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TPPP2_HUMAN
ID   TPPP2_HUMAN             Reviewed;         170 AA.
AC   P59282; Q2VYF3;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Tubulin polymerization-promoting protein family member 2 {ECO:0000303|PubMed:30680919};
DE   AltName: Full=Protein p25-beta {ECO:0000303|Ref.1};
DE   AltName: Full=TPPP/p18 {ECO:0000303|PubMed:17105200};
GN   Name=TPPP2 {ECO:0000303|PubMed:30680919, ECO:0000312|HGNC:HGNC:19293};
GN   Synonyms=C14orf8 {ECO:0000312|HGNC:HGNC:19293};
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], AND VARIANT LEU-133.
RA   Zhang Z., Wang S., Mao Y.;
RT   "Cloning and characterization of a novel human gene homolog with bovine
RT   p25.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-133.
RA   Xu J., Xie Y., Mao Y.;
RT   "Characterization of a novel human gene that has a high identity with Bos
RT   taurus brain-specific protein p25.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-133.
RC   TISSUE=Brain;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17105200; DOI=10.1021/bi061305e;
RA   Vincze O., Toekesi N., Olah J., Hlavanda E., Zotter A., Horvath I.,
RA   Lehotzky A., Tirian L., Medzihradszky K.F., Kovacs J., Orosz F., Ovadi J.;
RT   "Tubulin polymerization promoting proteins (TPPPs): members of a new family
RT   with distinct structures and functions.";
RL   Biochemistry 45:13818-13826(2006).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=23436708; DOI=10.1002/pmic.201200489;
RA   Liu M., Hu Z., Qi L., Wang J., Zhou T., Guo Y., Zeng Y., Zheng B., Wu Y.,
RA   Zhang P., Chen X., Tu W., Zhang T., Zhou Q., Jiang M., Guo X., Zhou Z.,
RA   Sha J.;
RT   "Scanning of novel cancer/testis proteins by human testis proteomic
RT   analysis.";
RL   Proteomics 13:1200-1210(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=30680919; DOI=10.1111/jcmm.14149;
RA   Zhu F., Yan P., Zhang J., Cui Y., Zheng M., Cheng Y., Guo Y., Yang X.,
RA   Guo X., Zhu H.;
RT   "Deficiency of TPPP2, a factor linked to oligoasthenozoospermia, causes
RT   subfertility in male mice.";
RL   J. Cell. Mol. Med. 23:2583-2594(2019).
CC   -!- FUNCTION: Probable regulator of microtubule dynamics required for sperm
CC       motility (Probable). In contrast to other members of the family, has no
CC       microtubule bundling activity (PubMed:17105200).
CC       {ECO:0000269|PubMed:17105200, ECO:0000305|PubMed:30680919}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:17105200}.
CC       Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q0P5Y3}.
CC       Note=Present in the middle piece of sperm tail.
CC       {ECO:0000250|UniProtKB:Q0P5Y3}.
CC   -!- TISSUE SPECIFICITY: Expressed in spermatids (PubMed:23436708). Detected
CC       in liver cancer (at protein level) (PubMed:23436708).
CC       {ECO:0000269|PubMed:23436708}.
CC   -!- SIMILARITY: Belongs to the TPPP family. {ECO:0000305}.
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DR   EMBL; AY072034; AAL62338.1; -; mRNA.
DR   EMBL; AY173946; AAO49716.1; -; mRNA.
DR   EMBL; AL161668; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC038970; AAH38970.1; -; mRNA.
DR   CCDS; CCDS9566.1; -.
DR   RefSeq; NP_776245.2; NM_173846.4.
DR   RefSeq; XP_005267381.1; XM_005267324.4.
DR   RefSeq; XP_016876455.1; XM_017020966.1.
DR   AlphaFoldDB; P59282; -.
DR   SMR; P59282; -.
DR   BioGRID; 125786; 10.
DR   STRING; 9606.ENSP00000317595; -.
DR   iPTMnet; P59282; -.
DR   PhosphoSitePlus; P59282; -.
DR   BioMuta; TPPP2; -.
DR   DMDM; 288558831; -.
DR   MassIVE; P59282; -.
DR   PaxDb; P59282; -.
DR   PeptideAtlas; P59282; -.
DR   PRIDE; P59282; -.
DR   ProteomicsDB; 57137; -.
DR   Antibodypedia; 70; 60 antibodies from 16 providers.
DR   DNASU; 122664; -.
DR   Ensembl; ENST00000321760.11; ENSP00000317595.6; ENSG00000179636.15.
DR   Ensembl; ENST00000530140.6; ENSP00000435356.2; ENSG00000179636.15.
DR   GeneID; 122664; -.
DR   KEGG; hsa:122664; -.
DR   MANE-Select; ENST00000321760.11; ENSP00000317595.6; NM_173846.5; NP_776245.2.
DR   UCSC; uc001vzh.4; human.
DR   CTD; 122664; -.
DR   DisGeNET; 122664; -.
DR   GeneCards; TPPP2; -.
DR   HGNC; HGNC:19293; TPPP2.
DR   HPA; ENSG00000179636; Tissue enriched (testis).
DR   MIM; 616956; gene.
DR   neXtProt; NX_P59282; -.
DR   OpenTargets; ENSG00000179636; -.
DR   PharmGKB; PA162406822; -.
DR   VEuPathDB; HostDB:ENSG00000179636; -.
DR   eggNOG; KOG4070; Eukaryota.
DR   GeneTree; ENSGT00940000153875; -.
DR   HOGENOM; CLU_091734_0_0_1; -.
DR   InParanoid; P59282; -.
DR   OMA; RAKNART; -.
DR   OrthoDB; 1317210at2759; -.
DR   PhylomeDB; P59282; -.
DR   TreeFam; TF314440; -.
DR   PathwayCommons; P59282; -.
DR   BioGRID-ORCS; 122664; 10 hits in 1070 CRISPR screens.
DR   GenomeRNAi; 122664; -.
DR   Pharos; P59282; Tdark.
DR   PRO; PR:P59282; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P59282; protein.
DR   Bgee; ENSG00000179636; Expressed in sperm and 103 other tissues.
DR   ExpressionAtlas; P59282; baseline and differential.
DR   Genevisible; P59282; HS.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0032273; P:positive regulation of protein polymerization; IBA:GO_Central.
DR   GO; GO:1901317; P:regulation of flagellated sperm motility; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR008907; P25-alpha.
DR   InterPro; IPR030794; TPPP2.
DR   PANTHER; PTHR12932; PTHR12932; 1.
DR   PANTHER; PTHR12932:SF21; PTHR12932:SF21; 1.
DR   Pfam; PF05517; p25-alpha; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Differentiation; Flagellum;
KW   Reference proteome; Spermatogenesis.
FT   CHAIN           1..170
FT                   /note="Tubulin polymerization-promoting protein family
FT                   member 2"
FT                   /id="PRO_0000221137"
FT   REGION          127..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         133
FT                   /note="R -> L (in dbSNP:rs9624)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT                   ECO:0000269|Ref.2"
FT                   /id="VAR_059147"
SQ   SEQUENCE   170 AA;  18503 MW;  0DC766D7E979653D CRC64;
     MASEAEKTFH RFAAFGESSS SGTEMNNKNF SKLCKDCGIM DGKTVTSTDV DIVFSKVKAK
     NARTITFQQF KEAVKELGQK RFKGKSPDEV LENIYGLMEG KDPATTGATK ATTVGAVDRL
     TDTSKYTGTH KERFDESGKG KGIAGREEMT DNTGYVSGYK GSGTYDKKTK
 
 
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