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Q14676 (MDC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of DNA damage checkpoint protein 1
Alternative name(s):
Nuclear factor with BRCT domains 1
Gene names
Name:MDC1
Synonyms:KIAA0170, NFBD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2089 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

Homodimer. Interacts with several proteins involved in the DNA damage response, although not all these interactions may be direct. Interacts with H2AFX, which requires phosphorylation of H2AFX on 'Ser-139'. Interacts with the MRN complex, composed of MRE11A/MRE11, RAD50, and NBN. Interacts with CHEK2, which requires ATM-mediated phosphorylation of 'Thr-68' within the FHA domain of CHEK2. Interacts constitutively with the BRCA1-BARD1 complex, SMC1A and TP53BP1. Interacts with ATM and FANCD2, and these interactions are reduced upon DNA damage. Also interacts with the PRKDC complex, composed of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7. This interaction may be required for PRKDC autophosphorylation, which is essential for DNA double strand break (DSB) repair. When phosphorylated by ATM, interacts with RNF8 (via FHA domain). Interacts with CEP164. When phosphorylated, interacts with APTX (via FHA-like domain). Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.22 Ref.23 Ref.29 Ref.32 Ref.34

Subcellular location

Nucleus. Chromosome By similarity. Note: Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires 'Ser-139' phosphorylation of H2AFX. Colocalizes with APTX at sites of DNA double-strand breaks. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.29

Tissue specificity

Highly expressed in testis. Ref.10

Domain

Tandemly repeated BRCT domains are characteristic of proteins involved in DNA damage signaling. In MDC1, these repeats are required for localization to chromatin which flanks sites of DNA damage marked by 'Ser-139' phosphorylation of H2AFX. Ref.10

Post-translational modification

Phosphorylated upon exposure to ionizing radiation (IR), ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation in response to IR requires ATM, NBN, and possibly CHEK2. Also phosphorylated during the G2/M phase of the cell cycle and during activation of the mitotic spindle checkpoint. Phosphorylation at Thr-4 by ATM stabilizes and enhances homodimerization via the FHA domain. Ref.10 Ref.13 Ref.14 Ref.15 Ref.37

Sumoylation at Lys-1840 by PIAS4 following DNA damage promotes ubiquitin-mediated degradation. Ref.32

Ubiquitinated by RNF4, leading to proteasomal degradation; undergoes 'Lys-48'-linked polyubiquitination. Ref.32

Sequence similarities

Contains 2 BRCT domains.

Contains 1 FHA domain.

Sequence caution

The sequence BAA11487.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAH18685.1 differs from that shown. Reason: Erroneous termination at position 1804. Translated as Gln.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14676-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14676-2)

The sequence of this isoform differs from the canonical sequence as follows:
     741-1004: Missing.
Isoform 3 (identifier: Q14676-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1124-1410: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q14676-4)

The sequence of this isoform differs from the canonical sequence as follows:
     741-1004: Missing.
     1029-1787: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20892089Mediator of DNA damage checkpoint protein 1
PRO_0000096316

Regions

Domain54 – 10552FHA
Domain1892 – 197079BRCT 1
Domain1991 – 208292BRCT 2
Region1 – 150150Interaction with CHEK2
Region2 – 220219Interaction with the MRN complex
Region145 – 568424Required for nuclear localization (NLS1)
Region1148 – 1610463Interaction with the PRKDC complex
Region1698 – 2089392Required for nuclear localization (NLS2)
Compositional bias1034 – 1469436Pro-rich

Amino acid modifications

Modified residue41Phosphothreonine; by ATM Ref.37
Modified residue1081Phosphoserine Ref.30
Modified residue1681Phosphoserine Ref.19 Ref.20 Ref.27 Ref.30
Modified residue2991Phosphoserine Ref.25 Ref.31
Modified residue3011Phosphothreonine Ref.25 Ref.31
Modified residue3291Phosphoserine Ref.27 Ref.30 Ref.31
Modified residue3311Phosphothreonine Ref.27 Ref.30
Modified residue3721Phosphoserine Ref.21 Ref.27
Modified residue3761Phosphoserine Ref.21 Ref.27
Modified residue3781Phosphothreonine Ref.21 Ref.27
Modified residue3941Phosphoserine Ref.25
Modified residue3971Phosphoserine Ref.25
Modified residue4021Phosphoserine Ref.25 Ref.27 Ref.30 Ref.31
Modified residue4041Phosphothreonine Ref.25 Ref.27 Ref.30 Ref.31
Modified residue4111Phosphoserine Ref.27
Modified residue4491Phosphothreonine Ref.25 Ref.27
Modified residue4531Phosphoserine Ref.25 Ref.27
Modified residue4551Phosphothreonine Ref.25 Ref.27 Ref.31
Modified residue4851Phosphoserine Ref.30
Modified residue4951Phosphoserine Ref.25 Ref.31
Modified residue4981Phosphoserine Ref.25 Ref.31
Modified residue5131Phosphoserine Ref.21 Ref.25 Ref.30
Modified residue5231Phosphothreonine Ref.21
Modified residue7801Phosphoserine Ref.21 Ref.25
Modified residue7931Phosphoserine Ref.25
Modified residue8121N6-acetyllysine Ref.28
Modified residue9551Phosphoserine Ref.30
Modified residue10331Phosphoserine Ref.25
Modified residue10681Phosphoserine Ref.25 Ref.30
Modified residue11571Phosphothreonine Ref.27
Modified residue11981Phosphothreonine Ref.25
Modified residue13991Phosphoserine Ref.25 Ref.30
Modified residue14001Phosphoserine Ref.25
Modified residue14021N6-acetyllysine Ref.28
Modified residue14031Phosphothreonine Ref.24 Ref.25 Ref.30
Modified residue14251Phosphothreonine Ref.24 Ref.25 Ref.30
Modified residue14661Phosphothreonine Ref.25 Ref.27
Modified residue15481Phosphothreonine Ref.25
Modified residue15671Phosphothreonine Ref.31
Modified residue15891Phosphothreonine Ref.25 Ref.30
Modified residue16041Phosphoserine Ref.25
Modified residue16301Phosphothreonine Ref.25
Modified residue16641Phosphothreonine Ref.25
Modified residue16711Phosphothreonine Ref.25
Modified residue16811Phosphoserine Ref.25
Modified residue16971Phosphothreonine Ref.25
Modified residue17021Phosphoserine Ref.25
Modified residue17111Phosphoserine Ref.25
Modified residue17751Phosphoserine Ref.25 Ref.30
Modified residue18001Phosphothreonine Ref.30
Modified residue18201Phosphoserine Ref.30 Ref.31
Modified residue18581Phosphothreonine Ref.25
Cross-link1840Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.32

Natural variations

Alternative sequence741 – 1004264Missing in isoform 2 and isoform 4.
VSP_014593
Alternative sequence1029 – 1787759Missing in isoform 4.
VSP_034103
Alternative sequence1124 – 1410287Missing in isoform 3.
VSP_034104
Natural variant1791R → C.
Corresponds to variant rs28986464 [ dbSNP | Ensembl ].
VAR_051160
Natural variant2511E → K. Ref.3
Corresponds to variant rs2517560 [ dbSNP | Ensembl ].
VAR_022843
Natural variant2681R → K. Ref.2 Ref.5
Corresponds to variant rs9262152 [ dbSNP | Ensembl ].
VAR_022844
Natural variant3711E → K. Ref.4
Corresponds to variant rs2075015 [ dbSNP | Ensembl ].
VAR_022845
Natural variant3861P → L. Ref.4
Corresponds to variant rs28986465 [ dbSNP | Ensembl ].
VAR_051161
Natural variant5361I → M. Ref.1 Ref.7
Corresponds to variant rs58344693 [ dbSNP | Ensembl ].
VAR_043922
Natural variant5861S → A. Ref.3
Corresponds to variant rs2844707 [ dbSNP | Ensembl ].
VAR_022846
Natural variant9171R → S.
Corresponds to variant rs28986467 [ dbSNP | Ensembl ].
VAR_051162
Natural variant11001P → A.
Corresponds to variant rs28994869 [ dbSNP | Ensembl ].
VAR_051163
Natural variant11121S → F.
Corresponds to variant rs28987085 [ dbSNP | Ensembl ].
VAR_051164
Natural variant11801S → P. Ref.4
Corresponds to variant rs9461623 [ dbSNP | Ensembl ].
VAR_051165
Natural variant15091E → D. Ref.3 Ref.4
Corresponds to variant rs3132589 [ dbSNP | Ensembl ].
VAR_022847
Natural variant15401S → P. Ref.1 Ref.3 Ref.7 Ref.25
Corresponds to variant rs3130645 [ dbSNP | Ensembl ].
VAR_022848
Natural variant15451Q → R. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs17292678 [ dbSNP | Ensembl ].
VAR_043923
Natural variant17451P → R.
Corresponds to variant rs28994871 [ dbSNP | Ensembl ].
VAR_051166
Natural variant17911V → E.
Corresponds to variant rs28994873 [ dbSNP | Ensembl ].
VAR_051167
Natural variant18551D → E.
Corresponds to variant rs28994874 [ dbSNP | Ensembl ].
VAR_051168
Natural variant18831R → Q.
Corresponds to variant rs28994875 [ dbSNP | Ensembl ].
VAR_051169
Natural variant19041R → Q.
Corresponds to variant rs28994876 [ dbSNP | Ensembl ].
VAR_051170

Experimental info

Mutagenesis581R → A: Abrogates binding to the MRE11 complex and to CHEK2. Ref.13 Ref.14
Mutagenesis721S → A: Abrogates binding to CHEK2. Ref.14
Mutagenesis961N → A: Abrogates binding to CHEK2; when associated with A-97 and A-98. Ref.14
Mutagenesis971G → A: Abrogates binding to CHEK2; when associated with A-96 and A-98. Ref.14
Mutagenesis981T → A: Abrogates binding to CHEK2; when associated with A-96 and A-97. Ref.14
Mutagenesis18401K → R: Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination. Ref.32
Sequence conflict6381L → P in CAH18685. Ref.2
Sequence conflict645 – 1326682Missing in CAH18685. Ref.2
Sequence conflict10051G → GS in BAB63322. Ref.3
Sequence conflict10411T → A in BAA11487. Ref.1
Sequence conflict10411T → A in AAI52557. Ref.7
Sequence conflict12661Y → S in BAE78617. Ref.4
Sequence conflict12831P → T in BAE78617. Ref.4
Sequence conflict15331A → T in BAC54931. Ref.4
Sequence conflict15331A → T in BAF31266. Ref.4
Sequence conflict15361E → A in CAM25929. Ref.5
Sequence conflict16641T → S in BAE78617. Ref.4
Sequence conflict16681Q → R in CAH18685. Ref.2
Sequence conflict17341A → T in BAE78617. Ref.4
Sequence conflict18431E → K Ref.2
Sequence conflict20481H → R Ref.2

Secondary structure

............................................................ 2089
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 3.
Checksum: A8B880A25617EC96

FASTA2,089226,666
        10         20         30         40         50         60 
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP 

        70         80         90        100        110        120 
DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL 

       130        140        150        160        170        180 
ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGETQPQ RLLLAEDSEE EVDFLSERRM 

       190        200        210        220        230        240 
VKKSRTTSSS VIVPESDEEG HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG 

       250        260        270        280        290        300 
ATVEAKQSEA EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD 

       310        320        330        340        350        360 
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR KIFHGVGTRG 

       370        380        390        400        410        420 
PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI NSDTDDEEEV SAALTLAHLK 

       430        440        450        460        470        480 
ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE RDSDTDVEEE ELPVENREAV LKDHTKIRAL 

       490        500        510        520        530        540 
VRAHSEKDQP PFGDSDDSVE ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK 

       550        560        570        580        590        600 
HQVSVEGTNQ TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL 

       610        620        630        640        650        660 
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV DTDTLGESTQ 

       670        680        690        700        710        720 
PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ CFLENQGLEA VQSMEDEPTQ 

       730        740        750        760        770        780 
AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL ATQPFCLRES EDSETQPFDT HLEAYGPCLS 

       790        800        810        820        830        840 
PPRAIPGDQH PESPVHTEPM GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP 

       850        860        870        880        890        900 
ERQTDVTGEE ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI 

       910        920        930        940        950        960 
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE PEGGSQDQKG 

       970        980        990       1000       1010       1020 
QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR RHQKGLLNCK MPPAEKASRI 

      1030       1040       1050       1060       1070       1080 
RAAEKVSRGD QESPDACLPP TVPEAPAPPQ KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK 

      1090       1100       1110       1120       1130       1140 
TRQDGSQEAP EAPLSSELEP FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK 

      1150       1160       1170       1180       1190       1200 
PTSQATRSRT NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE 

      1210       1220       1230       1240       1250       1260 
TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL QPSTSTDQPV 

      1270       1280       1290       1300       1310       1320 
TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP VTPKPTSRTT RSRTNMSSVK 

      1330       1340       1350       1360       1370       1380 
TPETVVPTAP ELQISTSTDQ PVTPKPTSRT TRSRTNMSSV KNPESTVPIA PELPPSTSTE 

      1390       1400       1410       1420       1430       1440 
QPVTPEPTSR ATRGRKNRSS GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS 

      1450       1460       1470       1480       1490       1500 
SVKTPETVVP TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA 

      1510       1520       1530       1540       1550       1560 
STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE PTSRATRGRT 

      1570       1580       1590       1600       1610       1620 
NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR TNRSSVKTPE PVVPTAPEPH 

      1630       1640       1650       1660       1670       1680 
PTTSTDQPVT PKLTSRATRR KTNRSSVKTP KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ 

      1690       1700       1710       1720       1730       1740 
SKTLRSSTVR AMPVPTTPEF QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK 

      1750       1760       1770       1780       1790       1800 
PCSAPLEPKS QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT 

      1810       1820       1830       1840       1850       1860 
PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP GKEEDVVTPK 

      1870       1880       1890       1900       1910       1920 
PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV VDARGERAVL ALGGSLAGSA 

      1930       1940       1950       1960       1970       1980 
AEASHLVTDR IRRTVKFLCA LGRGIPILSL DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG 

      1990       2000       2010       2020       2030       2040 
FSLQDALSRA RERRLLEGYE IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI 

      2050       2060       2070       2080 
TCPQDFPHCS IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST 

« Hide

Isoform 2 [UniParc].

Checksum: A8837EC5FB7EC360
Show »

FASTA1,825197,598
Isoform 3 [UniParc].

Checksum: FF7FB09BDF3E6178
Show »

FASTA1,802195,986
Isoform 4 [UniParc].

Checksum: F3816B14D9E11884
Show »

FASTA1,066116,634

References

« Hide 'large scale' references
[1]"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."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS MET-536; PRO-1540 AND ARG-1545.
Tissue: Myelomonocyte.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-268.
Tissue: Testis.
[3]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-251; ALA-586; ASP-1509; PRO-1540 AND ARG-1545.
[4]"Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A. expand/collapse author list , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-371; LEU-386; PRO-1180; ASP-1509 AND ARG-1545.
Tissue: Peripheral blood leukocyte.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-268 AND ARG-1545.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-1545.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-2089 (ISOFORM 4), VARIANTS MET-536; PRO-1540 AND ARG-1545.
Tissue: Pancreas.
[8]"53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage."
Mochan T.A., Venere M., DiTullio R.A. Jr., Halazonetis T.D.
Cancer Res. 63:8586-8591(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"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."
Shang Y.L., Bodero A.J., Chen P.-L.
J. Biol. Chem. 278:6323-6329(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways."
Xu X., Stern D.F.
J. Biol. Chem. 278:8795-8803(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL CYCLE-DEPENDENT PHOSPHORYLATION, DOMAINS NLS1 AND NLS2.
[11]"NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage."
Peng A., Chen P.-L.
J. Biol. Chem. 278:8873-8876(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2.
[12]"Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control."
Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.
J. Biol. Chem. 278:13599-13602(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND BARD1.
[13]"MDC1 is required for the intra-S-phase DNA damage checkpoint."
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D., Bartek J., Jackson S.P.
Nature 421:952-956(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, MUTAGENESIS OF ARG-58.
[14]"MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
Lou Z., Minter-Dykhouse K., Wu X., Chen J.
Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2, PHOSPHORYLATION BY ATM AND CHEK2, MUTAGENESIS OF ARG-58; SER-72; ASN-96; GLY-97 AND THR-98.
[15]"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM; FANCD2; H2AFX; SMC1A AND TP53BP1, PHOSPHORYLATION BY ATM.
[16]"MDC1/NFBD1: a key regulator of the DNA damage response in higher eukaryotes."
Stucki M., Jackson S.P.
DNA Repair 3:953-957(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention."
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.
EMBO J. 23:2674-2683(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH H2AFX.
[18]"MDC1 regulates DNA-PK autophosphorylation in response to DNA damage."
Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J., Chen J.
J. Biol. Chem. 279:46359-46362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PRKDC COMPLEX.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[21]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-376; THR-378; SER-513; THR-523 AND SER-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[22]"Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase."
Kolas N.K., Chapman J.R., Nakada S., Ylanko J., Chahwan R., Sweeney F.D., Panier S., Mendez M., Wildenhain J., Thomson T.M., Pelletier L., Jackson S.P., Durocher D.
Science 318:1637-1640(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF8.
[23]"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1."
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.
Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP164.
[24]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1403 AND THR-1425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; THR-301; SER-394; SER-397; SER-402; THR-404; THR-449; SER-453; THR-455; SER-495; SER-498; SER-513; SER-780; SER-793; SER-1033; SER-1068; THR-1198; SER-1399; SER-1400; THR-1403; THR-1425; THR-1466; THR-1548; THR-1589; SER-1604; THR-1630; THR-1664; THR-1671; SER-1681; THR-1697; SER-1702; SER-1711; SER-1775 AND THR-1858, VARIANT [LARGE SCALE ANALYSIS] PRO-1540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-329; THR-331; SER-372; SER-376; THR-378; SER-402; THR-404; SER-411; THR-449; SER-453; THR-455; THR-1157 AND THR-1466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-812 AND LYS-1402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response."
Becherel O.J., Jakob B., Cherry A.L., Gueven N., Fusser M., Kijas A.W., Peng C., Katyal S., McKinnon P.J., Chen J., Epe B., Smerdon S.J., Taucher-Scholz G., Lavin M.F.
Nucleic Acids Res. 38:1489-1503(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APTX.
[30]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-168; SER-329; THR-331; SER-402; THR-404; SER-485; SER-513; SER-955; SER-1068; SER-1399; THR-1403; THR-1425; THR-1589; SER-1775; THR-1800 AND SER-1820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; THR-301; SER-329; SER-402; THR-404; THR-455; SER-495; SER-498; THR-1567 AND SER-1820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Sumoylation of MDC1 is important for proper DNA damage response."
Luo K., Zhang H., Wang L., Yuan J., Lou Z.
EMBO J. 31:3008-3019(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-1840, UBIQUITINATION BY RNF4, MUTAGENESIS OF LYS-1840, INTERACTION WITH TP53BP1.
[33]"MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks."
Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P.
Cell 123:1213-1226(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1883-2089 IN COMPLEX WITH PHOSPHORYLATED H2AFX.
[34]"Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail."
Lee M.S., Edwards R.A., Thede G.L., Glover J.N.M.
J. Biol. Chem. 280:32053-32056(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1891-2086, INTERACTION WITH PHOSPHORYLATED H2AFX.
[35]"Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1."
Campbell S.J., Edwards R.A., Glover J.N.
Structure 18:167-176(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1891-2089 IN COMPLEX WITH PHOSPHORYLATED HISTONE TETRAPEPTIDE.
[36]"Molecular basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex."
Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.
J. Biol. Chem. 287:2854-2862(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1884-2089.
[37]"Structural mechanism of the phosphorylation-dependent dimerization of the MDC1 forkhead-associated domain."
Liu J., Luo S., Zhao H., Liao J., Li J., Yang C., Xu B., Stern D.F., Xu X., Ye K.
Nucleic Acids Res. 40:3898-3912(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-10 AND 19-138, PHOSPHORYLATION AT THR-4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D79992 mRNA. Translation: BAA11487.2. Different initiation.
CR749828 mRNA. Translation: CAH18685.1. Different termination.
BA000025 Genomic DNA. Translation: BAB63322.1.
AB088099 Genomic DNA. Translation: BAC54931.1.
AB202097 Genomic DNA. Translation: BAE78617.1.
AB103605 Genomic DNA. Translation: BAF31266.1.
AL662848 Genomic DNA. Translation: CAI17440.1.
AL662797 Genomic DNA. Translation: CAI18195.1.
AL845353 Genomic DNA. Translation: CAI41890.2.
AL845353 Genomic DNA. Translation: CAI41891.1.
AL662848 Genomic DNA. Translation: CAM24847.1.
AL662797 Genomic DNA. Translation: CAM25512.1.
BX248307 Genomic DNA. Translation: CAM25928.1.
BX248307 Genomic DNA. Translation: CAM25929.1.
BX927283 Genomic DNA. Translation: CAQ06769.1.
BX927283 Genomic DNA. Translation: CAQ06770.1.
CR936878 Genomic DNA. Translation: CAQ06813.1.
CR936878 Genomic DNA. Translation: CAQ06814.1.
CR788240 Genomic DNA. Translation: CAQ07571.1.
CR788240 Genomic DNA. Translation: CAQ07572.1.
CR759873 Genomic DNA. Translation: CAQ08690.1.
CR759873 Genomic DNA. Translation: CAQ08691.1.
CH471081 Genomic DNA. Translation: EAX03321.1.
BC110645 mRNA. Translation: AAI10646.1.
BC152556 mRNA. Translation: AAI52557.1.
RefSeqNP_055456.2. NM_014641.2.
XP_005249551.1. XM_005249494.2.
XP_005272968.1. XM_005272911.2.
XP_005274958.1. XM_005274901.2.
XP_005275124.1. XM_005275067.2.
XP_005275253.1. XM_005275196.2.
XP_005275257.1. XM_005275200.1.
XP_005275380.1. XM_005275323.2.
UniGeneHs.653495.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ADOX-ray1.45A/B1891-2086[»]
2AZMX-ray2.41A/B1883-2089[»]
2ETXX-ray1.33A/B1884-2089[»]
3K05X-ray1.33A/B1891-2089[»]
3UEOX-ray2.60E/F325-336[»]
3UMZX-ray1.65A/B27-138[»]
3UN0X-ray2.30A/B26-138[»]
3UNMX-ray1.80A/B27-138[»]
3UNNX-ray1.70A27-138[»]
B1-8[»]
3UOTX-ray1.80A/B19-138[»]
D/E1-10[»]
ProteinModelPortalQ14676.
SMRQ14676. Positions 29-133, 1891-2085.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115014. 176 interactions.
DIPDIP-33603N.
IntActQ14676. 15 interactions.
MINTMINT-259925.

PTM databases

PhosphoSiteQ14676.

Proteomic databases

PaxDbQ14676.
PRIDEQ14676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376405; ENSP00000365587; ENSG00000137337. [Q14676-2]
ENST00000376406; ENSP00000365588; ENSG00000137337. [Q14676-1]
ENST00000383566; ENSP00000373060; ENSG00000206481.
ENST00000420019; ENSP00000396484; ENSG00000224587. [Q14676-1]
ENST00000420320; ENSP00000416511; ENSG00000225589. [Q14676-1]
ENST00000427406; ENSP00000387429; ENSG00000234012. [Q14676-1]
ENST00000435664; ENSP00000404318; ENSG00000231135.
ENST00000440369; ENSP00000415212; ENSG00000228575. [Q14676-1]
ENST00000449153; ENSP00000409167; ENSG00000237095. [Q14676-1]
ENST00000546487; ENSP00000448679; ENSG00000237095. [Q14676-3]
ENST00000547047; ENSP00000449059; ENSG00000228575. [Q14676-3]
ENST00000547874; ENSP00000447682; ENSG00000234012. [Q14676-2]
ENST00000548112; ENSP00000448434; ENSG00000224587. [Q14676-3]
ENST00000548542; ENSP00000446597; ENSG00000228575. [Q14676-2]
ENST00000550004; ENSP00000447084; ENSG00000224587. [Q14676-2]
ENST00000551204; ENSP00000447799; ENSG00000225589. [Q14676-3]
ENST00000551460; ENSP00000449274; ENSG00000234012. [Q14676-3]
ENST00000552263; ENSP00000447069; ENSG00000225589. [Q14676-2]
ENST00000553048; ENSP00000447787; ENSG00000237095. [Q14676-2]
GeneID9656.
KEGGhsa:9656.
UCSCuc003nrf.4. human. [Q14676-4]
uc003nrg.4. human. [Q14676-1]
uc011dmp.1. human. [Q14676-2]

Organism-specific databases

CTD9656.
GeneCardsGC06M030667.
GC06Mi30675.
GC06Mj30657.
GC06Mk30657.
GC06Ml30712.
GC06Mm30746.
GC06Mn30657.
GC06Mo30659.
HGNCHGNC:21163. MDC1.
HPAHPA006915.
MIM607593. gene.
neXtProtNX_Q14676.
PharmGKBPA134942837.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG080567.
InParanoidQ14676.
OMAVIEILAW.
PhylomeDBQ14676.
TreeFamTF329580.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SignaLinkQ14676.

Gene expression databases

ArrayExpressQ14676.
BgeeQ14676.
GenevestigatorQ14676.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 2 hits.
SM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMDC1. human.
EvolutionaryTraceQ14676.
GeneWikiMDC1.
GenomeRNAi9656.
NextBio36251.
PROQ14676.
SOURCESearch...

Entry information

Entry nameMDC1_HUMAN
AccessionPrimary (citable) accession number: Q14676
Secondary accession number(s): A2AB04 expand/collapse secondary AC list , A2BF04, A2RRA8, A7YY86, B0S8A2, Q0EFC2, Q2L6H7, Q2TAZ4, Q5JP55, Q5JP56, Q5ST83, Q68CQ3, Q86Z06, Q96QC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM