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SHP1L_MOUSE
ID   SHP1L_MOUSE             Reviewed;         639 AA.
AC   Q3TTP0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Testicular spindle-associated protein SHCBP1L {ECO:0000305};
DE   AltName: Full=SHC SH2 domain-binding protein 1-like protein {ECO:0000312|MGI:MGI:1919086};
GN   Name=Shcbp1l {ECO:0000312|MGI:MGI:1919086};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION, INTERACTION WITH HSPA2, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, ACETYLATION AT SER-3; LYS-556 AND LYS-631, PHOSPHORYLATION AT
RP   SER-50, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=24557841; DOI=10.1093/molehr/gau014;
RA   Liu M., Shi X., Bi Y., Qi L., Guo X., Wang L., Zhou Z., Sha J.;
RT   "SHCBP1L, a conserved protein in mammals, is predominantly expressed in
RT   male germ cells and maintains spindle stability during meiosis in testis.";
RL   Mol. Hum. Reprod. 20:463-475(2014).
CC   -!- FUNCTION: Testis-specific spindle-associated factor that plays a role
CC       in spermatogenesis (PubMed:24557841). In association with HSPA2,
CC       participates in the maintenance of spindle integrity during meiosis in
CC       male germ cells (PubMed:24557841). {ECO:0000269|PubMed:24557841}.
CC   -!- SUBUNIT: Interacts with HSPA2; this interaction may promote the
CC       recruitment of HSPA2 to the spindle (PubMed:24557841).
CC       {ECO:0000269|PubMed:24557841}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:24557841}. Note=Colocalizes with alpha tubulin
CC       during meiosis (PubMed:24557841). Colocalizes with HSPA2 at spindle
CC       during the meiosis process (PubMed:24557841).
CC       {ECO:0000269|PubMed:24557841}.
CC   -!- TISSUE SPECIFICITY: Expressed in pachytene spermatocytes and elongating
CC       spermatids inside the seminiferous tubules (PubMed:24557841). Not
CC       detected in ovary (at protein level) (PubMed:24557841). Testis-specific
CC       (PubMed:24557841). {ECO:0000269|PubMed:24557841}.
CC   -!- DISRUPTION PHENOTYPE: Male mice exhibit decreased fertility and produce
CC       reduced epididymal sperm content, but do not influence the rates of
CC       motility, capacitation and acrosome reaction of sperm
CC       (PubMed:24557841). Meiosis-arrested spermatocytes are increased in the
CC       early stages of meiosis and undergo programmed cell death
CC       (PubMed:24557841). Display a diminution of the HSPA2 signal at the
CC       spindle and disordered chromosomes during male meiosis
CC       (PubMed:24557841). {ECO:0000269|PubMed:24557841}.
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DR   EMBL; AK161274; BAE36285.1; -; mRNA.
DR   EMBL; BC113157; AAI13158.1; -; mRNA.
DR   CCDS; CCDS15372.1; -.
DR   RefSeq; NP_001028334.1; NM_001033162.2.
DR   AlphaFoldDB; Q3TTP0; -.
DR   SMR; Q3TTP0; -.
DR   STRING; 10090.ENSMUSP00000036347; -.
DR   iPTMnet; Q3TTP0; -.
DR   PhosphoSitePlus; Q3TTP0; -.
DR   PaxDb; Q3TTP0; -.
DR   PRIDE; Q3TTP0; -.
DR   ProteomicsDB; 257154; -.
DR   Antibodypedia; 50328; 47 antibodies from 12 providers.
DR   Ensembl; ENSMUST00000042373; ENSMUSP00000036347; ENSMUSG00000042708.
DR   GeneID; 71836; -.
DR   KEGG; mmu:71836; -.
DR   UCSC; uc007czx.1; mouse.
DR   CTD; 81626; -.
DR   MGI; MGI:1919086; Shcbp1l.
DR   VEuPathDB; HostDB:ENSMUSG00000042708; -.
DR   eggNOG; ENOG502QT5S; Eukaryota.
DR   GeneTree; ENSGT00940000161173; -.
DR   HOGENOM; CLU_022717_0_0_1; -.
DR   InParanoid; Q3TTP0; -.
DR   OMA; KMNNNHI; -.
DR   OrthoDB; 1276823at2759; -.
DR   PhylomeDB; Q3TTP0; -.
DR   TreeFam; TF329196; -.
DR   BioGRID-ORCS; 71836; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q3TTP0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q3TTP0; protein.
DR   Bgee; ENSMUSG00000042708; Expressed in spermatocyte and 93 other tissues.
DR   ExpressionAtlas; Q3TTP0; baseline and differential.
DR   Genevisible; Q3TTP0; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072687; C:meiotic spindle; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007112; P:male meiosis cytokinesis; IBA:GO_Central.
DR   GO; GO:2001252; P:positive regulation of chromosome organization; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045140; SHCBP1-like.
DR   PANTHER; PTHR14695; PTHR14695; 1.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SMART; SM00722; CASH; 1.
DR   SMART; SM00710; PbH1; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW   Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
FT   CHAIN           1..639
FT                   /note="Testicular spindle-associated protein SHCBP1L"
FT                   /id="PRO_0000284839"
FT   REPEAT          479..500
FT                   /note="PbH1 1"
FT   REPEAT          501..523
FT                   /note="PbH1 2"
FT   REPEAT          524..557
FT                   /note="PbH1 3"
FT   REPEAT          560..582
FT                   /note="PbH1 4"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          285..312
FT                   /evidence="ECO:0000255"
FT   MOD_RES         3
FT                   /note="O-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:24557841"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZQ2"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:24557841"
FT   MOD_RES         556
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:24557841"
FT   MOD_RES         631
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:24557841"
SQ   SEQUENCE   639 AA;  70948 MW;  8BF32326B0AD652D CRC64;
     MESDATTSEP KASVGSDSSP AEQTVLATLR DSVAAPTRGF MSPVRSVVAS PRPVKGKAAR
     RRLQLPPVTQ AETCDEEPVP AVPEDQEEAQ PLPPIYASPM RGMWRSEKVA LYCDQVLQGS
     KAEDAEEAMS RYLLEKLKAK DRWLGVWKSN PELFFEKYEE ASIPFVGILV EVTCKPRQNL
     SSCFKVTVSV AEPFSSNIAN IPRDLVDEVL GELEYSAPLL EVYPVDGQDA DVRDIALALE
     VVRFFYDFLW RDWDDEENCE NYTALIEERI NLWCDIQDGT IPGPIAQRFK KTLEKYKNKR
     VELIEYQSNI KEDPSAAEAV ECWKKYYEIV MLCGLLKMWE DLRLRVHGPF FPRILRRRKG
     KRDFGKTITH IVAKVMTTDM VKNLSSDTLL QQHNDLNLAL DSCYSGDIVV IFPGEYQASN
     LALLTDDITI KGVGKREEIM ITSEPSHDSF VVSKADNVKL MQLSLIQQGT VDGIVVVESG
     HLTLENCLLK CEGTGVCVLT GASLTITNSE ITGAQGAGVE LYPGSIAILE GNEIHHCNNL
     RTSDSSKSTL GGVNMKVLPA PKLKMTNNHI YNNNGYGVSI LQPSEQFFIV AEAALNKGAA
     SGDKKDDKML SKVMQTLNVE MNNNRIEANL KGDIRIVTG
 
 
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