioni

Gene expression databases

BgeeiP35606.
CleanExiHS_COPB2.
ExpressionAtlasiP35606. baseline and differential.
GenevestigatoriP35606.

Organism-specific databases

HPAiHPA036867.

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.By similarity

Protein-protein interaction databases

BioGridi114693. 37 interactions.
DIPiDIP-27603N.
IntActiP35606. 15 interactions.
MINTiMINT-5000992.
STRINGi9606.ENSP00000329419.

Structurei

3D structure databases

ProteinModelPortaliP35606.
SMRiP35606. 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 coili866 – 89126Sequence 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.
GeneTreeiENSGT00760000119311.
HOGENOMiHOG000163444.
HOVERGENiHBG051076.
KOiK17302.
OMAiIAHNPNG.
OrthoDBiEOG78PV85.
PhylomeDBiP35606.
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.
IPR011044. Quino_amine_DH_bsu.
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. 5 hits.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 1 hit.
SSF50978. SSF50978. 2 hits.
PROSITEiPS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35606-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 GDAEIKDGER 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
DWDNTELIRR IEIQPKHIFW SDSGELVCIA TEESFFILKY LSEKVLAAQE
510 520 530 540 550
THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV NRLNYYVGGE
560 570 580 590 600
IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIISYSLLVS VLEYQTAVMR
610 620 630 640 650
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ
660 670 680 690 700
LGELKIAYQL AVEAESEQKW KQLAELAISK CQFGLAQECL HHAQDYGGLL
710 720 730 740 750
LLATASGNAN MVNKLAEGAE RDGKNNVAFM SYFLQGKVDA CLELLIRTGR
760 770 780 790 800
LPEAAFLART YLPSQVSRVV KLWRENLSKV NQKAAESLAD PTEYENLFPG
810 820 830 840 850
LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEGK DFQPSRSTAQ
860 870 880 890 900
QELDGKPASP TPVIVASHTA NKEEKSLLEL EVDLDNLELE DIDTTDINLD

EDILDD
Length:906
Mass (Da):102,487
Last modified:January 23, 2007 - v2
Checksum:i824BB63BEFAA53F6
GO
Isoform 2 (identifier: P35606-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Note: No experimental confirmation available.

Show »
Length:877
Mass (Da):99,046
Checksum:i9E91476A4379BB1C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_056165Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70476 mRNA. Translation: CAA49900.1.
AK302943 mRNA. Translation: BAG64100.1.
AC024933 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79040.1.
BC000326 mRNA. Translation: AAH00326.1.
CCDSiCCDS3108.1. [P35606-1]
PIRiS35342.
RefSeqiNP_004757.1. NM_004766.2.
UniGeneiHs.681616.

Genome annotation databases

EnsembliENST00000333188; ENSP00000329419; ENSG00000184432. [P35606-1]
ENST00000507777; ENSP00000422295; ENSG00000184432. [P35606-2]
GeneIDi9276.
KEGGihsa:9276.
UCSCiuc003etf.4. human. [P35606-1]

Polymorphism databases

DMDMi544076.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70476 mRNA. Translation: CAA49900.1 .
AK302943 mRNA. Translation: BAG64100.1 .
AC024933 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79040.1 .
BC000326 mRNA. Translation: AAH00326.1 .
CCDSi CCDS3108.1. [P35606-1 ]
PIRi S35342.
RefSeqi NP_004757.1. NM_004766.2.
UniGenei Hs.681616.

3D structure databases

ProteinModelPortali P35606.
SMRi P35606. Positions 3-777.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114693. 37 interactions.
DIPi DIP-27603N.
IntActi P35606. 15 interactions.
MINTi MINT-5000992.
STRINGi 9606.ENSP00000329419.

PTM databases

PhosphoSitei P35606.

Polymorphism databases

DMDMi 544076.

Proteomic databases

MaxQBi P35606.
PaxDbi P35606.
PeptideAtlasi P35606.
PRIDEi P35606.

Protocols and materials databases

DNASUi 9276.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333188 ; ENSP00000329419 ; ENSG00000184432 . [P35606-1 ]
ENST00000507777 ; ENSP00000422295 ; ENSG00000184432 . [P35606-2 ]
GeneIDi 9276.
KEGGi hsa:9276.
UCSCi uc003etf.4. human. [P35606-1 ]

Organism-specific databases

CTDi 9276.
GeneCardsi GC03M139076.
HGNCi HGNC:2232. COPB2.
HPAi HPA036867.
MIMi 606990. gene.
neXtProti NX_P35606.
PharmGKBi PA26748.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00760000119311.
HOGENOMi HOG000163444.
HOVERGENi HBG051076.
KOi K17302.
OMAi IAHNPNG.
OrthoDBi EOG78PV85.
PhylomeDBi P35606.
TreeFami TF300688.

Enzyme and pathway databases

Reactomei REACT_11096. COPI Mediated Transport.
SignaLinki P35606.

Miscellaneous databases

ChiTaRSi COPB2. human.
GeneWikii COPB2.
GenomeRNAii 9276.
NextBioi 34765.
PROi P35606.
SOURCEi Search...

Gene expression databases

Bgeei P35606.
CleanExi HS_COPB2.
ExpressionAtlasi P35606. baseline and differential.
Genevestigatori P35606.

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.
IPR011044. Quino_amine_DH_bsu.
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. 5 hits.
[Graphical view ]
SUPFAMi SSF50969. SSF50969. 1 hit.
SSF50978. SSF50978. 2 hits.
PROSITEi PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Lung.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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.
  12. "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].
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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].
  16. Cited for: INTERACTION WITH JAGN1.

Entry informationi

Entry nameiCOPB2_HUMAN
AccessioniPrimary (citable) accession number: P35606
Secondary accession number(s): B4DZI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3