FYB1_RAT
ID FYB1_RAT Reviewed; 830 AA.
AC D3ZIE4;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=FYN-binding protein 1 {ECO:0000250|UniProtKB:O15117};
DE AltName: Full=Adhesion and degranulation promoting adaptor protein {ECO:0000250|UniProtKB:O15117};
DE Short=ADAP {ECO:0000250|UniProtKB:O15117};
DE AltName: Full=FYB-120/130 {ECO:0000250|UniProtKB:O15117};
DE Short=p120/p130 {ECO:0000250|UniProtKB:O15117};
DE AltName: Full=FYN-T-binding protein {ECO:0000250|UniProtKB:O15117};
DE AltName: Full=SLAP-130 {ECO:0000303|PubMed:12681493};
DE AltName: Full=SLP-76-associated phosphoprotein {ECO:0000250|UniProtKB:O15117};
GN Name=Fyb1 {ECO:0000312|RGD:1563421};
GN Synonyms=Fyb {ECO:0000312|RGD:1563421};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PROTEIN SEQUENCE OF 14-23; 68-77; 749-758 AND 769-776, FUNCTION,
RP INTERACTION WITH SKAP1, AND IDENTIFICATION IN A COMPLEX WITH SKAP1 AND
RP CLNK.
RX PubMed=12681493; DOI=10.1016/s0014-5793(03)00234-5;
RA Fujii Y., Wakahara S., Nakao T., Hara T., Ohtake H., Komurasaki T.,
RA Kitamura K., Tatsuno A., Fujiwara N., Hozumi N., Ra C., Kitamura D.,
RA Goitsuka R.;
RT "Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor
RT complex in mast cells(1).";
RL FEBS Lett. 540:111-116(2003).
RN [3] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling
CC cascades in T-cells (By similarity). May play a role in linking T-cell
CC signaling to remodeling of the actin cytoskeleton (By similarity).
CC Modulates the expression of IL2 (By similarity). Involved in platelet
CC activation (By similarity). Prevents the degradation of SKAP1 and SKAP2
CC (By similarity). May be involved in high affinity immunoglobulin
CC epsilon receptor signaling in mast cells (PubMed:12681493).
CC {ECO:0000250|UniProtKB:O15117, ECO:0000250|UniProtKB:O35601,
CC ECO:0000269|PubMed:12681493}.
CC -!- SUBUNIT: Part of a complex consisting of SKAP2, FYB1 and PTPNS1 (By
CC similarity). Part of a complex consisting of SKAP2, FYB1 and LILRB3 (By
CC similarity). Part of a complex consisting of SKAP1, FYB1 and CLNK
CC (PubMed:12681493). Interacts with CLNK (via its SH2 domain) and FYN;
CC this interaction allows SKAP1 and FYB1 to recruit FYN to the complex,
CC thus promoting the phosphorylation of CLNK by FYN (By similarity).
CC Interacts with FYN (By similarity). Interacts with LCP2 (By
CC similarity). Interacts with SKAP1 (PubMed:12681493). Interacts with
CC SKAP2 (By similarity). Interacts with FASLG (By similarity). Interacts
CC with EVL (By similarity). Interacts with TMEM47 (By similarity).
CC Interacts with LCK (By similarity). {ECO:0000250|UniProtKB:O15117,
CC ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:12681493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction
CC {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-
CC cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}.
CC -!- PTM: T-cell receptor ligation leads to increased tyrosine
CC phosphorylation.
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DR EMBL; AABR07008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006232081.1; XM_006232019.3.
DR AlphaFoldDB; D3ZIE4; -.
DR SMR; D3ZIE4; -.
DR STRING; 10116.ENSRNOP00000018634; -.
DR PaxDb; D3ZIE4; -.
DR PeptideAtlas; D3ZIE4; -.
DR PRIDE; D3ZIE4; -.
DR Ensembl; ENSRNOT00000018634; ENSRNOP00000018634; ENSRNOG00000013886.
DR GeneID; 499537; -.
DR UCSC; RGD:1563421; rat.
DR CTD; 2533; -.
DR RGD; 1563421; Fyb1.
DR eggNOG; ENOG502QTTQ; Eukaryota.
DR GeneTree; ENSGT00530000063460; -.
DR HOGENOM; CLU_339375_0_0_1; -.
DR InParanoid; D3ZIE4; -.
DR OMA; KSSTWSW; -.
DR OrthoDB; 831692at2759; -.
DR TreeFam; TF337003; -.
DR Reactome; R-RNO-202433; Generation of second messenger molecules.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR PRO; PR:D3ZIE4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013886; Expressed in thymus and 18 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR CDD; cd11867; hSH3_ADAP; 1.
DR InterPro; IPR030635; FYB1.
DR InterPro; IPR043443; FYB1/2-like.
DR InterPro; IPR035540; FYB_hSH3.
DR InterPro; IPR029294; hSH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR16830; PTHR16830; 2.
DR PANTHER; PTHR16830:SF13; PTHR16830:SF13; 2.
DR Pfam; PF14603; hSH3; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..830
FT /note="FYN-binding protein 1"
FT /id="PRO_0000448484"
FT DOMAIN 510..571
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 747..815
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..447
FT /note="Interaction with SKAP1"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT REGION 601..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..502
FT /evidence="ECO:0000255"
FT MOTIF 461..464
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 479..486
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 595..598
FT /note="SH2-binding; to LCP2"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOTIF 626..629
FT /note="SH2-binding; to FYN"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOTIF 732..739
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 11..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35601"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 570
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
FT MOD_RES 698
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15117"
SQ SEQUENCE 830 AA; 91412 MW; 4734DA9759534259 CRC64;
MDGKTDVKSL MAKFNTGSNP TEEVSTSSRP FKVAGQNSPS GIQSKKNLFD NQGNASPPAG
PSNMSKFGTT KPPLAAKPTY EEKSEKEPKP PFLKPTGVSP RFGTQPNSVS RDPEVKVGFL
KPVSPKPTSL TKEDSKPVIL RPPGNKLHNL NQESDLKTLG PKPGSTPPVP ENDLKPGFSK
IAGAKSKFMP APQDADSKPR FPRHTYGQKP SLSTEDAQEE ESIPKNTPVQ KGSPVQLGAK
SRGSPFKPAK EDPEDKDHGT PSSPFAGVVL KPAASRGSPG LSKNSEEKKE ERKTDIPKNI
FLNKLNQEEP ARFPKAPSKL TAGTPWGQSQ EKEGDKDSAT PKQKPLPPLS VLGPPPSKPS
RPPNVDLTRF RKADSANSSN KSQTPYSTTS LPPPPPTQPA SQPPLPASHP AHLPAPSLPP
RNIKPPLDLK HPINEENQDG VMHSDGTGNL EEEQESDGEM YEDIESSKER DKKREKEEKK
RLELERKEQK EREKKEQELR KKFKLTGPIQ VIHHAKACCD VKGGKNELSF KQGEDIEIIR
ITDNPEGKWL GRTARGSYGY IKTTAVKIDY DSLKRKKNTI NAVPPRPVEE DQDVYDDVAE
QDAPNSHSQS GSGGMFPPPP ADDDIYDGIE EEDADDGSVP QVDEKTNAWS WGILKMLKGK
DERKKSIREK PKVSESDSNE GSSFPSPHKQ LDVGEEVYDD VDASDFPPPP AEMSQGMSVG
KTKAEEKDPK KLKKQEKEEK DLRKKFKYDG EIRVLYSTKV ASSLTSKKWG TRDLQIKPGE
SLEVIQSTDD TKVLCRNEEG KYGYVLRSYL VDNDGEIYDD IADGCIYDND
