ID A0A2Y9MQ62_DELLE Unreviewed; 628 AA.
AC A0A2Y9MQ62;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=SH3 domain-containing kinase-binding protein 1 isoform X3 {ECO:0000313|RefSeq:XP_022421197.1};
GN Name=SH3KBP1 {ECO:0000313|RefSeq:XP_022421197.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022421197.1};
RN [1] {ECO:0000313|RefSeq:XP_022421197.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022421197.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022421197.1; XM_022565489.2.
DR AlphaFoldDB; A0A2Y9MQ62; -.
DR STRING; 9749.A0A2Y9MQ62; -.
DR Ensembl; ENSDLET00000032148; ENSDLEP00000029260; ENSDLEG00000020919.
DR KEGG; dle:111170377; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12055; SH3_CIN85_2; 1.
DR CDD; cd12057; SH3_CIN85_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR035771; CIN85_SH3_2.
DR InterPro; IPR035772; CIN85_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF6; SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_022421197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|RefSeq:XP_022421197.1}.
FT DOMAIN 61..120
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 230..291
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 68367 MW; 10AE8EB45FD53F95 CRC64;
MELSAAKAPS AADASEIEIK KEMKKDPLSS KAPEKPMHEV SSGNALLSSE TILRTNRRGE
RRRRRCQVAF SYLPQNDDEL ELKVGDIIEV VGEVEEGWWE GVLNGKTGMF PSNFIKELSG
ESDDLGISQD EQLSKSSLRE TTGSESDGGD SSSTKSEGAN GTVATAAIQP KKVKGVGFGD
IFKDKPIKLR PRSIEVENDF LPVEKTIGKK LPPTAATPDS SKTEMDSRTK AKDYCKVIFP
YEAQNDDELT IKEGDIVTLI NKDCIDVGWW EGELNGRRGV FPDNFVKLLP PDFEKEGNRP
KKPPPPSAPV IKQGAGTTER KHEIKKIPPE RPETLPNRTE EKERPEREPK LDLQKPSVPA
IPPKKPRPPK TNSLSRPGAL PPRRPERPAG PLTHTRGDGP KIDLAGSSIS GILDKDLSDR
SNDIDLEGFD SVVSSTEKLS HPTTSRPKAT GRRPPSQSLT SSSLSSPDIF DSPSPEEDKE
EHVSLAHRGV DASKKTSKTV TISQVSDNKA SLPPKPGTMA AGSGGPAPLS SAASSPLSSS
LGAVGHRANS PSLFGAEGKP KMEPPASSQA AMEELRTQVR ELRGIVETMK DQQKREIKQL
LSELDEEKKI RLRLQMEVND IKKALQSK
//
