Q07666

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession KHDR1_HUMAN; Q07666;
Entrez ID 10657
GenBank Protein ID NM_001271878.1; NM_006559.2;
GenBank Nucleotide ID NP_001258807.1; NP_006550.1;
Protein Name KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
Gene Name KHDRBS1; SAM68
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionRecruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively re(view all)
Sequence
(Fasta)
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA 60
TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE NKYLPELMAE KDSLDPSFTH 120
AMQLLTAEIE KIQKGDSKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ 180
GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA 240
YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV 300
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA GIQRIPLPPP 360
PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG HGEVQDSYEA YGQDDWNGTR 420
PSLKAPPARP VKGAYREHPY GRY 444

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1PhosphorylationThyroid cancer/carcinomaP16843637
[Reference]: The expression and tyrosine phosphorylation of Sam68, a protein implicated in mRNA nucleocytoplasmic translocation and splicing, were further examined in RET-transfected cells and thyroid tumors.
2PhosphorylationProstate cancer/carcinoma/adenocarcinomaP17237817
[Reference]: The tyrosine kinase Src is frequently activated in advanced human prostate carcinomas and its activation correlates with tyrosine phosphorylation of the RNA-binding protein Sam68.
3AcetylationBreast cancer/tumor/carcinomaU15021911
[Reference]: Interestingly, the highest level of acetylation was found in tumorigenic breast cancer cell lines.


※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 42)
(view all)
103       KMEPENKYLPELMAE     dbPAF
113       ELMAEKDSLDPSFTH     dbPAF
12        DDPAARMSRSSGRSG     dbPAF
137       EKIQKGDSKKDDEEN     dbPAF
14        PAARMSRSSGRSGSM     dbPAF
15        AARMSRSSGRSGSMD     dbPAF
Acetylation
(count: 11)
(view all)
139       IQKGDSKKDDEENYL     PLMD
152       YLDLFSHKNMKLKER     PLMD
165       ERVLIPVKQYPKFNF     PLMD
169       IPVKQYPKFNFVGKI     PLMD
175       PKFNFVGKILGPQGN     PLMD
185       GPQGNTIKRLQEETG     PLMD
Ubiquitination
(count: 11)
(view all)
138       KIQKGDSKKDDEENY     PLMD
152       YLDLFSHKNMKLKER     PLMD
155       LFSHKNMKLKERVLI     PLMD
165       ERVLIPVKQYPKFNF     PLMD
169       IPVKQYPKFNFVGKI     PLMD
175       PKFNFVGKILGPQGN     PLMD
Sumoylation
(count: 5)
102       VKMEPENKYLPELMA     PLMD
175       PKFNFVGKILGPQGN     PLMD
185       GPQGNTIKRLQEETG     PLMD
194       LQEETGAKISVLGKG     PLMD
96        PSATASVKMEPENKY     PLMD
Malonylation
(count: 1)
200       AKISVLGKGSMRDKA     PLMD
Methylation
(count: 2)
194       LQEETGAKISVLGKG     PLMD
200       AKISVLGKGSMRDKA     PLMD
Succinylation
(count: 2)
165       ERVLIPVKQYPKFNF     PLMD
185       GPQGNTIKRLQEETG     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
G3V0F8Q07666HPRD
H7C2I1Q07666HPRD; MINT
O14977Q07666IntAct
O60231Q07666MINT
O60861Q07666MINT
O60907Q07666IntAct
O75525Q07666HPRD
O75554Q07666HPRD; MINT
O75791Q07666HPRD
O95400Q07666MINT
O95503Q07666IntAct
P03372Q07666IntAct
P04350Q07666IntAct
P05408Q07666IntAct
P06213Q07666HPRD
P06239Q07666HPRD; IntAct; MINT
P06241Q07666HPRD; IntAct; MINT
P06493Q07666HPRD
P07948Q07666HPRD; IntAct; MINT
P08631Q07666HPRD; IntAct
P09651Q07666MINT
P09769Q07666MINT
P12931Q07666HPRD; IntAct; MINT;MINT
P14598Q07666HPRD
P15498Q07666MINT
P16333Q07666HPRD; MINT
P16885Q07666HPRD
P19174Q07666IntAct;HPRD
P20936Q07666HPRD; IntAct
P22681Q07666HPRD; IntAct
P27986Q07666HPRD
P28290Q07666IntAct
P28482Q07666HPRD
P29350Q07666IntAct
P38159Q07666IntAct
P40763Q07666HPRD; IntAct
P46108Q07666IntAct
P46109Q07666IntAct
P50616Q07666IntAct
P51531Q07666HPRD; DIP; IntAct
P52333Q07666HPRD; IntAct
P60709Q07666IntAct
P60763Q07666MINT
P61978Q07666IntAct;HPRD
P62987Q07666HPRD
P62993Q07666HPRD; IntAct
Q06187Q07666HPRD
Q07666Q07666HPRD; MINT
Q07666Q08211HPRD
Q07666Q08881HPRD
Q07666Q09472IntAct
Q07666Q12805IntAct
Q07666Q13509HPRD; MINT
Q07666Q13588HPRD
Q07666Q13702HPRD
Q07666Q13882HPRD
Q07666Q15796HPRD; MINT
Q07666Q4LE28HPRD
Q07666Q68CJ9IntAct
Q07666Q68CZ2IntAct
Q07666Q8AZK7MINT
Q07666Q8N3X1HPRD; MINT
Q07666Q92569IntAct
Q07666Q92731IntAct
Q07666Q92793IntAct
Q07666Q92979HPRD; IntAct; MINT
Q07666Q96MU7HPRD
Q07666Q9H492IntAct
Q07666Q9NQX3IntAct
Q07666Q9NUX5IntAct
Q07666Q9UL18IntAct
Q07666Q9UNE7HPRD; IntAct; MINT