ID   A0A2K6RC59_RHIRO        Unreviewed;       516 AA.
AC   A0A2K6RC59;
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=Hematopoietic cell-specific Lyn substrate 1 {ECO:0000313|Ensembl:ENSRROP00000038619.1};
GN   Name=HCLS1 {ECO:0000313|Ensembl:ENSRROP00000038619.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000038619.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000038619.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6RC59; -.
DR   STRING; 61622.ENSRROP00000038619; -.
DR   Ensembl; ENSRROT00000063093.1; ENSRROP00000038619.1; ENSRROG00000042649.1.
DR   GeneTree; ENSGT00940000158997; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR   GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0038158; P:granulocyte colony-stimulating factor signaling pathway; IEA:Ensembl.
DR   GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051169; P:nuclear transport; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0030854; P:positive regulation of granulocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR003134; Hs1_Cortactin.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR   PANTHER; PTHR10829:SF5; HEMATOPOIETIC LINEAGE CELL-SPECIFIC PROTEIN; 1.
DR   Pfam; PF02218; HS1_rep; 4.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51090; CORTACTIN; 4.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          418..516
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          242..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..395
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  57185 MW;  DDD72D8D9F12774C CRC64;
     MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE HINIHQLRNK
     VSEEHDVLKK KEMESGPKAS HGYGGRFGVE RDRMDKSAVG HEYVAEVEKH SSQTDAAKGF
     GGKYGVERDR ADKSAVGFDY KGEVEKHTSQ KDYSRGFGGR YGVEKDKRDK AALGYDYKGE
     TEKHESQRDY AKGFGGQYGI QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGARGLKA
     KFESMAEEKR KREEEEKAQQ VARRQQERKA VTKMSPEAPQ PVIAMEEPAV PAPLPKKISS
     EAWPPAGTPP SSEPEPVRTS RQHPVPLRPV RQTLLEDNEE PPALPPRTLE GLQVEEEPVY
     EAEPEPEPEN DYEDVEEMDR HEQEDEPEGD YEEVLEPEGS SFSSAPAGSS GCPVGAGALG
     ISAVALYDYQ GGRLGVACGA WYLQATDLRQ GDVGKETFMS DHSNIPSTFS SEGSDELSFD
     PDDVITDIEM VDEGWWRGHC HGHFGLFPAN YVKLLE
//