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Q14676

- MDC1_HUMAN

UniProt

Q14676 - MDC1_HUMAN

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Protein

Mediator of DNA damage checkpoint protein 1

Gene

MDC1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. FHA domain binding Source: UniProtKB
  2. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: Reactome
  2. double-strand break repair Source: Reactome
  3. double-strand break repair via homologous recombination Source: Reactome
  4. intra-S DNA damage checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_1924. ATM mediated phosphorylation of repair proteins.
REACT_97. Recruitment of repair and signaling proteins to double-strand breaks.
SignaLinkiQ14676.

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
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:21163. MDC1.

Subcellular locationi

Nucleus 11 Publications. 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.

GO - Cellular componenti

  1. chromosome Source: UniProtKB
  2. focal adhesion Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581R → A: Abrogates binding to the MRE11 complex and to CHEK2. 2 Publications
Mutagenesisi72 – 721S → A: Abrogates binding to CHEK2. 1 Publication
Mutagenesisi96 – 961N → A: Abrogates binding to CHEK2; when associated with A-97 and A-98. 1 Publication
Mutagenesisi97 – 971G → A: Abrogates binding to CHEK2; when associated with A-96 and A-98. 1 Publication
Mutagenesisi98 – 981T → A: Abrogates binding to CHEK2; when associated with A-96 and A-97. 1 Publication
Mutagenesisi1840 – 18401K → R: Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination. 1 Publication

Organism-specific databases

PharmGKBiPA134942837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20892089Mediator of DNA damage checkpoint protein 1PRO_0000096316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphothreonine; by ATM1 Publication
Modified residuei108 – 1081Phosphoserine1 Publication
Modified residuei168 – 1681Phosphoserine4 Publications
Modified residuei299 – 2991Phosphoserine2 Publications
Modified residuei301 – 3011Phosphothreonine2 Publications
Modified residuei329 – 3291Phosphoserine3 Publications
Modified residuei331 – 3311Phosphothreonine2 Publications
Modified residuei372 – 3721Phosphoserine2 Publications
Modified residuei376 – 3761Phosphoserine2 Publications
Modified residuei378 – 3781Phosphothreonine2 Publications
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei397 – 3971Phosphoserine1 Publication
Modified residuei402 – 4021Phosphoserine4 Publications
Modified residuei404 – 4041Phosphothreonine4 Publications
Modified residuei411 – 4111Phosphoserine1 Publication
Modified residuei449 – 4491Phosphothreonine2 Publications
Modified residuei453 – 4531Phosphoserine2 Publications
Modified residuei455 – 4551Phosphothreonine3 Publications
Modified residuei485 – 4851Phosphoserine1 Publication
Modified residuei495 – 4951Phosphoserine2 Publications
Modified residuei498 – 4981Phosphoserine2 Publications
Modified residuei513 – 5131Phosphoserine3 Publications
Modified residuei523 – 5231Phosphothreonine1 Publication
Modified residuei780 – 7801Phosphoserine2 Publications
Modified residuei793 – 7931Phosphoserine1 Publication
Modified residuei812 – 8121N6-acetyllysine1 Publication
Modified residuei955 – 9551Phosphoserine1 Publication
Modified residuei1033 – 10331Phosphoserine1 Publication
Modified residuei1068 – 10681Phosphoserine2 Publications
Modified residuei1157 – 11571Phosphothreonine1 Publication
Modified residuei1198 – 11981Phosphothreonine1 Publication
Modified residuei1399 – 13991Phosphoserine2 Publications
Modified residuei1400 – 14001Phosphoserine1 Publication
Modified residuei1402 – 14021N6-acetyllysine1 Publication
Modified residuei1403 – 14031Phosphothreonine3 Publications
Modified residuei1425 – 14251Phosphothreonine3 Publications
Modified residuei1466 – 14661Phosphothreonine2 Publications
Modified residuei1548 – 15481Phosphothreonine1 Publication
Modified residuei1567 – 15671Phosphothreonine1 Publication
Modified residuei1589 – 15891Phosphothreonine2 Publications
Modified residuei1604 – 16041Phosphoserine1 Publication
Modified residuei1630 – 16301Phosphothreonine1 Publication
Modified residuei1664 – 16641Phosphothreonine1 Publication
Modified residuei1671 – 16711Phosphothreonine1 Publication
Modified residuei1681 – 16811Phosphoserine1 Publication
Modified residuei1697 – 16971Phosphothreonine1 Publication
Modified residuei1702 – 17021Phosphoserine1 Publication
Modified residuei1711 – 17111Phosphoserine1 Publication
Modified residuei1775 – 17751Phosphoserine2 Publications
Modified residuei1800 – 18001Phosphothreonine1 Publication
Modified residuei1820 – 18201Phosphoserine2 Publications
Cross-linki1840 – 1840Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residuei1858 – 18581Phosphothreonine1 Publication

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.12 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, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14676.
PaxDbiQ14676.
PRIDEiQ14676.

PTM databases

PhosphoSiteiQ14676.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiQ14676.
ExpressionAtlasiQ14676. baseline and differential.
GenevestigatoriQ14676.

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

Protein-protein interaction databases

BioGridi115014. 180 interactions.
DIPiDIP-33603N.
IntActiQ14676. 15 interactions.
MINTiMINT-259925.

Structurei

Secondary structure

1
2089
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 244Combined sources
Beta strandi32 – 365Combined sources
Beta strandi39 – 424Combined sources
Beta strandi45 – 495Combined sources
Beta strandi51 – 599Combined sources
Beta strandi62 – 654Combined sources
Beta strandi76 – 805Combined sources
Beta strandi88 – 914Combined sources
Beta strandi98 – 1003Combined sources
Turni101 – 1044Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi126 – 1327Combined sources
Beta strandi1894 – 18974Combined sources
Helixi1903 – 19119Combined sources
Turni1920 – 19223Combined sources
Beta strandi1924 – 19274Combined sources
Helixi1935 – 19439Combined sources
Helixi1951 – 19599Combined sources
Helixi1966 – 19683Combined sources
Helixi1973 – 19786Combined sources
Helixi1983 – 199210Combined sources
Turni1995 – 19984Combined sources
Beta strandi2000 – 20034Combined sources
Helixi2011 – 202010Combined sources
Beta strandi2024 – 20263Combined sources
Beta strandi2037 – 20404Combined sources
Helixi2043 – 20486Combined sources
Helixi2050 – 20556Combined sources
Helixi2063 – 20719Combined sources
Helixi2076 – 20794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 29-133, 1891-2085.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 10552FHAPROSITE-ProRule annotationAdd
BLAST
Domaini1892 – 197079BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini1991 – 208292BRCT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 150150Interaction with CHEK2Add
BLAST
Regioni2 – 220219Interaction with the MRN complexAdd
BLAST
Regioni145 – 568424Required for nuclear localization (NLS1)Add
BLAST
Regioni1148 – 1610463Interaction with the PRKDC complexAdd
BLAST
Regioni1698 – 2089392Required for nuclear localization (NLS2)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1034 – 1469436Pro-richAdd
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00600000084454.
HOVERGENiHBG080567.
InParanoidiQ14676.
OMAiVIEILAW.
PhylomeDBiQ14676.
TreeFamiTF329580.

Family and domain databases

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.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
SM00240. 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. Align

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 BAA11487.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH18685.1 differs from that shown. Reason: Erroneous termination at position 1804. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti638 – 6381L → P in CAH18685. (PubMed:17974005)Curated
Sequence conflicti645 – 1326682Missing in CAH18685. (PubMed:17974005)CuratedAdd
BLAST
Sequence conflicti1005 – 10051G → GS in BAB63322. 1 PublicationCurated
Sequence conflicti1041 – 10411T → A in BAA11487. (PubMed:8724849)Curated
Sequence conflicti1041 – 10411T → A in AAI52557. (PubMed:15489334)Curated
Sequence conflicti1266 – 12661Y → S in BAE78617. (PubMed:16702430)Curated
Sequence conflicti1283 – 12831P → T in BAE78617. (PubMed:16702430)Curated
Sequence conflicti1533 – 15331A → T in BAC54931. (PubMed:16702430)Curated
Sequence conflicti1533 – 15331A → T in BAF31266. (PubMed:16702430)Curated
Sequence conflicti1536 – 15361E → A in CAM25929. (PubMed:14574404)Curated
Sequence conflicti1664 – 16641T → S in BAE78617. (PubMed:16702430)Curated
Sequence conflicti1668 – 16681Q → R in CAH18685. (PubMed:17974005)Curated
Sequence conflicti1734 – 17341A → T in BAE78617. (PubMed:16702430)Curated
Sequence conflicti1843 – 18431E → K(PubMed:17974005)Curated
Sequence conflicti2048 – 20481H → R(PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791R → C.
Corresponds to variant rs28986464 [ dbSNP | Ensembl ].
VAR_051160
Natural varianti251 – 2511E → K.1 Publication
Corresponds to variant rs2517560 [ dbSNP | Ensembl ].
VAR_022843
Natural varianti268 – 2681R → K.2 Publications
Corresponds to variant rs9262152 [ dbSNP | Ensembl ].
VAR_022844
Natural varianti371 – 3711E → K.1 Publication
Corresponds to variant rs2075015 [ dbSNP | Ensembl ].
VAR_022845
Natural varianti386 – 3861P → L.1 Publication
Corresponds to variant rs28986465 [ dbSNP | Ensembl ].
VAR_051161
Natural varianti536 – 5361I → M.2 Publications
Corresponds to variant rs58344693 [ dbSNP | Ensembl ].
VAR_043922
Natural varianti586 – 5861S → A.1 Publication
Corresponds to variant rs2844707 [ dbSNP | Ensembl ].
VAR_022846
Natural varianti917 – 9171R → S.
Corresponds to variant rs28986467 [ dbSNP | Ensembl ].
VAR_051162
Natural varianti1100 – 11001P → A.
Corresponds to variant rs28994869 [ dbSNP | Ensembl ].
VAR_051163
Natural varianti1112 – 11121S → F.
Corresponds to variant rs28987085 [ dbSNP | Ensembl ].
VAR_051164
Natural varianti1180 – 11801S → P.1 Publication
Corresponds to variant rs9461623 [ dbSNP | Ensembl ].
VAR_051165
Natural varianti1509 – 15091E → D.2 Publications
Corresponds to variant rs3132589 [ dbSNP | Ensembl ].
VAR_022847
Natural varianti1540 – 15401S → P.4 Publications
Corresponds to variant rs3130645 [ dbSNP | Ensembl ].
VAR_022848
Natural varianti1545 – 15451Q → R.6 Publications
Corresponds to variant rs17292678 [ dbSNP | Ensembl ].
VAR_043923
Natural varianti1745 – 17451P → R.
Corresponds to variant rs28994871 [ dbSNP | Ensembl ].
VAR_051166
Natural varianti1791 – 17911V → E.
Corresponds to variant rs28994873 [ dbSNP | Ensembl ].
VAR_051167
Natural varianti1855 – 18551D → E.
Corresponds to variant rs28994874 [ dbSNP | Ensembl ].
VAR_051168
Natural varianti1883 – 18831R → Q.
Corresponds to variant rs28994875 [ dbSNP | Ensembl ].
VAR_051169
Natural varianti1904 – 19041R → Q.
Corresponds to variant rs28994876 [ dbSNP | Ensembl ].
VAR_051170

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei741 – 1004264Missing in isoform 2 and isoform 4. 1 PublicationVSP_014593Add
BLAST
Alternative sequencei1029 – 1787759Missing in isoform 4. 1 PublicationVSP_034103Add
BLAST
Alternative sequencei1124 – 1410287Missing in isoform 3. 1 PublicationVSP_034104Add
BLAST

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_005249494.2. [Q14676-1]
XP_005272968.1. XM_005272911.2. [Q14676-1]
XP_005274958.1. XM_005274901.2. [Q14676-1]
XP_005275124.1. XM_005275067.2. [Q14676-1]
XP_005275253.1. XM_005275196.2. [Q14676-1]
XP_005275257.1. XM_005275200.1. [Q14676-2]
XP_005275380.1. XM_005275323.2. [Q14676-1]
XP_006725919.1. XM_006725856.1. [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.
UCSCiuc003nrf.4. human. [Q14676-4]
uc003nrg.4. human. [Q14676-1]
uc011dmp.1. human. [Q14676-2]

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 .
CCDSi CCDS34384.1. [Q14676-1 ]
RefSeqi NP_055456.2. NM_014641.2. [Q14676-1 ]
XP_005249551.1. XM_005249494.2. [Q14676-1 ]
XP_005272968.1. XM_005272911.2. [Q14676-1 ]
XP_005274958.1. XM_005274901.2. [Q14676-1 ]
XP_005275124.1. XM_005275067.2. [Q14676-1 ]
XP_005275253.1. XM_005275196.2. [Q14676-1 ]
XP_005275257.1. XM_005275200.1. [Q14676-2 ]
XP_005275380.1. XM_005275323.2. [Q14676-1 ]
XP_006725919.1. XM_006725856.1. [Q14676-1 ]
UniGenei Hs.653495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ADO X-ray 1.45 A/B 1891-2086 [» ]
2AZM X-ray 2.41 A/B 1883-2089 [» ]
2ETX X-ray 1.33 A/B 1884-2089 [» ]
3K05 X-ray 1.33 A/B 1891-2089 [» ]
3UEO X-ray 2.60 E/F 325-336 [» ]
3UMZ X-ray 1.65 A/B 27-138 [» ]
3UN0 X-ray 2.30 A/B 26-138 [» ]
3UNM X-ray 1.80 A/B 27-138 [» ]
3UNN X-ray 1.70 A 27-138 [» ]
B 1-8 [» ]
3UOT X-ray 1.80 A/B 19-138 [» ]
D/E 1-10 [» ]
ProteinModelPortali Q14676.
SMRi Q14676. Positions 29-133, 1891-2085.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115014. 180 interactions.
DIPi DIP-33603N.
IntActi Q14676. 15 interactions.
MINTi MINT-259925.

PTM databases

PhosphoSitei Q14676.

Proteomic databases

MaxQBi Q14676.
PaxDbi Q14676.
PRIDEi Q14676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli 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 ]
GeneIDi 9656.
KEGGi hsa:9656.
UCSCi uc003nrf.4. human. [Q14676-4 ]
uc003nrg.4. human. [Q14676-1 ]
uc011dmp.1. human. [Q14676-2 ]

Organism-specific databases

CTDi 9656.
GeneCardsi GC06M030667.
GC06Mi30675.
GC06Mj30657.
GC06Mk30657.
GC06Ml30712.
GC06Mm30746.
GC06Mn30657.
GC06Mo30659.
HGNCi HGNC:21163. MDC1.
HPAi HPA006915.
MIMi 607593. gene.
neXtProti NX_Q14676.
PharmGKBi PA134942837.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00600000084454.
HOVERGENi HBG080567.
InParanoidi Q14676.
OMAi VIEILAW.
PhylomeDBi Q14676.
TreeFami TF329580.

Enzyme and pathway databases

Reactomei REACT_1924. ATM mediated phosphorylation of repair proteins.
REACT_97. Recruitment of repair and signaling proteins to double-strand breaks.
SignaLinki Q14676.

Miscellaneous databases

ChiTaRSi MDC1. human.
EvolutionaryTracei Q14676.
GeneWikii MDC1.
GenomeRNAii 9656.
NextBioi 36251.
PROi Q14676.
SOURCEi Search...

Gene expression databases

Bgeei Q14676.
ExpressionAtlasi Q14676. baseline and differential.
Genevestigatori Q14676.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
Pfami PF00498. FHA. 1 hit.
[Graphical view ]
SMARTi SM00292. BRCT. 2 hits.
SM00240. FHA. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. 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. 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. 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.

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 26, 2014
This is version 148 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

External Data

Dasty 3