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UniProtKB - 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: 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
Complete GO annotation...

GO - Biological processi

  • double-strand break repair via nonhomologous end joining Source: Reactome
  • intra-S DNA damage checkpoint Source: UniProtKB
Complete GO annotation...

Keywordsi

Biological processCell cycle, DNA damage, DNA repair

Enzyme and pathway databases

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21163. MDC1.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • focal adhesion Source: HPA
  • nuclear body 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.
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 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

Show more details

GO - Molecular functioni

  • FHA domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
Complete GO annotation...

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

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di3.40.50.10190. 2 hits.
InterProiView protein in InterPro
IPR001357. BRCT_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
PfamiView protein in Pfam
PF00498. FHA. 1 hit.
PF16770. RTT107_BRCT_5. 1 hit.
SMARTiView protein in SMART
SM00240. FHA. 1 hit.
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiView protein in PROSITE
PS50172. BRCT. 1 hit.
PS50006. FHA_DOMAIN. 1 hit.

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 dbSNP:rs28986464Ensembl.1
Natural variantiVAR_022843251E → K1 PublicationCorresponds to variant dbSNP:rs2517560Ensembl.1
Natural variantiVAR_022844268R → K2 PublicationsCorresponds to variant dbSNP:rs9262152Ensembl.1
Natural variantiVAR_022845371E → K1 PublicationCorresponds to variant dbSNP:rs2075015Ensembl.1
Natural variantiVAR_051161386P → L1 PublicationCorresponds to variant dbSNP:rs28986465Ensembl.1
Natural variantiVAR_043922536I → M2 PublicationsCorresponds to variant dbSNP:rs58344693Ensembl.1
Natural variantiVAR_022846586S → A1 PublicationCorresponds to variant dbSNP:rs2844707Ensembl.1
Natural variantiVAR_051162917R → S. Corresponds to variant dbSNP:rs28986467Ensembl.1
Natural variantiVAR_0511631100P → A. Corresponds to variant dbSNP:rs28994869Ensembl.1
Natural variantiVAR_0511641112S → F. Corresponds to variant dbSNP:rs28987085Ensembl.1
Natural variantiVAR_0511651180S → P1 PublicationCorresponds to variant dbSNP:rs9461623Ensembl.1
Natural variantiVAR_0228471509E → D2 PublicationsCorresponds to variant dbSNP:rs3132589Ensembl.1
Natural variantiVAR_0228481540S → PCombined sources3 PublicationsCorresponds to variant dbSNP:rs3130645Ensembl.1
Natural variantiVAR_0439231545Q → R6 PublicationsCorresponds to variant dbSNP:rs17292678Ensembl.1
Natural variantiVAR_0511661745P → R. Corresponds to variant dbSNP:rs28994871Ensembl.1
Natural variantiVAR_0511671791V → E. Corresponds to variant dbSNP:rs28994873Ensembl.1
Natural variantiVAR_0511681855D → E. Corresponds to variant dbSNP:rs28994874Ensembl.1
Natural variantiVAR_0511691883R → Q. Corresponds to variant dbSNP:rs28994875Ensembl.1
Natural variantiVAR_0511701904R → Q. Corresponds to variant dbSNP:rs28994876Ensembl.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

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.

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 historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: June 7, 2017
This is version 175 of the entry and version 3 of the sequence. See 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