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Protein

Copine-3

Gene

CPNE3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation (PubMed:20010870).1 Publication

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • transporter activity Source: ProtInc

GO - Biological processi

  • cellular response to calcium ion Source: UniProtKB
  • cellular response to growth factor stimulus Source: UniProtKB
  • ERBB2 signaling pathway Source: UniProtKB
  • glycerophospholipid biosynthetic process Source: Reactome
  • lipid metabolic process Source: ProtInc
  • phospholipid metabolic process Source: Reactome
  • positive regulation of cell migration Source: UniProtKB
  • protein phosphorylation Source: GOC
  • small molecule metabolic process Source: Reactome
  • vesicle-mediated transport Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-1483206. Glycerophospholipid biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Copine-3Curated
Alternative name(s):
Copine III1 PublicationImported
Gene namesi
Name:CPNE3Imported
Synonyms:CPN3, KIAA06361 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2316. CPNE3.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26833.

Polymorphism and mutation databases

BioMutaiCPNE3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 537537Copine-3PRO_0000144838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine and threonine residues (PubMed:11041869).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75131.
MaxQBiO75131.
PaxDbiO75131.
PeptideAtlasiO75131.
PRIDEiO75131.

PTM databases

iPTMnetiO75131.
PhosphoSiteiO75131.
SwissPalmiO75131.

Expressioni

Tissue specificityi

Expressed in breast and weakly in prostate and ovarian tissues (PubMed:20010870). Expressed in neutrophils (at protein level) (PubMed:12949241). Widely expressed (PubMed:11041869). Expressed in the brain. Expressed in neutrophil precursors from the bone marrow and peripheral blood (PubMed:12949241). Expressed in primary breast tumors and ovarian endometrioid adenocarcinoma (PubMed:20010870).3 Publications

Gene expression databases

BgeeiO75131.
CleanExiHS_CPNE3.
ExpressionAtlasiO75131. baseline and differential.
GenevisibleiO75131. HS.

Organism-specific databases

HPAiHPA029552.

Interactioni

Subunit structurei

Monomer (PubMed:12949241). Interacts with ERBB2 (preferentially with the tyrosine phosphorylated form); this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (PubMed:20010870). Interacts with SHC1; this interaction may mediate the binding of CPNE3 with ERBB2 (PubMed:20010870). Interacts with RACK1 (PubMed:20010870).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TINF2Q9BSI42EBI-718988,EBI-717399

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114412. 18 interactions.
IntActiO75131. 9 interactions.
MINTiMINT-4526920.
STRINGi9606.ENSP00000198765.

Structurei

3D structure databases

ProteinModelPortaliO75131.
SMRiO75131. Positions 17-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9998C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 230106C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 513223VWFAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the copine family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1327. Eukaryota.
ENOG410XPC8. LUCA.
GeneTreeiENSGT00760000119085.
HOGENOMiHOG000220898.
HOVERGENiHBG066841.
InParanoidiO75131.
OMAiIDYYFEL.
OrthoDBiEOG77DJ57.
PhylomeDBiO75131.
TreeFamiTF316419.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR010734. Copine.
IPR002035. VWF_A.
[Graphical view]
PfamiPF00168. C2. 2 hits.
PF07002. Copine. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF53300. SSF53300. 1 hit.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75131-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER
60 70 80 90 100
IKNCLNPQFS KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC
110 120 130 140 150
TLGQIVSSKK LTRPLVMKTG RPAGKGSITI SAEEIKDNRV VLFEMEARKL
160 170 180 190 200
DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT EVVKNNLNPV WRPFKISLNS
210 220 230 240 250
LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS RSSPVEFECI
260 270 280 290 300
NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG
310 320 330 340 350
SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ
360 370 380 390 400
IPPQWQVSHE FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI
410 420 430 440 450
INHVARFAAA ATQQQTASQY FVLLIITDGV ITDLDETRQA IVNASRLPMS
460 470 480 490 500
IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE VAIRDIVQFV PFRQFQNAPK
510 520 530
EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ
Length:537
Mass (Da):60,131
Last modified:November 1, 1998 - v1
Checksum:i91F2C5EAD611B842
GO

Sequence cautioni

The sequence BAA31611.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 3941P → Q in AAH36242 (PubMed:15489334).Curated
Sequence conflicti419 – 4191Q → R in AAH36242 (PubMed:15489334).Curated
Sequence conflicti475 – 4751R → H in AAH36242 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti252 – 2521E → D.
Corresponds to variant rs41333046 [ dbSNP | Ensembl ].
VAR_048848
Natural varianti412 – 4121T → M.1 Publication
Corresponds to variant rs2304789 [ dbSNP | Ensembl ].
VAR_024424

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077226 mRNA. Translation: AAD46074.2.
AB014536 mRNA. Translation: BAA31611.2. Different initiation.
AK292912 mRNA. Translation: BAF85601.1.
BC036242 mRNA. Translation: AAH36242.1.
BC066597 mRNA. Translation: AAH66597.1.
CCDSiCCDS6243.1.
RefSeqiNP_003900.1. NM_003909.4.
XP_005251150.1. XM_005251093.3.
UniGeneiHs.191219.

Genome annotation databases

EnsembliENST00000198765; ENSP00000198765; ENSG00000085719.
ENST00000517490; ENSP00000477590; ENSG00000085719.
GeneIDi8895.
KEGGihsa:8895.
UCSCiuc033bsf.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077226 mRNA. Translation: AAD46074.2.
AB014536 mRNA. Translation: BAA31611.2. Different initiation.
AK292912 mRNA. Translation: BAF85601.1.
BC036242 mRNA. Translation: AAH36242.1.
BC066597 mRNA. Translation: AAH66597.1.
CCDSiCCDS6243.1.
RefSeqiNP_003900.1. NM_003909.4.
XP_005251150.1. XM_005251093.3.
UniGeneiHs.191219.

3D structure databases

ProteinModelPortaliO75131.
SMRiO75131. Positions 17-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114412. 18 interactions.
IntActiO75131. 9 interactions.
MINTiMINT-4526920.
STRINGi9606.ENSP00000198765.

PTM databases

iPTMnetiO75131.
PhosphoSiteiO75131.
SwissPalmiO75131.

Polymorphism and mutation databases

BioMutaiCPNE3.

Proteomic databases

EPDiO75131.
MaxQBiO75131.
PaxDbiO75131.
PeptideAtlasiO75131.
PRIDEiO75131.

Protocols and materials databases

DNASUi8895.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000198765; ENSP00000198765; ENSG00000085719.
ENST00000517490; ENSP00000477590; ENSG00000085719.
GeneIDi8895.
KEGGihsa:8895.
UCSCiuc033bsf.1. human.

Organism-specific databases

CTDi8895.
GeneCardsiCPNE3.
HGNCiHGNC:2316. CPNE3.
HPAiHPA029552.
MIMi604207. gene.
neXtProtiNX_O75131.
PharmGKBiPA26833.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1327. Eukaryota.
ENOG410XPC8. LUCA.
GeneTreeiENSGT00760000119085.
HOGENOMiHOG000220898.
HOVERGENiHBG066841.
InParanoidiO75131.
OMAiIDYYFEL.
OrthoDBiEOG77DJ57.
PhylomeDBiO75131.
TreeFamiTF316419.

Enzyme and pathway databases

ReactomeiR-HSA-1483206. Glycerophospholipid biosynthesis.

Miscellaneous databases

ChiTaRSiCPNE3. human.
GenomeRNAii8895.
NextBioi33407.
PROiO75131.
SOURCEiSearch...

Gene expression databases

BgeeiO75131.
CleanExiHS_CPNE3.
ExpressionAtlasiO75131. baseline and differential.
GenevisibleiO75131. HS.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR010734. Copine.
IPR002035. VWF_A.
[Graphical view]
PfamiPF00168. C2. 2 hits.
PF07002. Copine. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF53300. SSF53300. 1 hit.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human copine III as a phosphoprotein with associated kinase activity."
    Caudell E.G., Caudell J.J., Tang C.-H., Yu T.-K., Frederick M.J., Grimm E.A.
    Biochemistry 39:13034-13043(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, PHOSPHORYLATION.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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], VARIANT MET-412.
    Tissue: Trachea.
  4. "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: Brain and Skin.
  5. "Tissue expression of copines and isolation of copines I and III from the cytosol of human neutrophils."
    Cowland J.B., Carter D., Bjerregaard M.D., Johnsen A.H., Borregaard N., Lollike K.
    J. Leukoc. Biol. 74:379-388(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Copines-1, -2, -3, -6 and -7 show different calcium-dependent intracellular membrane translocation and targeting."
    Perestenko P.V., Pooler A.M., Noorbakhshnia M., Gray A., Bauccio C., Jeffrey McIlhinney R.A.
    FEBS J. 277:5174-5189(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: FUNCTION, INTERACTION WITH ERBB2; RACK1 AND SHC1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCPNE3_HUMAN
AccessioniPrimary (citable) accession number: O75131
Secondary accession number(s): A8KA47, Q8IYA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: March 16, 2016
This is version 140 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

Caution

Was reported to have a protein kinase activity.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.