Reviewed, UniProtKB/Swiss-Prot Q14676 (MDC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Mediator of DNA damage checkpoint protein 1
Alternative name(s):
    Nuclear factor with BRCT domains 1

Gene names

Name:	MDC1
Synonyms:	KIAA0170, NFBD1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2089 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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/CHK1 and CHEK2/CHK2/CDS1 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	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/CHK2/CDS1, 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 G22P1/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. Interacts with CEP164. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.25 Ref.27 Ref.31
Subcellular location	Nucleus. Note: Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires 'Ser-139' phosphorylation of H2AFX. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18
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. Ref.10 Ref.13 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29
Sequence similarities	Contains 2 BRCT domains. Contains 1 FHA domain.
Sequence caution	The sequence CAH18685.1 differs from that shown. Reason: Erroneous termination at position 1804. Translated as Gln. The sequence CAI41890.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoskeleton Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay. Source: HPA nucleoplasm Ref.13 Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.15 Ref.24 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATM	Q13315	1	EBI-495644,EBI-495465
BRCA1	P38398	1	EBI-495644,EBI-349905
H2AFX	P16104	3	EBI-495644,EBI-494830
NBN	O60934	2	EBI-495644,EBI-494844
RNF8	O76064	5	EBI-495644,EBI-373337

Alternative products

This entry describes 5 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.

Isoform 5 (identifier: Q14676-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1311: Missing.
     1312-1336: SRTNMSSVKTPETVVPTAPELQIST → MWMMTAGLLEGQLRSIWKGLSLLAS

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2089

2089

Mediator of DNA damage checkpoint protein 1

PRO_0000096316

Regions

Domain

54 – 105

52

FHA

Domain

1892 – 1970

79

BRCT 1

Domain

1991 – 2082

92

BRCT 2

Region

1 – 150

150

Interaction with CHEK2

Region

2 – 220

219

Interaction with the MRN complex

Region

145 – 568

424

Required for nuclear localization (NLS1)

Region

1148 – 1610

463

Interaction with the PRKDC complex

Region

1698 – 2089

392

Required for nuclear localization (NLS2)

Compositional bias

1034 – 1469

436

Pro-rich

Amino acid modifications

Modified residue

168

1

Phosphoserine Ref.19 Ref.20 Ref.22 Ref.26 Ref.29

Modified residue

176

1

Phosphoserine Ref.29

Modified residue

299

1

Phosphoserine Ref.29

Modified residue

301

1

Phosphothreonine Ref.29

Modified residue

329

1

Phosphoserine Ref.19 Ref.20 Ref.29

Modified residue

331

1

Phosphothreonine Ref.20 Ref.29

Modified residue

341

1

Phosphothreonine Ref.29

Modified residue

372

1

Phosphoserine Ref.24

Modified residue

376

1

Phosphoserine Ref.24

Modified residue

378

1

Phosphothreonine Ref.24

Modified residue

394

1

Phosphoserine Ref.29

Modified residue

397

1

Phosphoserine Ref.29

Modified residue

402

1

Phosphoserine Ref.20 Ref.29

Modified residue

404

1

Phosphothreonine Ref.20 Ref.29

Modified residue

422

1

Phosphoserine Ref.24

Modified residue

449

1

Phosphothreonine Ref.29

Modified residue

453

1

Phosphoserine Ref.29

Modified residue

455

1

Phosphothreonine Ref.29

Modified residue

495

1

Phosphoserine Ref.20 Ref.29

Modified residue

498

1

Phosphoserine Ref.20 Ref.29

Modified residue

504

1

Phosphoserine Ref.29

Modified residue

513

1

Phosphoserine Ref.24 Ref.29

Modified residue

516

1

Phosphoserine Ref.24

Modified residue

523

1

Phosphothreonine Ref.24

Modified residue

652

1

Phosphothreonine Ref.24

Modified residue

659

1

Phosphothreonine Ref.24

Modified residue

763

1

Phosphoserine Ref.24

Modified residue

765

1

Phosphothreonine Ref.24

Modified residue

780

1

Phosphoserine Ref.24 Ref.29

Modified residue

793

1

Phosphoserine Ref.29

Modified residue

882

1

Phosphoserine Ref.20

Modified residue

955

1

Phosphoserine Ref.24

Modified residue

964

1

Phosphoserine Ref.19 Ref.24

Modified residue

986

1

Phosphoserine Ref.24

Modified residue

988

1

Phosphoserine Ref.19

Modified residue

995

1

Phosphoserine Ref.19

Modified residue

1033

1

Phosphoserine Ref.29

Modified residue

1068

1

Phosphoserine Ref.21 Ref.29

Modified residue

1086

1

Phosphoserine Ref.24

Modified residue

1095

1

Phosphoserine Ref.24

Modified residue

1198

1

Phosphothreonine Ref.29

Modified residue

1212

1

Phosphoserine Ref.29

Modified residue

1399

1

Phosphoserine Ref.28 Ref.29

Modified residue

1400

1

Phosphoserine Ref.29

Modified residue

1403

1

Phosphothreonine Ref.28 Ref.29

Modified residue

1425

1

Phosphothreonine Ref.19 Ref.28 Ref.29

Modified residue

1430

1

Phosphoserine Ref.24

Modified residue

1444

1

Phosphothreonine Ref.29

Modified residue

1461

1

Phosphothreonine Ref.19

Modified residue

1466

1

Phosphothreonine Ref.29

Modified residue

1589

1

Phosphothreonine Ref.29

Modified residue

1601

1

Phosphothreonine Ref.29

Modified residue

1604

1

Phosphoserine Ref.29

Modified residue

1608

1

Phosphothreonine Ref.29

Modified residue

1623

1

Phosphothreonine Ref.23

Modified residue

1630

1

Phosphothreonine Ref.29

Modified residue

1649

1

Phosphothreonine Ref.29

Modified residue

1664

1

Phosphothreonine Ref.29

Modified residue

1671

1

Phosphothreonine Ref.29

Modified residue

1681

1

Phosphoserine Ref.29

Modified residue

1696

1

Phosphothreonine Ref.29

Modified residue

1697

1

Phosphothreonine Ref.29

Modified residue

1702

1

Phosphoserine Ref.29

Modified residue

1711

1

Phosphoserine Ref.29

Modified residue

1775

1

Phosphoserine Ref.29

Modified residue

1797

1

Phosphoserine Ref.20 Ref.21

Modified residue

1814

1

Phosphoserine Ref.23

Modified residue

1820

1

Phosphoserine Ref.23

Modified residue

1858

1

Phosphothreonine Ref.29

Natural variations

Alternative sequence

1 – 1311

1311

Missing in isoform 5.

VSP_034102

Alternative sequence

741 – 1004

264

Missing in isoform 2 and isoform 4.

VSP_014593

Alternative sequence

1029 – 1787

759

Missing in isoform 4.

VSP_034103

Alternative sequence

1124 – 1410

287

Missing in isoform 3.

VSP_034104

Alternative sequence

1312 – 1336

25

SRTNM…LQIST → MWMMTAGLLEGQLRSIWKGL SLLAS in isoform 5.

VSP_034105

Natural variant

179

1

R → C: dbSNP rs28986464.

VAR_051160

Natural variant

251

1

E → K: dbSNP rs2517560. Ref.3

VAR_022843

Natural variant

268

1

R → K: dbSNP rs9262152. Ref.2 Ref.5

VAR_022844

Natural variant

371

1

E → K: dbSNP rs2075015. Ref.4

VAR_022845

Natural variant

386

1

P → L: dbSNP rs28986465. Ref.4

VAR_051161

Natural variant

536

1

I → M: dbSNP rs58344693. Ref.1 Ref.7

VAR_043922

Natural variant

586

1

S → A: dbSNP rs2844707. Ref.3

VAR_022846

Natural variant

917

1

R → S: dbSNP rs28986467.

VAR_051162

Natural variant

1100

1

P → A: dbSNP rs28994869.

VAR_051163

Natural variant

1112

1

S → F: dbSNP rs28987085.

VAR_051164

Natural variant

1180

1

S → P: dbSNP rs9461623. Ref.4

VAR_051165

Natural variant

1509

1

E → D: dbSNP rs3132589. Ref.3 Ref.4

VAR_022847

Natural variant

1540

1

S → P: dbSNP rs3130645. Ref.3 Ref.1 Ref.7

VAR_022848

Natural variant

1545

1

Q → R: dbSNP rs17292678. Ref.3 Ref.5 Ref.4 Ref.1 Ref.7 Ref.6

VAR_043923

Natural variant

1745

1

P → R: dbSNP rs28994871.

VAR_051166

Natural variant

1791

1

V → E: dbSNP rs28994873.

VAR_051167

Natural variant

1855

1

D → E: dbSNP rs28994874.

VAR_051168

Natural variant

1883

1

R → Q: dbSNP rs28994875.

VAR_051169

Natural variant

1904

1

R → Q: dbSNP rs28994876.

VAR_051170

Experimental info

Mutagenesis

58

1

R → A: Abrogates binding to the MRE11 complex and to CHEK2. Ref.13 Ref.14

Mutagenesis

72

1

S → A: Abrogates binding to CHEK2. Ref.14

Mutagenesis

96

1

N → A: Abrogates binding to CHEK2; when associated with A-97 and A-98. Ref.14

Mutagenesis

97

1

G → A: Abrogates binding to CHEK2; when associated with A-96 and A-98. Ref.14

Mutagenesis

98

1

T → A: Abrogates binding to CHEK2; when associated with A-96 and A-97. Ref.14

Sequence conflict

638

1

L → P in CAH18685. Ref.2

Sequence conflict

645 – 1326

682

Missing in CAH18685. Ref.2

Sequence conflict

1005

1

G → GS in BAB63322. Ref.3

Sequence conflict

1041

1

T → A in BAA11487. Ref.1

Sequence conflict

1041

1

T → A in AAI52557. Ref.7

Sequence conflict

1266

1

Y → S in BAE78617. Ref.4

Sequence conflict

1283

1

P → T in BAE78617. Ref.4

Sequence conflict

1533

1

A → T in BAC54931. Ref.4

Sequence conflict

1533

1

A → T in BAF31266. Ref.4

Sequence conflict

1536

1

E → A in CAM25929. Ref.5

Sequence conflict

1664

1

T → S in BAE78617. Ref.4

Sequence conflict

1668

1

Q → R in CAH18685. Ref.2

Sequence conflict

1734

1

A → T in BAE78617. Ref.4

Sequence conflict

1843

1

E → K Ref.2

Sequence conflict

2048

1

H → R Ref.2

Secondary structure

1

.

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2089

Helix Strand Turn

Details...

Beta strand

1894 – 1897

4

Helix

1903 – 1911

9

Turn

1920 – 1922

3

Beta strand

1924 – 1927

4

Helix

1935 – 1943

9

Helix

1951 – 1959

9

Helix

1966 – 1968

3

Helix

1973 – 1979

7

Helix

1983 – 1992

10

Turn

1995 – 1998

4

Beta strand

2000 – 2003

4

Helix

2011 – 2020

10

Beta strand

2037 – 2040

4

Helix

2043 – 2048

6

Helix

2050 – 2055

6

Helix

2062 – 2071

10

Helix

2076 – 2078

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 3. Checksum: A8B880A25617EC96	FASTA	2,089	226,666
	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
	Isoform 2. Checksum: A8837EC5FB7EC360	FASTA	1,825	197,598
	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 GLLNCKMPPA EKASRIRAAE KVSRGDQESP DACLPPTVPE 790 800 810 820 830 840 APAPPQKPLN SQSQKHLAPP PLLSPLLPSI KPTVRKTRQD GSQEAPEAPL SSELEPFHPK 850 860 870 880 890 900 PKIRTRKSSR MTPFPATSAA PEPHPSTSTA QPVTPKPTSQ ATRSRTNRSS VKTPEPVVPT 910 920 930 940 950 960 APELQPSTST DQPVTSEPTS QVTRGRKSRS SVKTPETVVP TALELQPSTS TDRPVTSEPT 970 980 990 1000 1010 1020 SQATRGRKNR SSVKTPEPVV PTAPELQPST STDQPVTSEP TYQATRGRKN RSSVKTPEPV 1030 1040 1050 1060 1070 1080 VPTAPELRPS TSTDRPVTPK PTSRTTRSRT NMSSVKTPET VVPTAPELQI STSTDQPVTP 1090 1100 1110 1120 1130 1140 KPTSRTTRSR TNMSSVKNPE STVPIAPELP PSTSTEQPVT PEPTSRATRG RKNRSSGKTP 1150 1160 1170 1180 1190 1200 ETLVPTAPKL EPSTSTDQPV TPEPTSQATR GRTNRSSVKT PETVVPTAPE LQPSTSTDQP 1210 1220 1230 1240 1250 1260 VTPEPTSQAT RGRTDRSSVK TPETVVPTAP ELQASASTDQ PVTSEPTSRT TRGRKNRSSV 1270 1280 1290 1300 1310 1320 KTPETVVPAA PELQPSTSTD QPVTPEPTSR ATRGRTNRSS VKTPESIVPI APELQPSTSR 1330 1340 1350 1360 1370 1380 NQLVTPEPTS RATRCRTNRS SVKTPEPVVP TAPEPHPTTS TDQPVTPKLT SRATRRKTNR 1390 1400 1410 1420 1430 1440 SSVKTPKPVE PAASDLEPFT PTDQSVTPEA IAQGGQSKTL RSSTVRAMPV PTTPEFQSPV 1450 1460 1470 1480 1490 1500 TTDQPISPEP ITQPSCIKRQ RAAGNPGSLA APIDHKPCSA PLEPKSQASR NQRWGAVRAA 1510 1520 1530 1540 1550 1560 ESLTAIPEPA SPQLLETPIH ASQIQKVEPA GRSRFTPELQ PKASQSRKRS LATMDSPPHQ 1570 1580 1590 1600 1610 1620 KQPQRGEVSQ KTVIIKEEEE DTAEKPGKEE DVVTPKPGKR KRDQAEEEPN RIPSRSLRRT 1630 1640 1650 1660 1670 1680 KLNQESTAPK VLFTGVVDAR GERAVLALGG SLAGSAAEAS HLVTDRIRRT VKFLCALGRG 1690 1700 1710 1720 1730 1740 IPILSLDWLH QSRKAGFFLP PDEYVVTDPE QEKNFGFSLQ DALSRARERR LLEGYEIYVT 1750 1760 1770 1780 1790 1800 PGVQPPPPQM GEIISCCGGT YLPSMPRSYK PQRVVITCPQ DFPHCSIPLR VGLPLLSPEF 1810 1820 LLTGVLKQEA KPEAFVLSPL EMSST
	Isoform 3. Checksum: FF7FB09BDF3E6178	FASTA	1,802	195,986
	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 TSAAPKLEPS TSTDQPVTPE 1150 1160 1170 1180 1190 1200 PTSQATRGRT NRSSVKTPET VVPTAPELQP STSTDQPVTP EPTSQATRGR TDRSSVKTPE 1210 1220 1230 1240 1250 1260 TVVPTAPELQ ASASTDQPVT SEPTSRTTRG RKNRSSVKTP ETVVPAAPEL QPSTSTDQPV 1270 1280 1290 1300 1310 1320 TPEPTSRATR GRTNRSSVKT PESIVPIAPE LQPSTSRNQL VTPEPTSRAT RCRTNRSSVK 1330 1340 1350 1360 1370 1380 TPEPVVPTAP EPHPTTSTDQ PVTPKLTSRA TRRKTNRSSV KTPKPVEPAA SDLEPFTPTD 1390 1400 1410 1420 1430 1440 QSVTPEAIAQ GGQSKTLRSS TVRAMPVPTT PEFQSPVTTD QPISPEPITQ PSCIKRQRAA 1450 1460 1470 1480 1490 1500 GNPGSLAAPI DHKPCSAPLE PKSQASRNQR WGAVRAAESL TAIPEPASPQ LLETPIHASQ 1510 1520 1530 1540 1550 1560 IQKVEPAGRS RFTPELQPKA SQSRKRSLAT MDSPPHQKQP QRGEVSQKTV IIKEEEEDTA 1570 1580 1590 1600 1610 1620 EKPGKEEDVV TPKPGKRKRD QAEEEPNRIP SRSLRRTKLN QESTAPKVLF TGVVDARGER 1630 1640 1650 1660 1670 1680 AVLALGGSLA GSAAEASHLV TDRIRRTVKF LCALGRGIPI LSLDWLHQSR KAGFFLPPDE 1690 1700 1710 1720 1730 1740 YVVTDPEQEK NFGFSLQDAL SRARERRLLE GYEIYVTPGV QPPPPQMGEI ISCCGGTYLP 1750 1760 1770 1780 1790 1800 SMPRSYKPQR VVITCPQDFP HCSIPLRVGL PLLSPEFLLT GVLKQEAKPE AFVLSPLEMS ST
	Isoform 4. Checksum: F3816B14D9E11884	FASTA	1,066	116,634
	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 GLLNCKMPPA EKASRIRAAE KVSRIQKVEP AGRSRFTPEL 790 800 810 820 830 840 QPKASQSRKR SLATMDSPPH QKQPQRGEVS QKTVIIKEEE EDTAEKPGKE EDVVTPKPGK 850 860 870 880 890 900 RKRDQAEEEP NRIPSRSLRR TKLNQESTAP KVLFTGVVDA RGERAVLALG GSLAGSAAEA 910 920 930 940 950 960 SHLVTDRIRR TVKFLCALGR GIPILSLDWL HQSRKAGFFL PPDEYVVTDP EQEKNFGFSL 970 980 990 1000 1010 1020 QDALSRARER RLLEGYEIYV TPGVQPPPPQ MGEIISCCGG TYLPSMPRSY KPQRVVITCP 1030 1040 1050 1060 QDFPHCSIPL RVGLPLLSPE FLLTGVLKQE AKPEAFVLSP LEMSST
	Isoform 5. Checksum: 80E6864EA360A2CC	FASTA	778	84,296
	10 20 30 40 50 60 MWMMTAGLLE GQLRSIWKGL SLLASSTDQP VTPKPTSRTT RSRTNMSSVK NPESTVPIAP 70 80 90 100 110 120 ELPPSTSTEQ PVTPEPTSRA TRGRKNRSSG KTPETLVPTA PKLEPSTSTD QPVTPEPTSQ 130 140 150 160 170 180 ATRGRTNRSS VKTPETVVPT APELQPSTST DQPVTPEPTS QATRGRTDRS SVKTPETVVP 190 200 210 220 230 240 TAPELQASAS TDQPVTSEPT SRTTRGRKNR SSVKTPETVV PAAPELQPST STDQPVTPEP 250 260 270 280 290 300 TSRATRGRTN RSSVKTPESI VPIAPELQPS TSRNQLVTPE PTSRATRCRT NRSSVKTPEP 310 320 330 340 350 360 VVPTAPEPHP TTSTDQPVTP KLTSRATRRK TNRSSVKTPK PVEPAASDLE PFTPTDQSVT 370 380 390 400 410 420 PEAIAQGGQS KTLRSSTVRA MPVPTTPEFQ SPVTTDQPIS PEPITQPSCI KRQRAAGNPG 430 440 450 460 470 480 SLAAPIDHKP CSAPLEPKSQ ASRNQRWGAV RAAESLTAIP EPASPQLLET PIHASQIQKV 490 500 510 520 530 540 EPAGRSRFTP ELQPKASQSR KRSLATMDSP PHQKQPQRGE VSQKTVIIKE EEEDTAEKPG 550 560 570 580 590 600 KEEDVVTPKP GKRKRDQAEE EPNRIPSRSL RRTKLNQEST APKVLFTGVV DARGERAVLA 610 620 630 640 650 660 LGGSLAGSAA EASHLVTDRI RRTVKFLCAL GRGIPILSLD WLHQSRKAGF FLPPDEYVVT 670 680 690 700 710 720 DPEQEKNFGF SLQDALSRAR ERRLLEGYEI YVTPGVQPPP PQMGEIISCC GGTYLPSMPR 730 740 750 760 770 SYKPQRVVIT CPQDFPHCSI PLRVGLPLLS PEFLLTGVLK QEAKPEAFVL SPLEMSST

References

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[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: 8724849] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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. , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S. Genetics 173:1555-1570(2006) [PubMed: 16702430] [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: 14574404] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), 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: 14695167] [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: 12475977] [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: 12499369] [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: 12551934] [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: 12611903] [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: 12607003] [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: 12607004] [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: 12607005] [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: 15279781] [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: 15201865] [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: 15377652] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PRKDC COMPLEX.
[19]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-329; SER-964; SER-988; SER-995; THR-1425 AND THR-1461, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-329; THR-331; SER-402; THR-404; SER-495; SER-498; SER-882 AND SER-1797, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068 AND SER-1797, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY.
[23]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1623; SER-1814 AND SER-1820, MASS SPECTROMETRY.
[24]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-376; THR-378; SER-422; SER-513; SER-516; THR-523; THR-652; THR-659; SER-763; THR-765; SER-780; SER-955; SER-964; SER-986; SER-1086; SER-1095 AND SER-1430, MASS SPECTROMETRY.
[25]	"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: 18006705] [Abstract] Cited for: INTERACTION WITH RNF8.
[26]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY.
[27]	"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: 18283122] [Abstract] Cited for: INTERACTION WITH CEP164.
[28]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1399; THR-1403 AND THR-1425, MASS SPECTROMETRY.
[29]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-176; SER-299; THR-301; SER-329; THR-331; THR-341; SER-394; SER-397; SER-402; THR-404; THR-449; SER-453; THR-455; SER-495; SER-498; SER-504; SER-513; SER-780; SER-793; SER-1033; SER-1068; THR-1198; SER-1212; SER-1399; SER-1400; THR-1403; THR-1425; THR-1444; THR-1466; THR-1589; THR-1601; SER-1604; THR-1608; THR-1630; THR-1649; THR-1664; THR-1671; SER-1681; THR-1696; THR-1697; SER-1702; SER-1711; SER-1775 AND THR-1858, MASS SPECTROMETRY.
[30]	"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: 16377563] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1883-2089 IN COMPLEX WITH PHOSPHORYLATED H2AFX.
[31]	"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: 16049003] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1891-2086, INTERACTION WITH PHOSPHORYLATED H2AFX.
[32]	"Crystal structure of MDC1 tandem BRCT domains." Wasielewski E., Kim Y., Joachimiak A., Thompson J.R., Mer G. Submitted (NOV-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1884-2089.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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: CAI41890.1. Sequence problems.
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.
BC131491 mRNA. Translation: AAI31492.1.
BC152556 mRNA. Translation: AAI52557.1.

IPI

IPI00470805.
IPI00552897.
IPI00895837.
IPI00895842.
IPI00895860.

RefSeq

NP_055456.2.

UniGene

Hs.653495

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14676. 11 interactions.

PTM databases

PhosphoSite

Q14676.

Proteomic databases

PRIDE

Q14676.

Genome annotation databases

Ensembl

ENSG00000137337. Homo sapiens. [Contig view]
ENSG00000206385. Homo sapiens. [Contig view]

GeneID

9656.

KEGG

hsa:9656.

Organism-specific databases

GeneCards

GC06M030775.

HGNC

HGNC:21163. MDC1.

HPA

HPA006915.

MIM

607593. gene.

PharmGKB

PA134959259.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q14676.

OMA

Q14676. TSRATRG.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q14676.

Bgee

Q14676.

GermOnline

ENSG00000137337. Homo sapiens.

Family and domain databases

InterPro

IPR001357. BRCT.
IPR000253. FHA.
[Graphical view]

Gene3D

G3DSA:2.60.200.20. FHA. 1 hit.

Pfam

PF00533. BRCT. 2 hits.
PF00498. FHA. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 2 hits.
SM00240. FHA. 1 hit.
[Graphical view]

PROSITE

PS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

36251.

SOURCE

Search...

Entry information

Entry name

MDC1_HUMAN

Accession

Primary (citable) accession number: Q14676
Secondary accession number(s): A2AB04 , 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:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)