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Cytoskeleton-associated protein 4 (63-kDa cytoskeleton-linking membrane protein) (Climp-63) (p63)

 CKAP4_HUMAN             Reviewed;         602 AA.
Q07065; Q504S5; Q53ES6;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
05-DEC-2018, entry version 148.
RecName: Full=Cytoskeleton-associated protein 4;
AltName: Full=63-kDa cytoskeleton-linking membrane protein;
Short=Climp-63;
Short=p63;
Name=CKAP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 312-326; 413-429 AND
491-504, SUBCELLULAR LOCATION, AND PALMITOYLATION.
TISSUE=Placenta;
PubMed=8314870;
Schweizer A., Rohrer J., Jenoe P., De Maio A., Buchman T.G.,
Hauri H.-P.;
"A reversibly palmitoylated resident protein(p63) of an ER-Golgi
intermediate compartment is related to a circulatory shock
resuscitation protein.";
J. Cell Sci. 104:685-694(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION IN CYTOSKELETON ANCHORING, AND PHOSPHORYLATION AT SER-3;
SER-17 AND SER-19.
PubMed=15703217; DOI=10.1091/mbc.E04-07-0554;
Vedrenne C., Klopfenstein D.R., Hauri H.P.;
"Phosphorylation controls CLIMP-63-mediated anchoring of the
endoplasmic reticulum to microtubules.";
Mol. Biol. Cell 16:1928-1937(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
FUNCTION AS APF RECEPTOR, AND SUBCELLULAR LOCATION.
PubMed=17030514; DOI=10.1074/jbc.M604581200;
Conrads T.P., Tocci G.M., Hood B.L., Zhang C.O., Guo L., Koch K.R.,
Michejda C.J., Veenstra T.D., Keay S.K.;
"CKAP4/p63 is a receptor for the frizzled-8 protein-related
antiproliferative factor from interstitial cystitis patients.";
J. Biol. Chem. 281:37836-37843(2006).
[8]
FUNCTION IN CYTOSKELETON ANCHORING, AND SUBCELLULAR LOCATION.
PubMed=17567679; DOI=10.1242/jcs.008979;
Nikonov A.V., Hauri H.P., Lauring B., Kreibich G.;
"Climp-63-mediated binding of microtubules to the ER affects the
lateral mobility of translocon complexes.";
J. Cell Sci. 120:2248-2258(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-100 BY ZDHHC2.
PubMed=19144824; DOI=10.1091/mbc.E08-08-0849;
Planey S.L., Keay S.K., Zhang C.O., Zacharias D.A.;
"Palmitoylation of cytoskeleton associated protein 4 by DHHC2
regulates antiproliferative factor-mediated signaling.";
Mol. Biol. Cell 20:1454-1463(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
PHOSPHORYLATION AT SER-232.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: High-affinity epithelial cell surface receptor for APF.
-!- FUNCTION: Mediates the anchoring of the endoplasmic reticulum to
microtubules.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type II membrane protein. Cell membrane; Single-pass type II
membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear
region. Note=Translocates to the perinuclear region upon APF-
stimulation.
-!- PTM: Reversibly palmitoylated. Palmitoylation at Cys-100 by DHHC2
is required for its trafficking from the ER to the plasma membrane
and for its perinuclear localization.
{ECO:0000269|PubMed:19144824, ECO:0000269|PubMed:8314870}.
-!- PTM: Increased phosphorylation during mitosis prevents binding to
microtubules. {ECO:0000269|PubMed:15703217}.
-!- SEQUENCE CAUTION:
Sequence=AAH94824.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X69910; CAA49535.2; -; mRNA.
EMBL; AK223563; BAD97283.1; -; mRNA.
EMBL; AC079174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC082972; AAH82972.1; -; mRNA.
EMBL; BC094824; AAH94824.1; ALT_SEQ; mRNA.
CCDS; CCDS9103.1; -.
PIR; S33377; S33377.
RefSeq; NP_006816.2; NM_006825.3.
UniGene; Hs.74368; -.
ProteinModelPortal; Q07065; -.
SMR; Q07065; -.
BioGrid; 116167; 111.
IntAct; Q07065; 63.
MINT; Q07065; -.
STRING; 9606.ENSP00000367265; -.
iPTMnet; Q07065; -.
PhosphoSitePlus; Q07065; -.
SwissPalm; Q07065; -.
BioMuta; CKAP4; -.
DMDM; 74735614; -.
EPD; Q07065; -.
MaxQB; Q07065; -.
PaxDb; Q07065; -.
PeptideAtlas; Q07065; -.
PRIDE; Q07065; -.
ProteomicsDB; 58501; -.
Ensembl; ENST00000378026; ENSP00000367265; ENSG00000136026.
GeneID; 10970; -.
KEGG; hsa:10970; -.
UCSC; uc001tlk.4; human.
CTD; 10970; -.
DisGeNET; 10970; -.
EuPathDB; HostDB:ENSG00000136026.13; -.
GeneCards; CKAP4; -.
HGNC; HGNC:16991; CKAP4.
HPA; HPA000278; -.
HPA; HPA000792; -.
HPA; HPA001225; -.
neXtProt; NX_Q07065; -.
OpenTargets; ENSG00000136026; -.
PharmGKB; PA26527; -.
eggNOG; ENOG410IIRS; Eukaryota.
eggNOG; ENOG4111Q54; LUCA.
GeneTree; ENSGT00390000015968; -.
HOGENOM; HOG000060146; -.
HOVERGEN; HBG101940; -.
InParanoid; Q07065; -.
KO; K13999; -.
OMA; HQDFSRQ; -.
OrthoDB; EOG091G067G; -.
PhylomeDB; Q07065; -.
TreeFam; TF332395; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; CKAP4; human.
GeneWiki; CKAP4; -.
GenomeRNAi; 10970; -.
PRO; PR:Q07065; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000136026; Expressed in 243 organ(s), highest expression level in tibia.
CleanEx; HS_CKAP4; -.
ExpressionAtlas; Q07065; baseline and differential.
Genevisible; Q07065; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0042599; C:lamellar body; TAS:Reactome.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
InterPro; IPR028428; Ckap4.
PANTHER; PTHR45161; PTHR45161; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Endoplasmic reticulum;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 602 Cytoskeleton-associated protein 4.
/FTId=PRO_0000252417.
TOPO_DOM 1 106 Cytoplasmic. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TOPO_DOM 128 602 Extracellular. {ECO:0000255}.
COILED 130 214 {ECO:0000255}.
COILED 256 460 {ECO:0000255}.
COILED 533 602 {ECO:0000255}.
COMPBIAS 36 59 Pro-rich.
COMPBIAS 71 77 Poly-Gly.
COMPBIAS 85 94 Poly-Ala.
COMPBIAS 118 121 Poly-Ala.
MOD_RES 3 3 Phosphoserine.
{ECO:0000269|PubMed:15703217}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15703217}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000269|PubMed:15703217}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BMK4}.
MOD_RES 232 232 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
LIPID 100 100 S-palmitoyl cysteine; by ZDHHC2.
{ECO:0000269|PubMed:19144824}.
VARIANT 348 348 A -> T (in dbSNP:rs3088113).
/FTId=VAR_027853.
CONFLICT 60 60 Q -> R (in Ref. 2; BAD97283).
{ECO:0000305}.
CONFLICT 362 362 S -> P (in Ref. 4; AAH94824).
{ECO:0000305}.
SEQUENCE 602 AA; 66022 MW; 216E6A92ED5E058A CRC64;
MPSAKQRGSK GGHGAASPSE KGAHPSGGAD DVAKKPPPAP QQPPPPPAPH PQQHPQQHPQ
NQAHGKGGHR GGGGGGGKSS SSSSASAAAA AAAASSSASC SRRLGRALNF LFYLALVAAA
AFSGWCVHHV LEEVQQVRRS HQDFSRQREE LGQGLQGVEQ KVQSLQATFG TFESILRSSQ
HKQDLTEKAV KQGESEVSRI SEVLQKLQNE ILKDLSDGIH VVKDARERDF TSLENTVEER
LTELTKSIND NIAIFTEVQK RSQKEINDMK AKVASLEESE GNKQDLKALK EAVKEIQTSA
KSREWDMEAL RSTLQTMESD IYTEVRELVS LKQEQQAFKE AADTERLALQ ALTEKLLRSE
ESVSRLPEEI RRLEEELRQL KSDSHGPKED GGFRHSEAFE ALQQKSQGLD SRLQHVEDGV
LSMQVASARQ TESLESLLSK SQEHEQRLAA LQGRLEGLGS SEADQDGLAS TVRSLGETQL
VLYGDVEELK RSVGELPSTV ESLQKVQEQV HTLLSQDQAQ AARLPPQDFL DRLSSLDNLK
ASVSQVEADL KMLRTAVDSL VAYSVKIETN ENNLESAKGL LDDLRNDLDR LFVKVEKIHE
KV


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