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CC134_HUMAN
ID   CC134_HUMAN             Reviewed;         229 AA.
AC   Q9H6E4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Coiled-coil domain-containing protein 134;
DE   Flags: Precursor;
GN   Name=CCDC134;
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 MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney epithelium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary carcinoma;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-27, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=18087676; DOI=10.1007/s00018-007-7448-5;
RA   Huang J., Shi T., Ma T., Zhang Y., Ma X., Lu Y., Song Q., Liu W., Ma D.,
RA   Qiu X.;
RT   "CCDC134, a novel secretory protein, inhibits activation of ERK and JNK,
RT   but not p38 MAPK.";
RL   Cell. Mol. Life Sci. 65:338-349(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   FUNCTION, INTERACTION WITH TADA2A, ASSOCIATION WITH THE PCAF COMPLEX,
RP   SUBCELLULAR LOCATION, AND MOTIF.
RX   PubMed=22644376; DOI=10.1007/s00418-012-0932-5;
RA   Huang J., Zhang L., Liu W., Liao Q., Shi T., Xiao L., Hu F., Qiu X.;
RT   "CCDC134 interacts with hADA2a and functions as a regulator of hADA2a in
RT   acetyltransferase activity, DNA damage-induced apoptosis and cell cycle
RT   arrest.";
RL   Histochem. Cell Biol. 138:41-55(2012).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23070808; DOI=10.1007/s11010-012-1418-4;
RA   Zhong J., Zhao M., Luo Q., Ma Y., Liu J., Wang J., Yang M., Yuan X.,
RA   Sang J., Huang C.;
RT   "CCDC134 is down-regulated in gastric cancer and its silencing promotes
RT   cell migration and invasion of GES-1 and AGS cells via the MAPK pathway.";
RL   Mol. Cell. Biochem. 372:1-8(2013).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=25125657; DOI=10.1158/0008-5472.can-13-3132;
RA   Huang J., Xiao L., Gong X., Shao W., Yin Y., Liao Q., Meng Y., Zhang Y.,
RA   Ma D., Qiu X.;
RT   "Cytokine-like molecule CCDC134 contributes to CD8(+) T-cell effector
RT   functions in cancer immunotherapy.";
RL   Cancer Res. 74:5734-5745(2014).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: In extracellular secreted form, promotes proliferation and
CC       activation of CD8(+) T cells, suggesting a cytokine-like function
CC       (PubMed:25125657). Enhances cytotoxic anti-tumor activity of CD8(+) T
CC       cells (PubMed:25125657). May inhibit ERK and JNK signaling activity
CC       (PubMed:18087676, PubMed:23070808). May suppress cell migration and
CC       invasion activity, via its effects on ERK and JNK signaling
CC       (PubMed:23070808). {ECO:0000269|PubMed:18087676,
CC       ECO:0000269|PubMed:23070808, ECO:0000269|PubMed:25125657}.
CC   -!- FUNCTION: In the nucleus, enhances stability of the PCAF histone
CC       acetyltransferase (HAT) complex member TADA2A and thus promotes PCAF-
CC       mediated H3K14 and H4K8 HAT activity. May inhibit TADA2A-mediated
CC       TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and
CC       transcriptional activity. May also promote TADA2A-mediated XRCC6
CC       acetylation thus facilitating cell apoptosis in response to DNA damage.
CC       {ECO:0000269|PubMed:22644376}.
CC   -!- SUBUNIT: Interacts with TADA2A. Associates with the PCAF complex via
CC       TADA2A binding. {ECO:0000269|PubMed:22644376}.
CC   -!- INTERACTION:
CC       Q9H6E4; O00264: PGRMC1; NbExp=3; IntAct=EBI-953766, EBI-1045534;
CC       Q9H6E4; Q16849-3: PTPRN; NbExp=3; IntAct=EBI-953766, EBI-10200782;
CC       Q9H6E4; O75478: TADA2A; NbExp=6; IntAct=EBI-953766, EBI-742268;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22644376}. Cytoplasm
CC       {ECO:0000269|PubMed:22644376}. Secreted {ECO:0000269|PubMed:18087676}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:18087676}. Note=Accumulates
CC       in the nucleus in response to UV irradiation (PubMed:22644376).
CC       {ECO:0000269|PubMed:22644376}.
CC   -!- TISSUE SPECIFICITY: Expressed in cervical gland, cervical squamous
CC       epithelium, endometrium, stomach, kidney distal convoluted tubule,
CC       spermatogenic cells in testis, mammary gland, liver and striated muscle
CC       (at protein level) (PubMed:18087676, PubMed:23070808). Also detected in
CC       placenta (PubMed:18087676). Highest expression in testis relative to
CC       other tissues (PubMed:18087676). Detected in T cells and dendritic
CC       cells; highly expressed in activated CD8(+) T cells, and also expressed
CC       at lower levels in CD4(+) T cells (PubMed:25125657).
CC       {ECO:0000269|PubMed:18087676, ECO:0000269|PubMed:23070808,
CC       ECO:0000269|PubMed:25125657}.
CC   -!- PTM: O-glycosylated, with additional sialic acid modifications.
CC       {ECO:0000269|PubMed:18087676}.
CC   -!- SIMILARITY: Belongs to the CCDC134 family. {ECO:0000305}.
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DR   EMBL; CR456484; CAG30370.1; -; mRNA.
DR   EMBL; AK026002; BAB15315.1; -; mRNA.
DR   EMBL; AL021453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017693; AAH17693.1; -; mRNA.
DR   CCDS; CCDS33654.1; -.
DR   RefSeq; NP_079097.1; NM_024821.3.
DR   RefSeq; XP_005261805.1; XM_005261748.3.
DR   AlphaFoldDB; Q9H6E4; -.
DR   BioGRID; 122966; 26.
DR   IntAct; Q9H6E4; 6.
DR   STRING; 9606.ENSP00000255784; -.
DR   iPTMnet; Q9H6E4; -.
DR   PhosphoSitePlus; Q9H6E4; -.
DR   BioMuta; CCDC134; -.
DR   DMDM; 74752694; -.
DR   EPD; Q9H6E4; -.
DR   jPOST; Q9H6E4; -.
DR   MassIVE; Q9H6E4; -.
DR   MaxQB; Q9H6E4; -.
DR   PaxDb; Q9H6E4; -.
DR   PeptideAtlas; Q9H6E4; -.
DR   PRIDE; Q9H6E4; -.
DR   ProteomicsDB; 80982; -.
DR   Antibodypedia; 289; 229 antibodies from 29 providers.
DR   DNASU; 79879; -.
DR   Ensembl; ENST00000255784.6; ENSP00000255784.5; ENSG00000100147.14.
DR   GeneID; 79879; -.
DR   KEGG; hsa:79879; -.
DR   MANE-Select; ENST00000255784.6; ENSP00000255784.5; NM_024821.5; NP_079097.1.
DR   UCSC; uc003bbh.2; human.
DR   CTD; 79879; -.
DR   DisGeNET; 79879; -.
DR   GeneCards; CCDC134; -.
DR   HGNC; HGNC:26185; CCDC134.
DR   HPA; ENSG00000100147; Low tissue specificity.
DR   MIM; 618788; gene.
DR   neXtProt; NX_Q9H6E4; -.
DR   OpenTargets; ENSG00000100147; -.
DR   PharmGKB; PA162381361; -.
DR   VEuPathDB; HostDB:ENSG00000100147; -.
DR   eggNOG; ENOG502QVE7; Eukaryota.
DR   GeneTree; ENSGT00390000020164; -.
DR   HOGENOM; CLU_099195_0_0_1; -.
DR   InParanoid; Q9H6E4; -.
DR   OMA; NPFKADH; -.
DR   OrthoDB; 1509108at2759; -.
DR   PhylomeDB; Q9H6E4; -.
DR   TreeFam; TF323839; -.
DR   PathwayCommons; Q9H6E4; -.
DR   SignaLink; Q9H6E4; -.
DR   BioGRID-ORCS; 79879; 23 hits in 1083 CRISPR screens.
DR   ChiTaRS; CCDC134; human.
DR   GenomeRNAi; 79879; -.
DR   Pharos; Q9H6E4; Tbio.
DR   PRO; PR:Q9H6E4; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9H6E4; protein.
DR   Bgee; ENSG00000100147; Expressed in adrenal tissue and 127 other tissues.
DR   ExpressionAtlas; Q9H6E4; baseline and differential.
DR   Genevisible; Q9H6E4; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR   GO; GO:1990402; P:embryonic liver development; IEA:Ensembl.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR   InterPro; IPR026321; Coiled-coil_dom_con_pro_134.
DR   PANTHER; PTHR14735; PTHR14735; 1.
DR   Pfam; PF15002; ERK-JNK_inhib; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW   Nucleus; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:18087676"
FT   CHAIN           23..229
FT                   /note="Coiled-coil domain-containing protein 134"
FT                   /id="PRO_0000254109"
FT   REGION          193..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          196..218
FT                   /evidence="ECO:0000255"
FT   MOTIF           206..213
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768,
FT                   ECO:0000269|PubMed:22644376"
FT   COMPBIAS        197..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  26561 MW;  F14C6797854B0598 CRC64;
     MDLLQFLAFL FVLLLSGMGA TGTLRTSLDP SLEIYKKMFE VKRREQLLAL KNLAQLNDIH
     QQYKILDVML KGLFKVLEDS RTVLTAADVL PDGPFPQDEK LKDAFSHVVE NTAFFGDVVL
     RFPRIVHYYF DHNSNWNLLI RWGISFCNQT GVFNQGPHSP ILSLMAQELG ISEKDSNFQN
     PFKIDRTEFI PSTDPFQKAL REEEKRRKKE EKRKEIRKGP RISRSQSEL
 
 
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