E3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING finger protein 196) (RING-type E3 ubiquitin transferase CHFR)
1_MERPE 6_ EGKQS 11_ PPPQP 16_ WGRLL 21_ RLGAE 26_ EGEPH 31_ VLLRK 36_ REWTI 41_ GRRRG 46_ CDLSF 51_ PSNKL 56_ VSGDH 61_ CRIVV 66_ DEKSG 71_ QVTLE 76_ DTSTS 81_ GTVIN 86_ KLKVV 91_ KKQTC 96_ PLQTG 101_ DVIYL 106_ VYRKN 111_ EPEHN 116_ VAYLY 121_ ESLSE 126_ KQGMT 131_ QESFE 136_ ANKEN 141_ VFHGT 146_ KDTSG 151_ AGAGR 156_ GADPR 161_ VPPSS 166_ PATQV 171_ CFEEP 176_ QPSTS 181_ TSDLF 186_ PTASA 191_ SSTEP 196_ SPAGR 201_ ERSSS 206_ CGSGG 211_ GGISP 216_ KGSGP 221_ SVASD 226_ EVSSF 231_ ASALP 236_ DRKTA 241_ SFSSL 246_ EPQDQ 251_ EDLEP 256_ VKKKM 261_ RGDGD 266_ LDLNG 271_ QLLVA 276_ QPRRN 281_ AQTVH 286_ EDVRA 291_ AAGKP 296_ DKMEE 301_ TLTCI 306_ ICQDL 311_ LHDCV 316_ SLQPC 321_ MHTFC 326_ AACYS 331_ GWMER 336_ SSLCP 341_ TCRCP 346_ VERIC 351_ KNHIL 356_ NNLVE 361_ AYLIQ 366_ HPDKS 371_ RSEED 376_ VQSMD 381_ ARNKI 386_ TQDML 391_ QPKVR 396_ RSFSD 401_ EEGSS 406_ EDLLE 411_ LSDVD 416_ SESSD 421_ ISQPY 426_ VVCRQ 431_ CPEYR 436_ RQAAQ 441_ PPHCP 446_ APEGE 451_ PGAPQ 456_ ALGDA 461_ PSTSV 466_ SLTTA 471_ VQDYV 476_ CPLQG 481_ SHALC 486_ TCCFQ 491_ PMPDR 496_ RAERE 501_ QDPRV 506_ APQQC 511_ AVCLQ 516_ PFCHL 521_ YWGCT 526_ RTGCY 531_ GCLAP 536_ FCELN 541_ LGDKC 546_ LDGVL 551_ NNNSY 556_ ESDIL 561_ KNYLA 566_ TRGLT 571_ WKNML 576_ TESLV 581_ ALQRG 586_ VFLLS 591_ DYRVT 596_ GDTVL 601_ CYCCG 606_ LRSFR 611_ ELTYQ 616_ YRQNI 621_ PASEL 626_ PVAVT 631_ SRPDC 636_ YWGRN 641_ CRTQV 646_ KAHHA 651_ MKFNH 656_ICEQT
1: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress