位置:首页 > 蛋白库 > TPGS1_HUMAN
TPGS1_HUMAN
ID   TPGS1_HUMAN             Reviewed;         290 AA.
AC   Q6ZTW0; Q96GE2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Tubulin polyglutamylase complex subunit 1 {ECO:0000305};
DE            Short=PGs1;
GN   Name=TPGS1 {ECO:0000312|HGNC:HGNC:25058}; Synonyms=C19orf20;
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] (ISOFORM 2).
RC   TISSUE=Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-290 (ISOFORM 1).
RC   TISSUE=Placenta;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [4]
RP   INTERACTION WITH PCM1; CSTPP1 AND LRRC49, AND SUBCELLULAR LOCATION.
RX   PubMed=34782749; DOI=10.1038/s41422-021-00584-9;
RA   Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H.,
RA   Sanchez I., Dynlacht B.D.;
RT   "Regulators of tubulin polyglutamylation control nuclear shape and cilium
RT   disassembly by balancing microtubule and actin assembly.";
RL   Cell Res. 32:190-209(2022).
CC   -!- FUNCTION: Subunit of the tubulin polyglutamylase complex (TPGC). The
CC       complex mediates cilia and flagella polyglutamylation which is
CC       essential for their biogenesis and motility (Probable). May act in the
CC       targeting of the tubulin polyglutamylase complex. Required for the
CC       development of the spermatid flagellum (By similarity).
CC       {ECO:0000250|UniProtKB:Q99MS8, ECO:0000305|PubMed:34782749}.
CC   -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC       contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1 (Probable). Interacts
CC       with PCM1, CSTPP1 and LRRC49 (PubMed:34782749).
CC       {ECO:0000269|PubMed:34782749, ECO:0000305|PubMed:34782749}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, cilium
CC       basal body {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton,
CC       flagellum basal body {ECO:0000250|UniProtKB:Q99MS8}. Cell projection,
CC       axon {ECO:0000250|UniProtKB:Q99MS8}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q99MS8}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q99MS8}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriolar satellite {ECO:0000269|PubMed:34782749}. Note=Associated
CC       with microtubules from neurites, centrosomes, basal bodies and
CC       axonemes. {ECO:0000250|UniProtKB:Q99MS8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZTW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZTW0-2; Sequence=VSP_020401;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK126170; BAC86469.1; -; mRNA.
DR   EMBL; BC009520; AAH09520.1; -; mRNA.
DR   CCDS; CCDS42454.1; -. [Q6ZTW0-1]
DR   RefSeq; NP_277048.2; NM_033513.2. [Q6ZTW0-1]
DR   AlphaFoldDB; Q6ZTW0; -.
DR   BioGRID; 124900; 71.
DR   IntAct; Q6ZTW0; 24.
DR   STRING; 9606.ENSP00000352265; -.
DR   iPTMnet; Q6ZTW0; -.
DR   PhosphoSitePlus; Q6ZTW0; -.
DR   BioMuta; TPGS1; -.
DR   DMDM; 114152292; -.
DR   EPD; Q6ZTW0; -.
DR   jPOST; Q6ZTW0; -.
DR   MassIVE; Q6ZTW0; -.
DR   MaxQB; Q6ZTW0; -.
DR   PaxDb; Q6ZTW0; -.
DR   PeptideAtlas; Q6ZTW0; -.
DR   PRIDE; Q6ZTW0; -.
DR   ProteomicsDB; 68296; -. [Q6ZTW0-1]
DR   ProteomicsDB; 68297; -. [Q6ZTW0-2]
DR   Antibodypedia; 53504; 20 antibodies from 10 providers.
DR   DNASU; 91978; -.
DR   Ensembl; ENST00000359315.6; ENSP00000352265.4; ENSG00000141933.9. [Q6ZTW0-1]
DR   GeneID; 91978; -.
DR   KEGG; hsa:91978; -.
DR   MANE-Select; ENST00000359315.6; ENSP00000352265.4; NM_033513.3; NP_277048.2.
DR   UCSC; uc002lou.4; human. [Q6ZTW0-1]
DR   CTD; 91978; -.
DR   GeneCards; TPGS1; -.
DR   HGNC; HGNC:25058; TPGS1.
DR   HPA; ENSG00000141933; Low tissue specificity.
DR   neXtProt; NX_Q6ZTW0; -.
DR   OpenTargets; ENSG00000141933; -.
DR   PharmGKB; PA134901246; -.
DR   VEuPathDB; HostDB:ENSG00000141933; -.
DR   eggNOG; ENOG502S17Y; Eukaryota.
DR   GeneTree; ENSGT00500000045074; -.
DR   HOGENOM; CLU_084094_0_0_1; -.
DR   InParanoid; Q6ZTW0; -.
DR   OMA; FSDYIRQ; -.
DR   OrthoDB; 1306505at2759; -.
DR   PhylomeDB; Q6ZTW0; -.
DR   TreeFam; TF329086; -.
DR   PathwayCommons; Q6ZTW0; -.
DR   Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   SignaLink; Q6ZTW0; -.
DR   BioGRID-ORCS; 91978; 19 hits in 1082 CRISPR screens.
DR   ChiTaRS; TPGS1; human.
DR   GenomeRNAi; 91978; -.
DR   Pharos; Q6ZTW0; Tdark.
DR   PRO; PR:Q6ZTW0; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q6ZTW0; protein.
DR   Bgee; ENSG00000141933; Expressed in monocyte and 96 other tissues.
DR   Genevisible; Q6ZTW0; HS.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IEA:Ensembl.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR   GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR   GO; GO:0051648; P:vesicle localization; IEA:Ensembl.
DR   InterPro; IPR039235; TPGS1.
DR   PANTHER; PTHR31932; PTHR31932; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Flagellum; Microtubule;
KW   Phosphoprotein; Reference proteome; Spermatogenesis.
FT   CHAIN           1..290
FT                   /note="Tubulin polyglutamylase complex subunit 1"
FT                   /id="PRO_0000249316"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MS8"
FT   VAR_SEQ         248..266
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020401"
SQ   SEQUENCE   290 AA;  31275 MW;  51BB1D8875827E84 CRC64;
     MAAVEKRRQA VPPPAGFTDS GRQSVSRAAG AAESEEDFLR QVGVTEMLRA ALLKVLEARP
     EEPIAFLAHY FENMGLRSPV NGGAGEPPGQ LLLQQQRLGR ALWHLRLAHH SQRAAFNNNV
     SVAYECLSAG GRRKRPGLDG RTYSELLRRI CRDGQAPEEV VAPLLRKVQC RDHEAVPLSV
     FRAGTLTCFV LLEFVARAGA LFQLLEDSAA AVADRRVGQA VLDTLEGALQ ASDAAAPARF
     LEAGSRLGPD SLALALDRAV GGRRPSAPMT REEFLERAAA LFIAKVKPVG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024