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Protein

Mediator of DNA damage checkpoint protein 1

Gene

MDC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 TP53BP1.10 Publications

GO - Molecular functioni

  • FHA domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137337-MONOMER.
ZFISH:ENSG00000140406-MONOMER.
ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ14676.
SIGNORiQ14676.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of DNA damage checkpoint protein 1
Alternative name(s):
Nuclear factor with BRCT domains 1
Gene namesi
Name:MDC1
Synonyms:KIAA0170, NFBD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21163. MDC1.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • focal adhesion Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58R → A: Abrogates binding to the MRE11 complex and to CHEK2. 2 Publications1
Mutagenesisi72S → A: Abrogates binding to CHEK2. 1 Publication1
Mutagenesisi96N → A: Abrogates binding to CHEK2; when associated with A-97 and A-98. 1 Publication1
Mutagenesisi97G → A: Abrogates binding to CHEK2; when associated with A-96 and A-98. 1 Publication1
Mutagenesisi98T → A: Abrogates binding to CHEK2; when associated with A-96 and A-97. 1 Publication1
Mutagenesisi1840K → R: Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination. 1 Publication1

Organism-specific databases

DisGeNETi9656.
OpenTargetsiENSG00000137337.
ENSG00000224587.
ENSG00000225589.
ENSG00000228575.
ENSG00000234012.
ENSG00000237095.
PharmGKBiPA134942837.

Polymorphism and mutation databases

BioMutaiMDC1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000963161 – 2089Mediator of DNA damage checkpoint protein 1Add BLAST2089

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4Phosphothreonine; by ATM1 Publication1
Modified residuei108PhosphoserineCombined sources1
Modified residuei146PhosphothreonineCombined sources1
Modified residuei168PhosphoserineCombined sources1
Modified residuei176PhosphoserineBy similarity1
Modified residuei299PhosphoserineCombined sources1
Modified residuei301PhosphothreonineCombined sources1
Modified residuei329PhosphoserineCombined sources1
Modified residuei331PhosphothreonineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei376PhosphoserineCombined sources1
Modified residuei378PhosphothreonineCombined sources1
Modified residuei394PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei402PhosphoserineCombined sources1
Modified residuei404PhosphothreonineCombined sources1
Modified residuei411PhosphoserineCombined sources1
Modified residuei449PhosphothreonineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei455PhosphothreonineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei495PhosphoserineCombined sources1
Modified residuei498PhosphoserineCombined sources1
Modified residuei504PhosphoserineBy similarity1
Modified residuei505PhosphoserineBy similarity1
Modified residuei513PhosphoserineCombined sources1
Modified residuei523PhosphothreonineCombined sources1
Modified residuei590PhosphoserineBy similarity1
Cross-linki616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei780PhosphoserineCombined sources1
Modified residuei793PhosphoserineCombined sources1
Modified residuei812N6-acetyllysineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei998PhosphoserineCombined sources1
Modified residuei1033PhosphoserineCombined sources1
Modified residuei1068PhosphoserineCombined sources1
Modified residuei1086PhosphoserineCombined sources1
Modified residuei1157PhosphothreonineCombined sources1
Modified residuei1198PhosphothreonineCombined sources1
Modified residuei1235PhosphoserineBy similarity1
Modified residuei1239PhosphothreonineCombined sources1
Modified residuei1280PhosphothreonineCombined sources1
Modified residuei1302PhosphothreonineCombined sources1
Modified residuei1399PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1
Modified residuei1402N6-acetyllysineCombined sources1
Modified residuei1403PhosphothreonineCombined sources1
Cross-linki1413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei1425PhosphothreonineCombined sources1
Modified residuei1466PhosphothreonineCombined sources1
Modified residuei1548PhosphothreonineCombined sources1
Modified residuei1564PhosphoserineCombined sources1
Modified residuei1567PhosphothreonineCombined sources1
Modified residuei1589PhosphothreonineCombined sources1
Modified residuei1604PhosphoserineCombined sources1
Modified residuei1608PhosphothreonineCombined sources1
Modified residuei1630PhosphothreonineCombined sources1
Modified residuei1664PhosphothreonineCombined sources1
Modified residuei1671PhosphothreonineCombined sources1
Modified residuei1681PhosphoserineCombined sources1
Modified residuei1697PhosphothreonineCombined sources1
Modified residuei1702PhosphoserineCombined sources1
Modified residuei1711PhosphoserineCombined sources1
Modified residuei1775PhosphoserineCombined sources1
Modified residuei1800PhosphothreonineCombined sources1
Modified residuei1820PhosphoserineCombined sources1
Cross-linki1840Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)2 Publications
Cross-linki1840Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1858PhosphothreonineCombined sources1
Modified residuei1943Omega-N-methylarginineCombined sources1

Post-translational modificationi

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.4 Publications
Sumoylation at Lys-1840 by PIAS4 following DNA damage promotes ubiquitin-mediated degradation.1 Publication
Ubiquitinated by RNF4, leading to proteasomal degradation; undergoes 'Lys-48'-linked polyubiquitination.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14676.
MaxQBiQ14676.
PaxDbiQ14676.
PeptideAtlasiQ14676.
PRIDEiQ14676.

PTM databases

iPTMnetiQ14676.
PhosphoSitePlusiQ14676.
SwissPalmiQ14676.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiENSG00000137337.
ExpressionAtlasiQ14676. baseline and differential.
GenevisibleiQ14676. HS.

Organism-specific databases

HPAiHPA006915.

Interactioni

Subunit structurei

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).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATMQ133152EBI-495644,EBI-495465
H2AFXP1610416EBI-495644,EBI-494830
NBNO6093426EBI-495644,EBI-494844
nbs1O430702EBI-495644,EBI-2125045From a different organism.
RNF8O7606411EBI-495644,EBI-373337

GO - Molecular functioni

  • FHA domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115014. 194 interactors.
DIPiDIP-33603N.
IntActiQ14676. 21 interactors.
MINTiMINT-259925.
STRINGi9606.ENSP00000365588.

Structurei

Secondary structure

12089
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 24Combined sources4
Beta strandi32 – 36Combined sources5
Beta strandi39 – 42Combined sources4
Beta strandi45 – 49Combined sources5
Beta strandi51 – 59Combined sources9
Beta strandi62 – 65Combined sources4
Beta strandi76 – 80Combined sources5
Beta strandi88 – 91Combined sources4
Beta strandi98 – 100Combined sources3
Turni101 – 104Combined sources4
Beta strandi120 – 123Combined sources4
Beta strandi126 – 132Combined sources7
Beta strandi1894 – 1897Combined sources4
Helixi1903 – 1911Combined sources9
Turni1920 – 1922Combined sources3
Beta strandi1924 – 1927Combined sources4
Helixi1935 – 1943Combined sources9
Helixi1951 – 1959Combined sources9
Helixi1966 – 1968Combined sources3
Helixi1973 – 1978Combined sources6
Helixi1983 – 1992Combined sources10
Turni1995 – 1998Combined sources4
Beta strandi2000 – 2003Combined sources4
Helixi2011 – 2020Combined sources10
Beta strandi2024 – 2026Combined sources3
Beta strandi2037 – 2040Combined sources4
Helixi2043 – 2048Combined sources6
Helixi2050 – 2055Combined sources6
Helixi2063 – 2071Combined sources9
Helixi2076 – 2079Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ14676.
SMRiQ14676.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 105FHAPROSITE-ProRule annotationAdd BLAST52
Domaini1892 – 1970BRCT 1PROSITE-ProRule annotationAdd BLAST79
Domaini1991 – 2082BRCT 2PROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 150Interaction with CHEK2Add BLAST150
Regioni2 – 220Interaction with the MRN complexAdd BLAST219
Regioni145 – 568Required for nuclear localization (NLS1)Add BLAST424
Regioni1148 – 1610Interaction with the PRKDC complexAdd BLAST463
Regioni1698 – 2089Required for nuclear localization (NLS2)Add BLAST392

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1034 – 1469Pro-richAdd BLAST436

Domaini

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.1 Publication

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation
Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2043. Eukaryota.
ENOG4111RPS. LUCA.
GeneTreeiENSGT00600000084454.
HOVERGENiHBG080567.
InParanoidiQ14676.
KOiK20780.
OMAiLSSEMEP.
OrthoDBiEOG091G0V3Z.
PhylomeDBiQ14676.
TreeFamiTF329580.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF16770. RTT107_BRCT_5. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14676-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH
60 70 80 90 100
LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI
110 120 130 140 150
LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET
160 170 180 190 200
PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG
210 220 230 240 250
HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA
260 270 280 290 300
EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
310 320 330 340 350
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR
360 370 380 390 400
KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI
410 420 430 440 450
NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE
460 470 480 490 500
RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE
510 520 530 540 550
ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ
560 570 580 590 600
TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
610 620 630 640 650
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV
660 670 680 690 700
DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ
710 720 730 740 750
CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL
760 770 780 790 800
ATQPFCLRES EDSETQPFDT HLEAYGPCLS PPRAIPGDQH PESPVHTEPM
810 820 830 840 850
GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP ERQTDVTGEE
860 870 880 890 900
ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
910 920 930 940 950
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE
960 970 980 990 1000
PEGGSQDQKG QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR
1010 1020 1030 1040 1050
RHQKGLLNCK MPPAEKASRI RAAEKVSRGD QESPDACLPP TVPEAPAPPQ
1060 1070 1080 1090 1100
KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK TRQDGSQEAP EAPLSSELEP
1110 1120 1130 1140 1150
FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK PTSQATRSRT
1160 1170 1180 1190 1200
NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE
1210 1220 1230 1240 1250
TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL
1260 1270 1280 1290 1300
QPSTSTDQPV TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP
1310 1320 1330 1340 1350
VTPKPTSRTT RSRTNMSSVK TPETVVPTAP ELQISTSTDQ PVTPKPTSRT
1360 1370 1380 1390 1400
TRSRTNMSSV KNPESTVPIA PELPPSTSTE QPVTPEPTSR ATRGRKNRSS
1410 1420 1430 1440 1450
GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS SVKTPETVVP
1460 1470 1480 1490 1500
TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA
1510 1520 1530 1540 1550
STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE
1560 1570 1580 1590 1600
PTSRATRGRT NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR
1610 1620 1630 1640 1650
TNRSSVKTPE PVVPTAPEPH PTTSTDQPVT PKLTSRATRR KTNRSSVKTP
1660 1670 1680 1690 1700
KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ SKTLRSSTVR AMPVPTTPEF
1710 1720 1730 1740 1750
QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK PCSAPLEPKS
1760 1770 1780 1790 1800
QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT
1810 1820 1830 1840 1850
PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP
1860 1870 1880 1890 1900
GKEEDVVTPK PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV
1910 1920 1930 1940 1950
VDARGERAVL ALGGSLAGSA AEASHLVTDR IRRTVKFLCA LGRGIPILSL
1960 1970 1980 1990 2000
DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG FSLQDALSRA RERRLLEGYE
2010 2020 2030 2040 2050
IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI TCPQDFPHCS
2060 2070 2080
IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST
Length:2,089
Mass (Da):226,666
Last modified:July 5, 2005 - v3
Checksum:iA8B880A25617EC96
GO
Isoform 2 (identifier: Q14676-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     741-1004: Missing.

Show »
Length:1,825
Mass (Da):197,598
Checksum:iA8837EC5FB7EC360
GO
Isoform 3 (identifier: Q14676-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1124-1410: Missing.

Note: No experimental confirmation available.
Show »
Length:1,802
Mass (Da):195,986
Checksum:iFF7FB09BDF3E6178
GO
Isoform 4 (identifier: Q14676-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     741-1004: Missing.
     1029-1787: Missing.

Note: No experimental confirmation available.
Show »
Length:1,066
Mass (Da):116,634
Checksum:iF3816B14D9E11884
GO

Sequence cautioni

The sequence BAA11487 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAH18685 differs from that shown. Reason: Erroneous termination at position 1804. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti638L → P in CAH18685 (PubMed:17974005).Curated1
Sequence conflicti645 – 1326Missing in CAH18685 (PubMed:17974005).CuratedAdd BLAST682
Sequence conflicti1005G → GS in BAB63322 (Ref. 3) Curated1
Sequence conflicti1041T → A in BAA11487 (PubMed:8724849).Curated1
Sequence conflicti1041T → A in AAI52557 (PubMed:15489334).Curated1
Sequence conflicti1266Y → S in BAE78617 (PubMed:16702430).Curated1
Sequence conflicti1283P → T in BAE78617 (PubMed:16702430).Curated1
Sequence conflicti1533A → T in BAC54931 (PubMed:16702430).Curated1
Sequence conflicti1533A → T in BAF31266 (PubMed:16702430).Curated1
Sequence conflicti1536E → A in CAM25929 (PubMed:14574404).Curated1
Sequence conflicti1664T → S in BAE78617 (PubMed:16702430).Curated1
Sequence conflicti1668Q → R in CAH18685 (PubMed:17974005).Curated1
Sequence conflicti1734A → T in BAE78617 (PubMed:16702430).Curated1
Sequence conflicti1843E → K (PubMed:17974005).Curated1
Sequence conflicti2048H → R (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051160179R → C.Corresponds to variant rs28986464dbSNPEnsembl.1
Natural variantiVAR_022843251E → K.1 PublicationCorresponds to variant rs2517560dbSNPEnsembl.1
Natural variantiVAR_022844268R → K.2 PublicationsCorresponds to variant rs9262152dbSNPEnsembl.1
Natural variantiVAR_022845371E → K.1 PublicationCorresponds to variant rs2075015dbSNPEnsembl.1
Natural variantiVAR_051161386P → L.1 PublicationCorresponds to variant rs28986465dbSNPEnsembl.1
Natural variantiVAR_043922536I → M.2 PublicationsCorresponds to variant rs58344693dbSNPEnsembl.1
Natural variantiVAR_022846586S → A.1 PublicationCorresponds to variant rs2844707dbSNPEnsembl.1
Natural variantiVAR_051162917R → S.Corresponds to variant rs28986467dbSNPEnsembl.1
Natural variantiVAR_0511631100P → A.Corresponds to variant rs28994869dbSNPEnsembl.1
Natural variantiVAR_0511641112S → F.Corresponds to variant rs28987085dbSNPEnsembl.1
Natural variantiVAR_0511651180S → P.1 PublicationCorresponds to variant rs9461623dbSNPEnsembl.1
Natural variantiVAR_0228471509E → D.2 PublicationsCorresponds to variant rs3132589dbSNPEnsembl.1
Natural variantiVAR_0228481540S → P.Combined sources3 PublicationsCorresponds to variant rs3130645dbSNPEnsembl.1
Natural variantiVAR_0439231545Q → R.6 PublicationsCorresponds to variant rs17292678dbSNPEnsembl.1
Natural variantiVAR_0511661745P → R.Corresponds to variant rs28994871dbSNPEnsembl.1
Natural variantiVAR_0511671791V → E.Corresponds to variant rs28994873dbSNPEnsembl.1
Natural variantiVAR_0511681855D → E.Corresponds to variant rs28994874dbSNPEnsembl.1
Natural variantiVAR_0511691883R → Q.Corresponds to variant rs28994875dbSNPEnsembl.1
Natural variantiVAR_0511701904R → Q.Corresponds to variant rs28994876dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_014593741 – 1004Missing in isoform 2 and isoform 4. 1 PublicationAdd BLAST264
Alternative sequenceiVSP_0341031029 – 1787Missing in isoform 4. 1 PublicationAdd BLAST759
Alternative sequenceiVSP_0341041124 – 1410Missing in isoform 3. 1 PublicationAdd BLAST287

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34384.1. [Q14676-1]
RefSeqiNP_055456.2. NM_014641.2. [Q14676-1]
XP_005249551.1. XM_005249494.4. [Q14676-1]
XP_011513303.1. XM_011515001.2. [Q14676-1]
XP_011513305.1. XM_011515003.2. [Q14676-1]
XP_016867008.1. XM_017011519.1. [Q14676-1]
UniGeneiHs.653495.

Genome annotation databases

EnsembliENST00000376406; 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]
GeneIDi9656.
KEGGihsa:9656.
UCSCiuc003nrg.5. human. [Q14676-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34384.1. [Q14676-1]
RefSeqiNP_055456.2. NM_014641.2. [Q14676-1]
XP_005249551.1. XM_005249494.4. [Q14676-1]
XP_011513303.1. XM_011515001.2. [Q14676-1]
XP_011513305.1. XM_011515003.2. [Q14676-1]
XP_016867008.1. XM_017011519.1. [Q14676-1]
UniGeneiHs.653495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ14676.
SMRiQ14676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115014. 194 interactors.
DIPiDIP-33603N.
IntActiQ14676. 21 interactors.
MINTiMINT-259925.
STRINGi9606.ENSP00000365588.

PTM databases

iPTMnetiQ14676.
PhosphoSitePlusiQ14676.
SwissPalmiQ14676.

Polymorphism and mutation databases

BioMutaiMDC1.

Proteomic databases

EPDiQ14676.
MaxQBiQ14676.
PaxDbiQ14676.
PeptideAtlasiQ14676.
PRIDEiQ14676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376406; 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]
GeneIDi9656.
KEGGihsa:9656.
UCSCiuc003nrg.5. human. [Q14676-1]

Organism-specific databases

CTDi9656.
DisGeNETi9656.
GeneCardsiMDC1.
HGNCiHGNC:21163. MDC1.
HPAiHPA006915.
MIMi607593. gene.
neXtProtiNX_Q14676.
OpenTargetsiENSG00000137337.
ENSG00000224587.
ENSG00000225589.
ENSG00000228575.
ENSG00000234012.
ENSG00000237095.
PharmGKBiPA134942837.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2043. Eukaryota.
ENOG4111RPS. LUCA.
GeneTreeiENSGT00600000084454.
HOVERGENiHBG080567.
InParanoidiQ14676.
KOiK20780.
OMAiLSSEMEP.
OrthoDBiEOG091G0V3Z.
PhylomeDBiQ14676.
TreeFamiTF329580.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137337-MONOMER.
ZFISH:ENSG00000140406-MONOMER.
ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ14676.
SIGNORiQ14676.

Miscellaneous databases

ChiTaRSiMDC1. human.
EvolutionaryTraceiQ14676.
GeneWikiiMDC1.
GenomeRNAii9656.
PROiQ14676.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137337.
ExpressionAtlasiQ14676. baseline and differential.
GenevisibleiQ14676. HS.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF16770. RTT107_BRCT_5. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDC1_HUMAN
AccessioniPrimary (citable) accession number: Q14676
Secondary accession number(s): A2AB04
, A2BF04, A2RRA8, A7YY86, B0S8A2, Q0EFC2, Q2L6H7, Q2TAZ4, Q5JP55, Q5JP56, Q5ST83, Q68CQ3, Q86Z06, Q96QC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.