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Database: UniProt
Entry: A0A2K5YQZ3_MANLE
LinkDB: A0A2K5YQZ3_MANLE
Original site: A0A2K5YQZ3_MANLE 
ID   A0A2K5YQZ3_MANLE        Unreviewed;      1229 AA.
AC   A0A2K5YQZ3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=SAM and SH3 domain containing 1 {ECO:0000313|Ensembl:ENSMLEP00000017939.1};
GN   Name=SASH1 {ECO:0000313|Ensembl:ENSMLEP00000017939.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000017939.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000017939.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K5YQZ3; -.
DR   STRING; 9568.ENSMLEP00000017939; -.
DR   Ensembl; ENSMLET00000041419.1; ENSMLEP00000017939.1; ENSMLEG00000033121.1.
DR   GeneTree; ENSGT00940000156778; -.
DR   OMA; SMSDWLI; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:1902498; P:regulation of protein autoubiquitination; IEA:Ensembl.
DR   GO; GO:1900044; P:regulation of protein K63-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd09559; SAM_SASH1_repeat1; 1.
DR   CDD; cd09492; SAM_SASH1_repeat2; 1.
DR   CDD; cd11967; SH3_SASH1; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR037627; SASH1_SAM_repeat1.
DR   InterPro; IPR037630; SASH1_SAM_repeat2.
DR   InterPro; IPR035720; SASH1_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR021090; SPIDER.
DR   PANTHER; PTHR12301:SF3; SAM AND SH3 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR12301; SAM-DOMAIN, SH3 AND NUCLEAR LOCALIZATION SIGNALS PROTEIN RELATED; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF12485; SLY; 1.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          531..592
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          610..674
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          1159..1223
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          103..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1042
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1229 AA;  135072 MW;  B84B4F2ABE5CE1FA CRC64;
     APEPEPEPEP GAGTSEAFSQ LWTDVMGILD GSLGNIDDLA QQYADYYNTC FSDVCERMEE
     LRKRRVSQDL DVEKPDASPT SLQLRSQIEE SLGFCSAVST PEVERKNPLH KSNSEDNSVG
     KGDWKKKNKY FWQNFRKNQK GIMRQTSKGE DVGYVASEIT MSDEERIQLM MMVKEKMITI
     EEALARLKEY EAQHRQSAAL DPADWPDGSY PTFDGSSNCN SREQSDDETE ESVKFKRLHK
     LVNSTRRVRK KLIRVEEMKK PSTEGGEEHV FENSPVLDER SALYSGVHKK PFFFDGSPEK
     PPEDDSDSLT TSPSSSSLDT WGAGRKLVKT FSKGESRGLI KPPKKMGTFF SYPEEEKAQK
     VSRSLTEGEM KKSLGSLSHG RTCSFGGFDL TNRSLHVGTN NSDPMGKEGD FVYKEVIKSP
     TASRISLGKK VKSVKETMRK RMSKKYSSSV SEQDSGLDGM PGSPPPSQPD PEHLDKPKLK
     AGGSVESLRS SLSGQSSMSG QTVSTTDSSA SNRESVKSED GDDEEPPYRG PFCGRARVHT
     DFTPSPYDTD SLKLKKGDII DIISKPPMGT WMGLLNNKVG TFKFIYVDVL SEDEEKPKRP
     TRRRRKGRPP QPKSVEDLLD RINLKEHMPT FLFNGYEDLD TFKLLEEEDL DELNIRDPEH
     RAVLLTAVEL LQEYDSNSDQ SGSQEKLLVD SQGLSGCSPR DSGCYESSEN LENGKTRKAS
     LLSAKSSAEP NLKSFSRNQL GNYPTLPLTK SGDALKQGQE EGRLGGGLAP DTSKSCDPPS
     VTGLNKNRRS LPVSICRSCE TLEGPQTVDT WPRSHSLDDL QAEPGAEQDV PTEVTEPPPQ
     IVPKVPQKMT ASSTKAQPLE RDSAVDNALL LTQSKRFSEP QKLTTKKLEG SIAASGRSLS
     PPQCLPRNYD AQAPGAKHGL ARTPLEGHRI GHEFEGTHHP LGTKEGVDAE QRVPEARTQP
     KIPSQPPPVP AKKSRERLAN GLYPVPMGPG GTLPSPDAPC LPVKRGSPTS PTSPSDCPPA
     LAPRPLSGQA PGSPPSTRPP PWLSELPENT SLQEHGVKLG PALTRKVSCA RGVDLEMLTE
     NKLHAEGIDL TEEPYSDKHG RCGIPEALVQ RYAEDLDQPE RDVAINMDQI RVKQLRKQHR
     MAIPSGGLTE ICRKPVSPGC ISSVSDWLIS IGLPMYASTL STAGFSTLSQ VPSLSHTCLQ
     EAGITEERHI RKLLSAARLF KLPPGPEAM
//
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