SHCBP_MOUSE
ID SHCBP_MOUSE Reviewed; 668 AA.
AC Q9Z179; Q3UED9; Q3UMD9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=SHC SH2 domain-binding protein 1;
DE AltName: Full=Protein expressed in activated lymphocytes;
DE Short=mPAL;
DE AltName: Full=SHC-binding protein;
GN Name=Shcbp1; Synonyms=Pal;
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 [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH SHC1.
RX PubMed=10086341; DOI=10.1038/sj.onc.1202507;
RA Schmandt R., Liu S.K., McGlade C.J.;
RT "Cloning and characterization of mPAL, a novel Shc SH2 domain-binding
RT protein expressed in proliferating cells.";
RL Oncogene 18:1867-1879(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [5]
RP FUNCTION, AND INTERACTION WITH TRIM71.
RX PubMed=22508726; DOI=10.1101/gad.187641.112;
RA Chen J., Lai F., Niswander L.;
RT "The ubiquitin ligase mLin41 temporally promotes neural progenitor cell
RT maintenance through FGF signaling.";
RL Genes Dev. 26:803-815(2012).
CC -!- FUNCTION: May play a role in signaling pathways governing cellular
CC proliferation, cell growth and differentiation. May be a component of a
CC novel signaling pathway downstream of Shc. Acts as a positive regulator
CC of FGF signaling in neural progenitor cells.
CC {ECO:0000269|PubMed:10086341, ECO:0000269|PubMed:22508726}.
CC -!- SUBUNIT: Interacts directly with isoform p52shc of SHC1 via its SH2
CC domain (PubMed:10086341). Interacts with TRIM71; leading to enhanced
CC SHCBP1 protein stability (PubMed:22508726). Interacts with both members
CC of the centralspindlin complex, KIF23 and RACGAP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NEM2, ECO:0000269|PubMed:10086341,
CC ECO:0000269|PubMed:22508726}.
CC -!- INTERACTION:
CC Q9Z179; P98083: Shc1; NbExp=5; IntAct=EBI-644352, EBI-300201;
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEM2}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NEM2}.
CC Note=Displays weak localization to the spindle midzone in some early
CC telophase cells and is concentrated at the midbody in late cytokinesis.
CC {ECO:0000250|UniProtKB:Q8NEM2}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lung and heart with higher
CC expression in testis. No expression in brain, liver and skeletal
CC muscle. Elevated expression in actively cycling cells.
CC {ECO:0000269|PubMed:10086341}.
CC -!- INDUCTION: Down-regulated upon growth inhibition.
CC {ECO:0000269|PubMed:10086341}.
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DR EMBL; AF017152; AAD01613.1; -; mRNA.
DR EMBL; AK144966; BAE26159.1; -; mRNA.
DR EMBL; AK149580; BAE28972.1; -; mRNA.
DR EMBL; BC070455; AAH70455.1; -; mRNA.
DR CCDS; CCDS22088.1; -.
DR RefSeq; NP_035499.1; NM_011369.3.
DR AlphaFoldDB; Q9Z179; -.
DR SMR; Q9Z179; -.
DR BioGRID; 203217; 18.
DR IntAct; Q9Z179; 24.
DR STRING; 10090.ENSMUSP00000022945; -.
DR iPTMnet; Q9Z179; -.
DR PhosphoSitePlus; Q9Z179; -.
DR EPD; Q9Z179; -.
DR MaxQB; Q9Z179; -.
DR PaxDb; Q9Z179; -.
DR PeptideAtlas; Q9Z179; -.
DR PRIDE; Q9Z179; -.
DR ProteomicsDB; 256998; -.
DR Antibodypedia; 43856; 120 antibodies from 20 providers.
DR Ensembl; ENSMUST00000022945; ENSMUSP00000022945; ENSMUSG00000022322.
DR GeneID; 20419; -.
DR KEGG; mmu:20419; -.
DR UCSC; uc009kua.1; mouse.
DR CTD; 79801; -.
DR MGI; MGI:1338802; Shcbp1.
DR VEuPathDB; HostDB:ENSMUSG00000022322; -.
DR eggNOG; ENOG502QUQ2; Eukaryota.
DR GeneTree; ENSGT00940000161310; -.
DR HOGENOM; CLU_022717_2_0_1; -.
DR InParanoid; Q9Z179; -.
DR OMA; KIEPAGW; -.
DR OrthoDB; 1276823at2759; -.
DR PhylomeDB; Q9Z179; -.
DR TreeFam; TF329196; -.
DR BioGRID-ORCS; 20419; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Shcbp1; mouse.
DR PRO; PR:Q9Z179; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z179; protein.
DR Bgee; ENSMUSG00000022322; Expressed in otic placode and 187 other tissues.
DR ExpressionAtlas; Q9Z179; baseline and differential.
DR Genevisible; Q9Z179; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR039448; Beta_helix.
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; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT CHAIN 2..668
FT /note="SHC SH2 domain-binding protein 1"
FT /id="PRO_0000076316"
FT REPEAT 428..451
FT /note="PbH1 1"
FT REPEAT 452..473
FT /note="PbH1 2"
FT REPEAT 474..496
FT /note="PbH1 3"
FT REPEAT 497..518
FT /note="PbH1 4"
FT REPEAT 526..548
FT /note="PbH1 5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM2"
FT CONFLICT 53
FT /note="G -> D (in Ref. 2; BAE26159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 75917 MW; EC614A982B744591 CRC64;
MADDLRAGGV LEPIAMVPPR PDLAAEKEPA SWKEGLFLDA DPCSDQGYHA NPGATVKTLI
PEGKTPFPRI IQTNELLFYE RFRAYQDYIL ADCKASEVKE FTVSFLEKVL EPSGWWAVWH
TNVFEVLVEV TNVDFPSLKA VVRLAEPCIY ESKLSTFTLA NVKELLDLKE FHLPLQELWV
VSDDSHEFHQ MALAIEHVRF FYKHIWRSWD EEEEDEYDYF VRCVEPRLRL YYDILEDRVP
SGLIVDYHNL LSQCEESYRK FLNLRSSLSN CNSDSEQENI SMVEGLNLYS EIEQLKQKLK
LIENPLLRYV FGYQKNSNIQ GKGTRQNGQK VIHVVSSTMK TGLLRSLFKD RFCEESCKEE
TEIKFHSDLL SGINACYDGD TVIICPGHYV VHGTCSIADS IELEGYGLPD DIVIEKRGKG
DTFVDCTGMD VKISGIKFIQ HDSVEGILII HHGKTTLENC VLQCETTGVT VRTSAELFMK
NSDVYGAKGA GIEIYPGSKC TLTDNGIHHC KEGILIKDFL DEHYDIPKIS MINNVIHNNE
GYGVVLVKPT IFCDLQENTQ DEINDNMVQK NKEADVTEGL DLEEMLQCVA SKMEPYATAD
FNEQAKGNCE IINELLAISM QKGRMKKRLS ELGITQADDN IMSQEMFIEI MGNQFKWNGK
GSFGTFLY
