ID A0A455B2G6_PHYMC Unreviewed; 631 AA.
AC A0A455B2G6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=SH3 domain-containing kinase-binding protein 1 isoform X1 {ECO:0000313|RefSeq:XP_028338276.1};
GN Name=SH3KBP1 {ECO:0000313|RefSeq:XP_028338276.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028338276.1};
RN [1] {ECO:0000313|RefSeq:XP_028338276.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028338276.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_028338276.1; XM_028482475.2.
DR AlphaFoldDB; A0A455B2G6; -.
DR Proteomes; UP000248484; Chromosome 21.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_028338276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|RefSeq:XP_028338276.1}.
FT DOMAIN 39..98
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 233..294
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 575..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 69049 MW; 6A848250B84CCA91 CRC64;
MKKDPVSSKA PEKPMHEVSS GNALLSSETI LRTNKRGERR RRRCQVAFSY LPQNDDELEL
KVGDIIEVVG EVEEGWWEGV LNGKTGMFPS NFIKELSGES DDLGISQDEQ LSKSRKTTFE
GTILYRAAPG KTEGHRRYYS LRETTGSESD GGDSSSTKSE GANGTVATAA IQPKKVKGVG
FGDIFKDKPI KLRPRSIEVE NDFLPVEKTI GKKLPPTAAT PDSSKTEMDS RTKAKDYCKV
IFPYEAQNDD ELTIKEGDIV TLINKDCIDV GWWEGELNGR RGVFPDNFVK LLPPDFEKEG
NRPKKPPPPS APVIKQGAGT TERKHEIKKI PPERPETLPN RTEEKERPER EPKLDLQKPS
VPAIPPKKPR PPKTNSLSRP GALPPRRPER PAGPLTHTRG DGPKIDLAGS SISGILDKDL
SDRSNDIDLE GFDSVVSSTE KLSHPTTSRP KATGRRPPSQ SLTSSSLSSP DIFDSPSPEE
DKEEHVSLAH RGADASKKTS KTVTISQVSD NKASLPPKPG TMAAGSGGPA PLSSAASSPL
SSSLGTVGHR ANSPSLFGAE GKPKMEPPAS SQAAVEELRT QVRELRNIIE TMKDQQKREI
KQLLSELDEE KKIRLRLQME VNDIKKALQS K
//
