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