ID F7HVR8_CALJA Unreviewed; 928 AA.
AC F7HVR8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Kinase suppressor of ras 1 {ECO:0000313|Ensembl:ENSCJAP00000043924.3};
GN Name=KSR1 {ECO:0000313|Ensembl:ENSCJAP00000043924.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000043924.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000043924.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000043924.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F7HVR8; -.
DR STRING; 9483.ENSCJAP00000043924; -.
DR Ensembl; ENSCJAT00000054159.4; ENSCJAP00000043924.3; ENSCJAG00000012392.5.
DR eggNOG; KOG0193; Eukaryota.
DR GeneTree; ENSGT00940000156066; -.
DR InParanoid; F7HVR8; -.
DR OMA; HAIPHKW; -.
DR OrthoDB; 4560496at2759; -.
DR TreeFam; TF317006; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000012392; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR CDD; cd20872; C1_KSR1; 1.
DR CDD; cd14152; STKc_KSR1; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.10.140.1120; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF716; KINASE SUPPRESSOR OF RAS 1; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 347..391
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 591..861
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 103301 MW; 8A685735C3F4E8A9 CRC64;
MDRAALRAAA MGEKKEGGGR GDAAAAEGGA GAAASRALQQ CGQLQKLIDI SIGSLRGLRT
KCAVSNDLTQ HEIRTLEAKL VRYICKQRQC KLSVAPGERT PELNSYPRFS DWLYTFNVRP
EVVQEIPREL TLDALLEMNE ARVKETLRRC GASAEECGRL QYALTCLRKV TGLGGEHKED
SGCSLLDARR ESGSGPSTDT LSPASLPWPP GSSQLSRAGN STQGPRSISV SAIPASDSPT
TSFSEGLSDT CIPLHASGRL TPRALHSFIT PPTTPQLRRH TKLKPPRTPP PPSRKVFQLL
PSFPTLTRSK SHESQLGNRI DEVSSMRFDL PHGSPQMVRR DIGLSVTHRF STKSWLSQVC
HVCQKSMIFG VKCKHCRLKC HNKCTKEAPA CRISFLPLTR LRRTESVPSD INNPVDRAAE
PHFGTLPKAL TKKEHPPAMN HLDSSSNPSS TTSSTPSSPA PFPTSSNPSS ATTPPNPSPG
QRDSRFNFPA AYFIHHRQQF IFPDISAFAQ AAPLPEAADS TRFNDQPKAD VLEAHEAEAE
EPEAGKSEAE DDEDEVDDLP SSRRPWRGPI SRKASQTSVY LQEWDIPFEQ VELGEPIGQG
RWGRVHRGRW HGEVAIRLLE MDGHNQDHLK LFKKEVMNYR QTRHENVVLF MGACMNPPHL
AIITSFCKGR TLHSFVRDPK TSLDINKTRQ IAQEIIKGMG YLHAKGIVHK DLKSKNVFYD
NGKVVITDFG LFGISGVVRE GRRENQLKLS HDWLCYLAPE IVREMTPGKD EDQLPFSKAA
DVYAFGTVWY ELQARDWPLK NQAAEASIWQ IGSGEGMKRV LASVSLGKEV SEILSACWAF
DLQERPSFSL LMDMLEKLPK LNRRLSHPGH FWKSADRWRS RYYGKGRYGH PDFKSSCPVL
EEYINSSKVV PRFERFGLGV LESSNSKM
//
