ID B4DL02_HUMAN Unreviewed; 520 AA.
AC B4DL02;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=SHC-transforming protein 1 {ECO:0000256|ARBA:ARBA00020297};
DE AltName: Full=Src homology 2 domain-containing-transforming protein C1 {ECO:0000256|ARBA:ARBA00031530};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG59364.1};
RN [1] {ECO:0000313|EMBL:BAG59364.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Tongue {ECO:0000313|EMBL:BAG59364.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AK296786; BAG59364.1; -; mRNA.
DR AlphaFoldDB; B4DL02; -.
DR MaxQB; B4DL02; -.
DR PeptideAtlas; B4DL02; -.
DR ProteomicsDB; 4499; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01209; PTB_Shc; 1.
DR CDD; cd09925; SH2_SHC; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006019; PID_Shc-like.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337; SHC TRANSFORMING PROTEIN; 1.
DR PANTHER; PTHR10337:SF2; SHC-TRANSFORMING PROTEIN 1; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00629; SHCPIDOMAIN.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 92..275
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 425..516
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 56178 MW; 57CBFA2A80EDBB72 CRC64;
MSNLRLANPA GGRPGSKGEP GRAADDGEGI VGAAMPDSGP LPLLQDMNKL SGGGGRRTRV
EGGQLGGEEW TRHGSFVNKP TRGWLHPNDK VMGPGVSYLV RYMGCVEVLQ SMRALDFNTR
TQVTREAISL VCEAVPGAKG ATRRRKPCSR PLSSILGRSN LKFAGMPITL TVSTSSLNLM
AADCKQIIAN HHMQSISFAS GGDPDTAEYV AYVAKDPVNQ RACHILECPE GLAQDVISTI
GQAFELRFKQ YLRNPPKLVT PHDRMAGFDG SAWDEEEEEP PDHQYYNDFP GKEPPLGGVV
DMRLREGAAP GAARPTAPNA QTPSHLGATL PVGQPVGGDP EVRKQMPPPP PCPAGRELFD
DPSYVNVQNL DKARQAVGGA GPPNPAINGS APRDLFDMKP FEDALRVPPP PQSVSMAEQL
RGEPWFHGKL SRREAEALLQ LNGDFLVRES TTTPGQYVLT GLQSGQPKHL LLVDPEGVVR
TKDHRFESVS HLISYHMDNH LPIISAGSEL CLQQPVERKL
//
