Gene name: SAV1

Uniprot entry:

Q9H4B6

Protein names:

Protein salvador homolog 1 (45 kDa WW domain protein) (hWW45)

Protein sequence:

1_MLSRK 6_ KTKNE 11_ VSKPA 16_ EVQGK 21_ YVKKE 26_ TSPLL 31_ RNLMP 36_ SFIRH 41_ GPTIP 46_ RRTDI 51_ CLPDS 56_ SPNAF 61_ STSGD 66_ VVSRN 71_ QSFLR 76_ TPIQR 81_ TPHEI 86_ MRRES 91_ NRLSA 96_ PSYLA 101_ RSLAD 106_ VPREY 111_ GSSQS 116_ FVTEV 121_ SFAVE 126_ NGDSG 131_ SRYYY 136_ SDNFF 141_ DGQRK 146_ RPLGD 151_ RAHED 156_ YRYYE 161_ YNHDL 166_ FQRMP 171_ QNQGR 176_ HASGI 181_ GRVAA 186_ TSLGN 191_ LTNHG 196_ SEDLP 201_ LPPGW 206_ SVDWT 211_ MRGRK 216_ YYIDH 221_ NTNTT 226_ HWSHP 231_ LEREG 236_ LPPGW 241_ ERVES 246_ SEFGT 251_ YYVDH 256_ TNKKA 261_ QYRHP 266_ CAPSV 271_ PRYDQ 276_ PPPVT 281_ YQPQQ 286_ TERNQ 291_ SLLVP 296_ ANPYH 301_ TAEIP 306_ DWLQV 311_ YARAP 316_ VKYDH 321_ ILKWE 326_ LFQLA 331_ DLDTY 336_ QGMLK 341_ LLFMK 346_ ELEQI 351_ VKMYE 356_ AYRQA 361_ LLTEL 366_ ENRKQ 371_ RQQWY 376_AQQHG

Protein annotations

Protein functions:

1: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:29063833). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation