Details for: MDC1
Associated with
Other Information
Genular Protein ID: 1562246674
Symbol: MDC1_HUMAN
Name: Mediator of DNA damage checkpoint protein 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8724849
Title: Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1.
PubMed ID: 8724849
PubMed ID: 17974005
Title: The full-ORF clone resource of the German cDNA consortium.
PubMed ID: 17974005
PubMed ID: 16702430
Title: Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity.
PubMed ID: 16702430
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 14695167
Title: 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage.
PubMed ID: 14695167
PubMed ID: 12475977
Title: NFBD1, a novel nuclear protein with signature motifs of FHA and BRCT, and an internal 41-amino acid repeat sequence, is an early participant in DNA damage response.
PubMed ID: 12475977
PubMed ID: 12499369
Title: NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways.
PubMed ID: 12499369
PubMed ID: 12551934
Title: NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage.
PubMed ID: 12551934
PubMed ID: 12611903
Title: Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control.
PubMed ID: 12611903
PubMed ID: 12607003
Title: MDC1 is required for the intra-S-phase DNA damage checkpoint.
PubMed ID: 12607003
DOI: 10.1038/nature01445
PubMed ID: 12607004
Title: MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways.
PubMed ID: 12607004
DOI: 10.1038/nature01447
PubMed ID: 12607005
Title: MDC1 is a mediator of the mammalian DNA damage checkpoint.
PubMed ID: 12607005
DOI: 10.1038/nature01446
PubMed ID: 15279781
Title: MDC1/NFBD1: a key regulator of the DNA damage response in higher eukaryotes.
PubMed ID: 15279781
PubMed ID: 15201865
Title: Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention.
PubMed ID: 15201865
PubMed ID: 15377652
Title: MDC1 regulates DNA-PK autophosphorylation in response to DNA damage.
PubMed ID: 15377652
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 17693683
Title: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.
PubMed ID: 17693683
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18006705
Title: Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase.
PubMed ID: 18006705
PubMed ID: 18283122
Title: Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1.
PubMed ID: 18283122
DOI: 10.1101/gad.1627708
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20008512
Title: CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response.
PubMed ID: 20008512
DOI: 10.1093/nar/gkp1149
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21482717
Title: MDC1 collaborates with TopBP1 in DNA replication checkpoint control.
PubMed ID: 21482717
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22635276
Title: Sumoylation of MDC1 is important for proper DNA damage response.
PubMed ID: 22635276
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 30898438
Title: MDC1 interacts with TOPBP1 to maintain chromosomal stability during mitosis.
PubMed ID: 30898438
PubMed ID: 35842428
Title: The CIP2A-TOPBP1 complex safeguards chromosomal stability during mitosis.
PubMed ID: 35842428
PubMed ID: 16377563
Title: MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks.
PubMed ID: 16377563
PubMed ID: 16049003
Title: Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail.
PubMed ID: 16049003
PubMed ID: 20159462
Title: Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1.
PubMed ID: 20159462
PubMed ID: 22139841
Title: Molecular basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex.
PubMed ID: 22139841
PubMed ID: 22234877
Title: Structural mechanism of the phosphorylation-dependent dimerization of the MDC1 forkhead-associated domain.
PubMed ID: 22234877
DOI: 10.1093/nar/gkr1296
PubMed ID: 23891287
Title: Structural insights into recognition of MDC1 by TopBP1 in DNA replication checkpoint control.
PubMed ID: 23891287
Sequence Information:
- Length: 2089
- Mass: 226666
- Checksum: A8B880A25617EC96
- Sequence:
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL ATQPFCLRES EDSETQPFDT HLEAYGPCLS PPRAIPGDQH PESPVHTEPM GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP ERQTDVTGEE ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE PEGGSQDQKG QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR RHQKGLLNCK MPPAEKASRI RAAEKVSRGD QESPDACLPP TVPEAPAPPQ KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK TRQDGSQEAP EAPLSSELEP FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK PTSQATRSRT NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL QPSTSTDQPV TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP VTPKPTSRTT RSRTNMSSVK TPETVVPTAP ELQISTSTDQ PVTPKPTSRT TRSRTNMSSV KNPESTVPIA PELPPSTSTE QPVTPEPTSR ATRGRKNRSS GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS SVKTPETVVP TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE PTSRATRGRT NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR TNRSSVKTPE PVVPTAPEPH PTTSTDQPVT PKLTSRATRR KTNRSSVKTP KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ SKTLRSSTVR AMPVPTTPEF QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK PCSAPLEPKS QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP GKEEDVVTPK PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV VDARGERAVL ALGGSLAGSA AEASHLVTDR IRRTVKFLCA LGRGIPILSL DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG FSLQDALSRA RERRLLEGYE IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI TCPQDFPHCS IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST
Genular Protein ID: 127554728
Symbol: A1Z5I9_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 19
- Mass: 2326
- Checksum: 0200C23525665A0E
- Sequence:
MEDTQAIDWD VEEEEETEQ
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.