FYB2_MOUSE
ID FYB2_MOUSE Reviewed; 729 AA.
AC A2A995;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=FYN-binding protein 2 {ECO:0000312|MGI:MGI:2685466};
DE AltName: Full=Activation-dependent, raft-recruited ADAP-like phosphoprotein;
GN Name=Fyb2 {ECO:0000312|MGI:MGI:2685466}; Synonyms=ARAP;
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 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC -!- FUNCTION: Adapter protein that plays a role in T-cell receptor (TCR)-
CC mediated activation of signaling pathways. Required for T-cell
CC activation and integrin-mediated T-cell adhesion in response to TCR
CC stimulation. {ECO:0000250|UniProtKB:Q5VWT5}.
CC -!- SUBUNIT: Interacts with SKAP1, LCK and FYN. The phosphorylated form
CC interacts with LCP2. {ECO:0000250|UniProtKB:Q5VWT5}.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000250|UniProtKB:Q5VWT5}.
CC Note=Recruited to membrane rafts and immunological synapse after TCR
CC stimulation. {ECO:0000250|UniProtKB:Q5VWT5}.
CC -!- PTM: Phosphorylation is required for its function in T-cell activation.
CC {ECO:0000250|UniProtKB:Q5VWT5}.
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DR EMBL; AK028077; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL627186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51250.2; -.
DR AlphaFoldDB; A2A995; -.
DR SMR; A2A995; -.
DR STRING; 10090.ENSMUSP00000102415; -.
DR iPTMnet; A2A995; -.
DR PhosphoSitePlus; A2A995; -.
DR MaxQB; A2A995; -.
DR PaxDb; A2A995; -.
DR PeptideAtlas; A2A995; -.
DR PRIDE; A2A995; -.
DR Antibodypedia; 33247; 54 antibodies from 11 providers.
DR Ensembl; ENSMUST00000106804; ENSMUSP00000102416; ENSMUSG00000078612.
DR UCSC; uc012dhy.1; mouse.
DR MGI; MGI:2685466; Fyb2.
DR VEuPathDB; HostDB:ENSMUSG00000078612; -.
DR eggNOG; ENOG502RXZD; Eukaryota.
DR GeneTree; ENSGT00530000063460; -.
DR HOGENOM; CLU_023222_0_0_1; -.
DR InParanoid; A2A995; -.
DR PhylomeDB; A2A995; -.
DR ChiTaRS; Fyb2; mouse.
DR PRO; PR:A2A995; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A995; protein.
DR Bgee; ENSMUSG00000078612; Expressed in animal zygote and 38 other tissues.
DR ExpressionAtlas; A2A995; baseline and differential.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR043443; FYB1/2-like.
DR InterPro; IPR029294; hSH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR16830; PTHR16830; 1.
DR Pfam; PF14603; hSH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..729
FT /note="FYN-binding protein 2"
FT /id="PRO_0000304584"
FT DOMAIN 668..728
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 18..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 520..523
FT /note="SH2-binding; to LCP2"
FT /evidence="ECO:0000250|UniProtKB:Q5VWT5"
FT COMPBIAS 44..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWT5"
FT MOD_RES 591
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWT5"
FT CONFLICT 523
FT /note="I -> V (in Ref. 1; AK028077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82296 MW; 62CDE8137EA7138A CRC64;
MEEEGIRNFK ELRAKFQKFN AAPLPGPMRF PAGVSRKHDR GSTQPAQDLA NRKCLSSHHH
QTPSHSSTGV SQPLKNQTLK SAQGDELQKT SSSSGTPEKS TVCPERDFQK AAVPLDVTKS
RAKTSNEEKG MTLSSFRYKL WNWEKVSSQN GEMSPAPLLT NGGIKTFHFE GQKTMGLAQD
KPEKSLKATG AQTLPPQSHS MAQRKSPVTS KASSVSLPPH SRKSTKSPAT EGSHRSSQCQ
PVYECELDSL VPEKPQSRHC RLPKTKPLPS IETLGPPPPK PSKPPFVNLY AFHRLPATVT
KTPKEETMKE GPLSPDSAEL EEAHNYDTTI SYLRHSGNSI NLCAEGESTE ATYEIEIEEL
QKPWRSFFLP ELSPRPKEEE NTMEEKESWE SEPLEPRKEL HPSRPPKVVV YKETPGKTQM
AGVHEDRRSV PAGNQEAMTD IMQNRLFPED VTLTRHSQDK SGYVEALEVT KETPSPSTIR
SSSSSEKTYD AVECSREDVR KWDFSSSFTS DSEENCEEMY EDIYKAKNDD PKTEVAGRTA
LRKLQQIFRK ENVVFRMKKT KSKEIVSNGF SVSLPDLGPR SQDDSQDGII YDDVDTREKE
SNDEDKVKTW KTKFLIPKGK KWGKGSQGSK SFSPRHFFRT KKQKLEKNRM EKEEKLFRER
FQYGKEILVI NRAVACASNS RNGMFDLPII PGEQLEVIDT TEQNLVICRN SKGKYGYVLV
EHLDFKHQG
