ID F6PRU9_CALJA Unreviewed; 2061 AA.
AC F6PRU9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Mediator of DNA damage checkpoint protein 1 {ECO:0000256|ARBA:ARBA00015014};
GN Name=MDC1 {ECO:0000313|Ensembl:ENSCJAP00000045692.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000045692.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000045692.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000045692.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
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DR STRING; 9483.ENSCJAP00000045692; -.
DR Ensembl; ENSCJAT00000061591.4; ENSCJAP00000045692.4; ENSCJAG00000019900.6.
DR GeneTree; ENSGT00940000161757; -.
DR InParanoid; F6PRU9; -.
DR OMA; HGDCETD; -.
DR Proteomes; UP000008225; Chromosome 4.
DR Bgee; ENSCJAG00000019900; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0140566; F:histone reader activity; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:Ensembl.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IEA:Ensembl.
DR CDD; cd17744; BRCT_MDC1_rpt1; 1.
DR CDD; cd18441; BRCT_MDC1_rpt2; 1.
DR CDD; cd22665; FHA_MDC1; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR23196:SF1; MEDIATOR OF DNA DAMAGE CHECKPOINT PROTEIN 1; 1.
DR PANTHER; PTHR23196; PAX TRANSCRIPTION ACTIVATION DOMAIN INTERACTING PROTEIN; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 1..42
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1864..1942
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2061 AA; 223461 MW; 6CB8EEDFE9C901FE CRC64;
MPGCSVALPF PSISKQHAEI EISAWDKAPI LRDCGSLNGT QILRPPKVLS PGVSHRLRDQ
ELILFADLPC QYHRLDVPLP FVSRGPLTVE ETPRVQGGTQ PQRLLLAEDS EEEVDSLSER
CVIKKSRTTS SSVGMIVPES DEEGNSPVLG GPGLPFAFTL NSDTVAEDQQ PATEEASSAA
RRGAAIEPEQ SEAEVTTEIQ LEKNQPSVKE RDNDTKVKRG AGNGVVLAGM MLERSQPPAE
DSDTDVDDDS RPPGRPAEVH LERVQPLGFI DSDTDIEEEG IPATPAVVPM KKRKIFHGVG
IRGPGAPGLA HLQESQAGSD TDMEEGKAPQ AVPLKKSQAS MVINSDTDDE EEVSAALTLA
RLKESQPALW NRDAEEDMAQ PVVLLQRSQT TTGRDSDTDE EEKLPVENKE AVPKGHTKIR
ALFRAHSEKN QHSFRDSDKS VEADKSSPGI HLERSQASTT VDINTQVKES AMVPMQGTNQ
TDVEAGGGRE KLLVVSLEEA WPPPHGLCET DAEEGTSLAA SAVADVRKSQ LPAEGDAGAE
WATAVLKQER ALKVGAQGQS PVAQMEQDLP ISRENLTDLV VDTDALGEST QRQGEGAQVP
TGREREPHVG GTKDSKDNCD DSEDLDLQAT QCFLERKNQS LEAVQSMEDE PTQTFMLTPP
QEPGPSHCSF QTPGSLDEPW EVLATQPFCL RESKDSETQP FDTYLEACGS CLSPPRAIPG
DQHPESPVHT EPMGIQGREM QTMDKDMGIP KETTERMAPE RVPLERETEK LMPERQTDVT
GEEELTRGMQ DREQKQLLAR DSQRQESGKK GESASPKRNR ESSKVEIQTS EEIQEKEVEK
QTLPNKTFER DVERPVADRE CEPAELEGKV PKVILERGTQ RGEPEGGSRD QKGQASSPTP
EPGVGVRDFP EPASAPIPSG SQSGERGSPV SPRRHQKGLN CKMPPAKKAS RIRAAKKASR
GDQESPDACL HPTVPETSAP PLKPLNSQSQ KRLAPQPLLS PFPPSIEPTI PKTRQNGNRE
APGTPLSSEL EPFHPKPKII TQKSSRMTPF PATSAALEPQ PSTSTTHPDT PKPTSQATRG
KTNRSSVKTP ETFVPTAPEL QPSTSTDQPV TPEPTFQATR GRKNRFSVKT PETVVPTAPE
PHPSTSRDQP VTPKPTSQAT RGKTNRSSIK TPETFVPTAP ELQPSTSTNQ LVTHEFTSWA
TRGRTNRSSV KTPESTVPVA PELPPSTSTD QPVTPEPTSR TTRGRTNKSS VKTPESVVST
APELQPCTST DQLVTPEPTS QTTRGRTNKS AVKSPESVVS TAPELQPCTS TDQLVTPEPT
SRATRGRKNR SSVKNPERVI STAPELQAST STDQPVTPEP TSQATRRRKN RSSVKTPETV
VPIASELQAS AFTDQPVTPE PTSQATRGRK NRPSVKTPET VVLIASELQA SASTDQPVTP
EPTSQATRGR KNRSSVKTPE TVVPIASELQ ASASTDQPVT PEPTSRTTRG RTNRSSVKTP
ESVVPTAPEL QVSASTVQPV TPEPTSQTTR GRTNRSSVKT PESVVPIAPE LQPSTSRNQL
VTPEPTSRAT RGRTDGSSVR TPEPVVPTAP EPVPTTSIDQ PVTPKPTSRA TRGRVNRSSV
KTPKPVEPAA SNLEPLIPTD LPVTPEAIAQ GSQSKTLRSS IVSAVSVPTT LEFQSPVTTD
QPISPEPIPQ ASCSKRQRVI GNPGSLKTPI DHKPCSAPLE TKSQASRNQR WGAVREAESL
TAIPEPASFQ LLETPTHASQ IQKVEAVGRS RFTSEPQPKV SQSRKRPFAT TDSPPLQKQP
RREVSQKTVF LKEELEDTTE KPGKEEDVMT PKPGKKKRDQ AEEEPNSIQS RSLRRTKLTR
ESTAPKVLFT GVVDAQGERA VLALGGSLAD SAAEASHLVT DRIRRTVKFL CALGRGIPIL
SLDWLHQSRK AGCFLPPDEY VVTDPEQEKN FGFSLQDALS RARERRLLEG YEIHVTPGVQ
PPPPQMGEII SCCGGTVLPS MPRSYKPQRV VITCSQDFPR CSVPRRVGLP LLSPEFLLTG
VLKQEAKPEA FVLSPLEMSS T
//
