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P61923

- COPZ1_HUMAN

UniProt

P61923 - COPZ1_HUMAN

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Protein

Coatomer subunit zeta-1

Gene

COPZ1

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
The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit zeta-1
Alternative name(s):
Zeta-1-coat protein
Short name:
Zeta-1 COP
Gene namesi
Name:COPZ1
Synonyms:COPZ
ORF Names:CGI-120, HSPC181
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2243. COPZ1.

Subcellular locationi

Cytoplasm 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.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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 592EI → KA: Reduced interaction with gamma subunit. 1 Publication
Mutagenesisi87 – 882EL → KA: Reduced interaction with gamma subunit. 1 Publication

Organism-specific databases

PharmGKBiPA26760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177Coatomer subunit zeta-1PRO_0000193825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP61923.
PaxDbiP61923.
PRIDEiP61923.

PTM databases

PhosphoSiteiP61923.

Expressioni

Gene expression databases

BgeeiP61923.
CleanExiHS_COPZ1.
ExpressionAtlasiP61923. baseline and differential.
GenevestigatoriP61923.

Organism-specific databases

HPAiHPA047727.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.1 Publication

Protein-protein interaction databases

BioGridi116495. 22 interactions.
DIPiDIP-29873N.
IntActiP61923. 2 interactions.
STRINGi9606.ENSP00000262061.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207Combined sources
Beta strandi25 – 306Combined sources
Helixi38 – 5215Combined sources
Beta strandi59 – 624Combined sources
Beta strandi65 – 728Combined sources
Beta strandi75 – 817Combined sources
Helixi88 – 10518Combined sources
Helixi111 – 1155Combined sources
Helixi118 – 12811Combined sources
Helixi139 – 14810Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HF6NMR-A1-149[»]
ProteinModelPortaliP61923.
SMRiP61923. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61923.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5541.
GeneTreeiENSGT00390000004405.
HOGENOMiHOG000214428.
HOVERGENiHBG051077.
InParanoidiP61923.
PhylomeDBiP61923.
TreeFamiTF300262.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PfamiPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61923-1) [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
MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN
60 70 80 90 100
KTHRTDSEIA LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS
110 120 130 140 150
LSQMLRKNVE KRALLENMEG LFLAVDEIVD GGVILESDPQ QVVHRVALRG
160 170
EDVPLTEQTV SQVLQSAKEQ IKWSLLR
Length:177
Mass (Da):20,198
Last modified:June 7, 2004 - v1
Checksum:i355530D032D3A049
GO
Isoform 2 (identifier: P61923-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MEALILEPSLYTVKAILILDNDGDRLFAKYYDDTYP → MMEIDFLPSTMTTPTPVSRSKRPLRRTFSTRPIGLT
     37-87: Missing.

Note: No experimental confirmation available.

Show »
Length:126
Mass (Da):14,253
Checksum:i63729DA05B6CAA87
GO
Isoform 3 (identifier: P61923-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-29: Missing.

Note: No experimental confirmation available.

Show »
Length:154
Mass (Da):17,624
Checksum:iB72D2F0155584233
GO
Isoform 4 (identifier: P61923-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MEALIL → MGGFRTEGMFVSLQ

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:185
Mass (Da):21,069
Checksum:i16ABA633D4510033
GO
Isoform 5 (identifier: P61923-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-163: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:160
Mass (Da):18,374
Checksum:iF13D7FACABD98416
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MEALI…DDTYP → MMEIDFLPSTMTTPTPVSRS KRPLRRTFSTRPIGLT in isoform 2. 1 PublicationVSP_053675Add
BLAST
Alternative sequencei1 – 66MEALIL → MGGFRTEGMFVSLQ in isoform 4. CuratedVSP_055049
Alternative sequencei7 – 2923Missing in isoform 3. 1 PublicationVSP_055050Add
BLAST
Alternative sequencei37 – 8751Missing in isoform 2. 1 PublicationVSP_053676Add
BLAST
Alternative sequencei147 – 16317Missing in isoform 5. CuratedVSP_055051Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047848 mRNA. Translation: BAB17659.1.
AF151878 mRNA. Translation: AAD34115.1.
AF161529 mRNA. Translation: AAF29144.1.
AF086911 mRNA. Translation: AAP97141.1.
AK293377 mRNA. Translation: BAG56889.1.
AK295325 mRNA. Translation: BAG58302.1.
AC078778 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96774.1.
BC002849 mRNA. Translation: AAH02849.1.
CCDSiCCDS61137.1. [P61923-5]
CCDS61138.1. [P61923-3]
CCDS61139.1. [P61923-4]
CCDS8877.1. [P61923-1]
RefSeqiNP_001258663.1. NM_001271734.1. [P61923-3]
NP_001258664.1. NM_001271735.1. [P61923-5]
NP_001258665.1. NM_001271736.1. [P61923-4]
NP_057141.1. NM_016057.2. [P61923-1]
UniGeneiHs.505652.

Genome annotation databases

EnsembliENST00000262061; ENSP00000262061; ENSG00000111481. [P61923-1]
ENST00000455864; ENSP00000410620; ENSG00000111481. [P61923-3]
ENST00000549043; ENSP00000449270; ENSG00000111481. [P61923-4]
ENST00000552362; ENSP00000448444; ENSG00000111481. [P61923-5]
GeneIDi22818.
KEGGihsa:22818.
UCSCiuc001sfs.2. human. [P61923-1]
uc001sft.3. human.
uc010sot.2. human.

Polymorphism databases

DMDMi48428830.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047848 mRNA. Translation: BAB17659.1 .
AF151878 mRNA. Translation: AAD34115.1 .
AF161529 mRNA. Translation: AAF29144.1 .
AF086911 mRNA. Translation: AAP97141.1 .
AK293377 mRNA. Translation: BAG56889.1 .
AK295325 mRNA. Translation: BAG58302.1 .
AC078778 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96774.1 .
BC002849 mRNA. Translation: AAH02849.1 .
CCDSi CCDS61137.1. [P61923-5 ]
CCDS61138.1. [P61923-3 ]
CCDS61139.1. [P61923-4 ]
CCDS8877.1. [P61923-1 ]
RefSeqi NP_001258663.1. NM_001271734.1. [P61923-3 ]
NP_001258664.1. NM_001271735.1. [P61923-5 ]
NP_001258665.1. NM_001271736.1. [P61923-4 ]
NP_057141.1. NM_016057.2. [P61923-1 ]
UniGenei Hs.505652.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HF6 NMR - A 1-149 [» ]
ProteinModelPortali P61923.
SMRi P61923. Positions 1-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116495. 22 interactions.
DIPi DIP-29873N.
IntActi P61923. 2 interactions.
STRINGi 9606.ENSP00000262061.

PTM databases

PhosphoSitei P61923.

Polymorphism databases

DMDMi 48428830.

Proteomic databases

MaxQBi P61923.
PaxDbi P61923.
PRIDEi P61923.

Protocols and materials databases

DNASUi 22818.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262061 ; ENSP00000262061 ; ENSG00000111481 . [P61923-1 ]
ENST00000455864 ; ENSP00000410620 ; ENSG00000111481 . [P61923-3 ]
ENST00000549043 ; ENSP00000449270 ; ENSG00000111481 . [P61923-4 ]
ENST00000552362 ; ENSP00000448444 ; ENSG00000111481 . [P61923-5 ]
GeneIDi 22818.
KEGGi hsa:22818.
UCSCi uc001sfs.2. human. [P61923-1 ]
uc001sft.3. human.
uc010sot.2. human.

Organism-specific databases

CTDi 22818.
GeneCardsi GC12P054718.
HGNCi HGNC:2243. COPZ1.
HPAi HPA047727.
MIMi 615472. gene.
neXtProti NX_P61923.
PharmGKBi PA26760.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5541.
GeneTreei ENSGT00390000004405.
HOGENOMi HOG000214428.
HOVERGENi HBG051077.
InParanoidi P61923.
PhylomeDBi P61923.
TreeFami TF300262.

Enzyme and pathway databases

Reactomei REACT_11096. COPI Mediated Transport.

Miscellaneous databases

ChiTaRSi COPZ1. human.
EvolutionaryTracei P61923.
GeneWikii COPZ1.
GenomeRNAii 22818.
NextBioi 35471054.
PROi P61923.
SOURCEi Search...

Gene expression databases

Bgeei P61923.
CleanExi HS_COPZ1.
ExpressionAtlasi P61923. baseline and differential.
Genevestigatori P61923.

Family and domain databases

InterProi IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view ]
Pfami PF01217. Clat_adaptor_s. 1 hit.
[Graphical view ]
SUPFAMi SSF64356. SSF64356. 1 hit.
PROSITEi PS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of novel isoforms of COP I subunits."
    Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.
    J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  4. "Cloning and expression of a new human cDNA homology to B.taurus z-cop mRNA."
    Tu Q., Yu L., Hu P.R., Zhang H.L., Huang J., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 2 AND 3).
    Tissue: Caudate nucleus and Urinary bladder.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Placenta.
  9. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats."
    Yu W., Lin J., Jin C., Xia B.
    J. Mol. Biol. 386:903-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT, MUTAGENESIS OF 58-LYS-ILE-59 AND 87-GLU-LEU-88.

Entry informationi

Entry nameiCOPZ1_HUMAN
AccessioniPrimary (citable) accession number: P61923
Secondary accession number(s): B4DDX8
, B4DHZ0, F8VS17, F8VWL5, Q549N6, Q9Y3C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: October 29, 2014
This is version 102 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3