CC85C_HUMAN
ID CC85C_HUMAN Reviewed; 419 AA.
AC A6NKD9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Coiled-coil domain-containing protein 85C;
GN Name=CCDC85C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP FUNCTION, INTERACTION WITH ARVCF; CTNND1; CTNND2 AND PKP4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
CC -!- FUNCTION: May play a role in cell-cell adhesion and epithelium
CC development through its interaction with proteins of the beta-catenin
CC family (Probable). May play an important role in cortical development,
CC especially in the maintenance of radial glia (By similarity).
CC {ECO:0000250|UniProtKB:E9Q6B2, ECO:0000305|PubMed:25009281}.
CC -!- SUBUNIT: May interact with ARVCF, CTNND1, CTNND2 and PKP4.
CC {ECO:0000305|PubMed:25009281}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:E9Q6B2}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:25009281}. Note=Localizes to the apical junction of
CC radial glia in the wall of lateral ventricles of the developing brain.
CC Colocalizes with TJP1 on the meshwork-like structure of adherens
CC junctions on the lateral ventricles wall.
CC {ECO:0000250|UniProtKB:E9Q6B2}.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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DR EMBL; AL110504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS45161.1; -.
DR RefSeq; NP_001138467.1; NM_001144995.1.
DR AlphaFoldDB; A6NKD9; -.
DR SMR; A6NKD9; -.
DR BioGRID; 130463; 114.
DR DIP; DIP-56878N; -.
DR IntAct; A6NKD9; 50.
DR MINT; A6NKD9; -.
DR STRING; 9606.ENSP00000369592; -.
DR GlyGen; A6NKD9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NKD9; -.
DR PhosphoSitePlus; A6NKD9; -.
DR BioMuta; CCDC85C; -.
DR EPD; A6NKD9; -.
DR jPOST; A6NKD9; -.
DR MassIVE; A6NKD9; -.
DR MaxQB; A6NKD9; -.
DR PaxDb; A6NKD9; -.
DR PeptideAtlas; A6NKD9; -.
DR PRIDE; A6NKD9; -.
DR ProteomicsDB; 1405; -.
DR Antibodypedia; 54727; 80 antibodies from 15 providers.
DR DNASU; 317762; -.
DR Ensembl; ENST00000380243.9; ENSP00000369592.4; ENSG00000205476.9.
DR GeneID; 317762; -.
DR KEGG; hsa:317762; -.
DR MANE-Select; ENST00000380243.9; ENSP00000369592.4; NM_001144995.2; NP_001138467.1.
DR UCSC; uc010avr.4; human.
DR CTD; 317762; -.
DR DisGeNET; 317762; -.
DR GeneCards; CCDC85C; -.
DR HGNC; HGNC:35459; CCDC85C.
DR HPA; ENSG00000205476; Tissue enhanced (brain).
DR neXtProt; NX_A6NKD9; -.
DR OpenTargets; ENSG00000205476; -.
DR PharmGKB; PA164717760; -.
DR VEuPathDB; HostDB:ENSG00000205476; -.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000159071; -.
DR HOGENOM; CLU_028762_0_0_1; -.
DR InParanoid; A6NKD9; -.
DR OMA; NGLACPA; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; A6NKD9; -.
DR TreeFam; TF320243; -.
DR PathwayCommons; A6NKD9; -.
DR SignaLink; A6NKD9; -.
DR BioGRID-ORCS; 317762; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; CCDC85C; human.
DR GenomeRNAi; 317762; -.
DR Pharos; A6NKD9; Tbio.
DR PRO; PR:A6NKD9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A6NKD9; protein.
DR Bgee; ENSG00000205476; Expressed in right hemisphere of cerebellum and 138 other tissues.
DR ExpressionAtlas; A6NKD9; baseline and differential.
DR Genevisible; A6NKD9; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Coiled coil; Developmental protein;
KW Phosphoprotein; Reference proteome; Tight junction.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..419
FT /note="Coiled-coil domain-containing protein 85C"
FT /id="PRO_0000345410"
FT REGION 162..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..88
FT /evidence="ECO:0000255"
FT COILED 118..159
FT /evidence="ECO:0000255"
FT COMPBIAS 238..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
SQ SEQUENCE 419 AA; 45210 MW; 01A8F447CE951007 CRC64;
MAKPAATAAA ASEELSQVPD EELLRWSKEE LARRLRRAEG EKVGLMLEHG GLMRDVNRRL
QQHLLEIRGL KDVNQRLQDD NQELRELCCF LDDDRQKGRK LAREWQRFGR HAAGAVWHEV
ARSQQKLREL EARQEALLRE NLELKELVLL LDEERAALAA TGAASGGGGG GGGAGSRSSI
DSQASLSGPL SGGAPGAGAR DVGDGSSTSS AGSGGSPDHH HHVPPPLLPP GPHKAPDGKA
GATRRSLDDL SAPPHHRSIP NGLHDPSSTY IRQLESKVRL LEGDKLLAQQ AGSGEFRTLR
KGFSPYHSES QLASLPPSYQ DSLQNGPACP APELPSPPSA GYSPAGQKPE AVVHAMKVLE
VHENLDRQLQ DSCEEDLSEK EKAIVREMCN VVWRKLGDAA SSKPSIRQHL SGNQFKGPL
