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TTC33_HUMAN
ID   TTC33_HUMAN             Reviewed;         262 AA.
AC   Q6PID6; B2R6G0; O95105;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Tetratricopeptide repeat protein 33;
DE            Short=TPR repeat protein 33;
DE   AltName: Full=Osmosis-responsive factor;
GN   Name=TTC33;
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 [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Giot J.F.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-251, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP   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).
CC   -!- INTERACTION:
CC       Q6PID6; P02649: APOE; NbExp=3; IntAct=EBI-2555404, EBI-1222467;
CC       Q6PID6; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2555404, EBI-21553822;
CC       Q6PID6; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2555404, EBI-12593112;
CC       Q6PID6; O14645: DNALI1; NbExp=3; IntAct=EBI-2555404, EBI-395638;
CC       Q6PID6; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-2555404, EBI-21603100;
CC       Q6PID6; O14901: KLF11; NbExp=3; IntAct=EBI-2555404, EBI-948266;
CC       Q6PID6; Q8WV92: MITD1; NbExp=3; IntAct=EBI-2555404, EBI-2691489;
CC       Q6PID6; Q92597: NDRG1; NbExp=3; IntAct=EBI-2555404, EBI-716486;
CC       Q6PID6; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2555404, EBI-2811583;
CC       Q6PID6; P20618: PSMB1; NbExp=3; IntAct=EBI-2555404, EBI-372273;
CC       Q6PID6; P56279: TCL1A; NbExp=7; IntAct=EBI-2555404, EBI-749995;
CC       Q6PID6; P40222: TXLNA; NbExp=6; IntAct=EBI-2555404, EBI-359793;
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DR   EMBL; AF023244; AAD09341.1; -; mRNA.
DR   EMBL; AK312560; BAG35457.1; -; mRNA.
DR   EMBL; CH471119; EAW55998.1; -; Genomic_DNA.
DR   EMBL; BC015701; AAH15701.1; -; mRNA.
DR   EMBL; BC036536; AAH36536.1; -; mRNA.
DR   CCDS; CCDS3931.1; -.
DR   RefSeq; NP_036514.1; NM_012382.2.
DR   RefSeq; XP_011512305.1; XM_011514003.2.
DR   AlphaFoldDB; Q6PID6; -.
DR   SMR; Q6PID6; -.
DR   BioGRID; 117092; 48.
DR   IntAct; Q6PID6; 32.
DR   MINT; Q6PID6; -.
DR   STRING; 9606.ENSP00000338533; -.
DR   GlyGen; Q6PID6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6PID6; -.
DR   PhosphoSitePlus; Q6PID6; -.
DR   BioMuta; TTC33; -.
DR   DMDM; 147737109; -.
DR   EPD; Q6PID6; -.
DR   jPOST; Q6PID6; -.
DR   MassIVE; Q6PID6; -.
DR   MaxQB; Q6PID6; -.
DR   PaxDb; Q6PID6; -.
DR   PeptideAtlas; Q6PID6; -.
DR   PRIDE; Q6PID6; -.
DR   ProteomicsDB; 67149; -.
DR   Antibodypedia; 23145; 186 antibodies from 23 providers.
DR   DNASU; 23548; -.
DR   Ensembl; ENST00000337702.5; ENSP00000338533.4; ENSG00000113638.14.
DR   GeneID; 23548; -.
DR   KEGG; hsa:23548; -.
DR   MANE-Select; ENST00000337702.5; ENSP00000338533.4; NM_012382.3; NP_036514.1.
DR   UCSC; uc003jma.4; human.
DR   CTD; 23548; -.
DR   DisGeNET; 23548; -.
DR   GeneCards; TTC33; -.
DR   HGNC; HGNC:29959; TTC33.
DR   HPA; ENSG00000113638; Low tissue specificity.
DR   neXtProt; NX_Q6PID6; -.
DR   OpenTargets; ENSG00000113638; -.
DR   PharmGKB; PA162407196; -.
DR   VEuPathDB; HostDB:ENSG00000113638; -.
DR   eggNOG; KOG0553; Eukaryota.
DR   GeneTree; ENSGT00390000017462; -.
DR   HOGENOM; CLU_1061581_0_0_1; -.
DR   InParanoid; Q6PID6; -.
DR   OMA; DDGNWLH; -.
DR   OrthoDB; 1579428at2759; -.
DR   PhylomeDB; Q6PID6; -.
DR   TreeFam; TF332142; -.
DR   PathwayCommons; Q6PID6; -.
DR   SignaLink; Q6PID6; -.
DR   BioGRID-ORCS; 23548; 10 hits in 1074 CRISPR screens.
DR   ChiTaRS; TTC33; human.
DR   GenomeRNAi; 23548; -.
DR   Pharos; Q6PID6; Tdark.
DR   PRO; PR:Q6PID6; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q6PID6; protein.
DR   Bgee; ENSG00000113638; Expressed in calcaneal tendon and 189 other tissues.
DR   ExpressionAtlas; Q6PID6; baseline and differential.
DR   Genevisible; Q6PID6; HS.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..262
FT                   /note="Tetratricopeptide repeat protein 33"
FT                   /id="PRO_0000287515"
FT   REPEAT          59..92
FT                   /note="TPR 1"
FT   REPEAT          93..126
FT                   /note="TPR 2"
FT   REPEAT          127..160
FT                   /note="TPR 3"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         251
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         69
FT                   /note="L -> M (in dbSNP:rs837105)"
FT                   /id="VAR_032317"
FT   CONFLICT        13
FT                   /note="K -> R (in Ref. 4; AAH36536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  29411 MW;  A5549AC3973FABC9 CRC64;
     MASFGWKRKI GEKVSKVTSQ QFEAEAADEK DVVDNDEGNW LHAIKRRKEI LLEGCAEKSK
     QLKDEGASLA ENKRYREAIQ KWDEALQLTP NDATLYEMKS QVLMSLHEMF PAVHAAEMAV
     QQNPHSWESW QTLGRAQLGL GEIILAIRSF QVALHIYPMN PEIWKEDLSW ARTLQEQQKV
     AQRIKKSEAP AEVTHFSPKS IPDYDFESDE IVAVCAAIAE KEKTVSANKT MVIVSASGAI
     ETVTEKEDGA TPPDGSVFIK AR
 
 
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