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Q96T76 (MMS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MMS19 nucleotide excision repair protein homolog

Short name=hMMS19
Alternative name(s):
MET18 homolog
MMS19-like protein
Gene names
Name:MMS19
Synonyms:MMS19L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1030 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. Ref.1 Ref.3 Ref.11 Ref.14 Ref.15

Subunit structure

Component of the CIA complex. Component of the MMXD complex, composed of CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with FAM96B; the interaction is direct. Interacts with ERCC2/XPD; the interaction is direct. Interacts with ERCC3/XPB and NCOA3/RAC3. Interacts with RTEL1; the interaction mediates the association of RTEL1 with the CIA complex. Ref.1 Ref.2 Ref.11 Ref.14 Ref.15

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle Ref.1 Ref.2 Ref.3 Ref.11 Ref.15.

Tissue specificity

Ubiquitously expressed with higher expression in testis. Ref.1 Ref.3

Sequence similarities

Belongs to the MET18/MMS19 family.

Contains 7 HEAT repeats.

Sequence caution

The sequence AAH80532.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAB55315.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB71223.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAG51657.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC29239.1 differs from that shown. Reason: Frameshift at positions 373 and 412.

Ontologies

Keywords
   Biological processChromosome partition
DNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

DNA repair

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.14. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

iron-sulfur cluster assembly

Inferred from mutant phenotype Ref.15Ref.14. Source: UniProtKB

nucleotide-excision repair

Non-traceable author statement Ref.2. Source: UniProtKB

phosphorelay signal transduction system

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.2. Source: UniProtKB

response to hormone

Non-traceable author statement Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentCIA complex

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

MMXD complex

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.11Ref.15. Source: UniProtKB

holo TFIIH complex

Non-traceable author statement Ref.2. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

spindle

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionestrogen receptor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

protein binding, bridging

Non-traceable author statement Ref.2. Source: UniProtKB

receptor signaling complex scaffold activity

Non-traceable author statement Ref.2. Source: UniProtKB

transcription coactivator activity

Inferred from mutant phenotype Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96T76-1)

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: Q96T76-7)

The sequence of this isoform differs from the canonical sequence as follows:
     309-318: VFQTASERVE → TAGTTCVNRT
     319-1030: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q96T76-6)

The sequence of this isoform differs from the canonical sequence as follows:
     38-40: DVK → GPL
     41-1030: Missing.
Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 4 (identifier: Q96T76-5)

The sequence of this isoform differs from the canonical sequence as follows:
     309-406: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q96T76-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRGEPVSSHRPYPLPRSLVRVM
Note: No experimental confirmation available.
Isoform 6 (identifier: Q96T76-9)

The sequence of this isoform differs from the canonical sequence as follows:
     165-207: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 10301029MMS19 nucleotide excision repair protein homolog
PRO_0000096514

Regions

Repeat43 – 8139HEAT 1
Repeat253 – 29139HEAT 2
Repeat387 – 42640HEAT 3
Repeat866 – 90439HEAT 4
Repeat908 – 94639HEAT 5
Repeat949 – 98739HEAT 6
Repeat990 – 102839HEAT 7

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue4961N6-acetyllysine Ref.10
Modified residue10271Phosphoserine Ref.12

Natural variations

Alternative sequence11M → MRGEPVSSHRPYPLPRSLVR VM in isoform 5.
VSP_044182
Alternative sequence38 – 403DVK → GPL in isoform 3.
VSP_040310
Alternative sequence41 – 1030990Missing in isoform 3.
VSP_040311
Alternative sequence165 – 20743Missing in isoform 6.
VSP_044183
Alternative sequence309 – 40698Missing in isoform 4.
VSP_015565
Alternative sequence309 – 31810VFQTASERVE → TAGTTCVNRT in isoform 2.
VSP_040312
Alternative sequence319 – 1030712Missing in isoform 2.
VSP_040313
Natural variant681A → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs2275586 [ dbSNP | Ensembl ].
VAR_023448
Natural variant981R → W. Ref.5
Corresponds to variant rs29001280 [ dbSNP | Ensembl ].
VAR_023449
Natural variant1971V → I. Ref.5
Corresponds to variant rs29001285 [ dbSNP | Ensembl ].
VAR_023450
Natural variant3061R → H. Ref.5
Corresponds to variant rs29001306 [ dbSNP | Ensembl ].
VAR_023451
Natural variant3651M → V. Ref.5
Corresponds to variant rs29001309 [ dbSNP | Ensembl ].
VAR_023452
Natural variant4091Q → P. Ref.5
Corresponds to variant rs29001311 [ dbSNP | Ensembl ].
VAR_023453
Natural variant4341Q → E. Ref.5
Corresponds to variant rs29001314 [ dbSNP | Ensembl ].
VAR_023454
Natural variant5261V → I. Ref.5
Corresponds to variant rs17112809 [ dbSNP | Ensembl ].
VAR_023455
Natural variant5581A → V. Ref.5
Corresponds to variant rs12360068 [ dbSNP | Ensembl ].
VAR_023456
Natural variant7901G → D. Ref.4 Ref.5 Ref.8
Corresponds to variant rs3740526 [ dbSNP | Ensembl ].
VAR_023457
Natural variant9831R → H. Ref.5
Corresponds to variant rs29001332 [ dbSNP | Ensembl ].
VAR_023458

Experimental info

Sequence conflict1791Q → H in AAK70402. Ref.2
Sequence conflict3891V → D in AAK70402. Ref.2
Sequence conflict3941L → P in AAK70402. Ref.2
Sequence conflict4731Q → R in BAG51657. Ref.4
Sequence conflict502 – 5032CR → W in BAG51657. Ref.4
Sequence conflict6071E → K in BAG65145. Ref.4
Sequence conflict6401E → G in BAB55315. Ref.4
Sequence conflict6611I → V in BAG65145. Ref.4
Sequence conflict7411L → F in AAK70402. Ref.2

Sequences

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

Last modified June 26, 2007. Version 2.
Checksum: 7EC22CF0E38EFE1D

FASTA1,030113,290
        10         20         30         40         50         60 
MAAAAAVEAA APMGALWGLV HDFVVGQQEG PADQVAADVK SGNYTVLQVV EALGSSLENP 

        70         80         90        100        110        120 
EPRTRARAIQ LLSQVLLHCH TLLLEKEVVH LILFYENRLK DHHLVIPSVL QGLKALSLCV 

       130        140        150        160        170        180 
ALPPGLAVSV LKAIFQEVHV QSLPQVDRHT VYNIITNFMR TREEELKSLG ADFTFGFIQV 

       190        200        210        220        230        240 
MDGEKDPRNL LVAFRIVHDL ISRDYSLGPF VEELFEVTSC YFPIDFTPPP NDPHGIQRED 

       250        260        270        280        290        300 
LILSLRAVLA STPRFAEFLL PLLIEKVDSE VLSAKLDSLQ TLNACCAVYG QKELKDFLPS 

       310        320        330        340        350        360 
LWASIRREVF QTASERVEAE GLAALHSLTA CLSRSVLRAD AEDLLDSFLS NILQDCRHHL 

       370        380        390        400        410        420 
CEPDMKLVWP SAKLLQAAAG ASARACDSVT SNVLPLLLEQ FHKHSQSSQR RTILEMLLGF 

       430        440        450        460        470        480 
LKLQQKWSYE DKDQRPLNGF KDQLCSLVFM ALTDPSTQLQ LVGIRTLTVL GAQPDLLSYE 

       490        500        510        520        530        540 
DLELAVGHLY RLSFLKEDSQ SCRVAALEAS GTLAALYPVA FSSHLVPKLA EELRVGESNL 

       550        560        570        580        590        600 
TNGDEPTQCS RHLCCLQALS AVSTHPSIVK ETLPLLLQHL WQVNRGNMVA QSSDVIAVCQ 

       610        620        630        640        650        660 
SLRQMAEKCQ QDPESCWYFH QTAIPCLLAL AVQASMPEKE PSVLRKVLLE DEVLAAMVSV 

       670        680        690        700        710        720 
IGTATTHLSP ELAAQSVTHI VPLFLDGNVS FLPENSFPSR FQPFQDGSSG QRRLIALLMA 

       730        740        750        760        770        780 
FVCSLPRNVE IPQLNQLMRE LLELSCCHSC PFSSTAAAKC FAGLLNKHPA GQQLDEFLQL 

       790        800        810        820        830        840 
AVDKVEAGLG SGPCRSQAFT LLLWVTKALV LRYHPLSSCL TARLMGLLSD PELGPAAADG 

       850        860        870        880        890        900 
FSLLMSDCTD VLTRAGHAEV RIMFRQRFFT DNVPALVQGF HAAPQDVKPN YLKGLSHVLN 

       910        920        930        940        950        960 
RLPKPVLLPE LPTLLSLLLE ALSCPDCVVQ LSTLSCLQPL LLEAPQVMSL HVDTLVTKFL 

       970        980        990       1000       1010       1020 
NLSSSPSMAV RIAALQCMHA LTRLPTPVLL PYKPQVIRAL AKPLDDKKRL VRKEAVSARG 

      1030 
EWFLLGSPGS 

« Hide

Isoform 2 [UniParc].

Checksum: 26BF6FED00AB85D4
Show »

FASTA31835,203
Isoform 3 [UniParc].

Checksum: 9AE881188641ECFA
Show »

FASTA403,888
Isoform 4 [UniParc].

Checksum: D55192BDBC190D1A
Show »

FASTA932102,639
Isoform 5 [UniParc].

Checksum: 1E9C9F27F55B9F62
Show »

FASTA1,051115,705
Isoform 6 [UniParc].

Checksum: 5BDE355AA44E8D1B
Show »

FASTA987108,380

References

« Hide 'large scale' references
[1]"Cloning of a human homolog of the yeast nucleotide excision repair gene MMS19 and interaction with transcription repair factor TFIIH via the XPB and XPD helicases."
Seroz T., Winkler G.S., Auriol J., Verhage R.A., Vermeulen W., Smit B., Brouwer J., Eker A.P.M., Weeda G., Egly J.-M., Hoeijmakers J.H.J.
Nucleic Acids Res. 28:4506-4513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ERCC2 AND ERCC3.
Tissue: Cervix carcinoma.
[2]"The human homologue of the yeast DNA repair and TFIIH regulator MMS19 is an AF-1-specific coactivator of estrogen receptor."
Wu X., Li H., Chen J.D.
J. Biol. Chem. 276:23962-23968(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, INTERACTION WITH NCOA3, SUBCELLULAR LOCATION.
[3]"Cloning the human and mouse MMS19 genes and functional complementation of a yeast mms19 deletion mutant."
Queimado L., Rao M., Schultz R.A., Koonin E.V., Aravind L., Nardo T., Stefanini M., Friedberg E.C.
Nucleic Acids Res. 29:1884-1891(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLY-68.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-1030 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-1030 (ISOFORM 2), VARIANTS GLY-68 AND ASP-790.
Tissue: Teratocarcinoma, Tongue and Trachea.
[5]NIEHS SNPs program
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-68; TRP-98; ILE-197; HIS-306; VAL-365; PRO-409; GLU-434; ILE-526; VAL-558; ASP-790 AND HIS-983.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-68.
[8]"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] (ISOFORMS 1 AND 3), VARIANTS GLY-68 AND ASP-790.
Tissue: Brain, Lymph and Uterus.
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation."
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., Kuraoka I., Hiraoka Y., Tanaka K.
Mol. Cell 39:632-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH FAM96B, SUBCELLULAR LOCATION.
[12]"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-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity."
Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T., Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.
Science 337:195-199(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CIA COMPLEX.
[15]"MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism."
Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.
Science 337:243-245(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH RTEL1.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ306408 mRNA. Translation: CAC29239.1. Frameshift.
AF357881 mRNA. Translation: AAK70402.1.
AF319947 mRNA. Translation: AAK52668.1.
AK027710 mRNA. Translation: BAB55315.1. Different initiation.
AK056244 mRNA. Translation: BAG51657.1. Different initiation.
AK056581 mRNA. Translation: BAB71223.1. Sequence problems.
AK298995 mRNA. Translation: BAG61084.1.
AK304287 mRNA. Translation: BAG65145.1.
AY974244 Genomic DNA. Translation: AAX59033.1.
AL355490, AL359388 Genomic DNA. Translation: CAI40770.1.
AL355490, AL359388 Genomic DNA. Translation: CAQ10792.1.
AL359388, AL355490 Genomic DNA. Translation: CAI14189.1.
AL359388, AL355490 Genomic DNA. Translation: CAQ08641.1.
CH471066 Genomic DNA. Translation: EAW49924.1.
CH471066 Genomic DNA. Translation: EAW49927.1.
CH471066 Genomic DNA. Translation: EAW49928.1.
BC002692 mRNA. Translation: AAH02692.1.
BC006575 mRNA. Translation: AAH06575.2.
BC009396 mRNA. Translation: AAH09396.2.
BC080532 mRNA. Translation: AAH80532.1. Sequence problems.
BC117129 mRNA. Translation: AAI17130.1.
RefSeqNP_071757.4. NM_022362.4.
UniGeneHs.500721.

3D structure databases

ProteinModelPortalQ96T76.
SMRQ96T76. Positions 258-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122103. 180 interactions.
IntActQ96T76. 5 interactions.

PTM databases

PhosphoSiteQ96T76.

Polymorphism databases

DMDM150421597.

Proteomic databases

PaxDbQ96T76.
PRIDEQ96T76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327238; ENSP00000320059; ENSG00000155229. [Q96T76-5]
ENST00000327277; ENSP00000322236; ENSG00000155229.
ENST00000355839; ENSP00000348097; ENSG00000155229. [Q96T76-9]
ENST00000370782; ENSP00000359818; ENSG00000155229. [Q96T76-1]
ENST00000415383; ENSP00000395045; ENSG00000155229. [Q96T76-6]
ENST00000438925; ENSP00000412698; ENSG00000155229. [Q96T76-1]
ENST00000441194; ENSP00000413801; ENSG00000155229. [Q96T76-6]
GeneID64210.
KEGGhsa:64210.
UCSCuc001knr.3. human. [Q96T76-1]
uc009xvt.3. human. [Q96T76-5]
uc010qox.3. human. [Q96T76-9]

Organism-specific databases

CTD64210.
GeneCardsGC10M099209.
H-InvDBHIX0009091.
HGNCHGNC:13824. MMS19.
HPAHPA051936.
HPA056299.
MIM614777. gene.
neXtProtNX_Q96T76.
PharmGKBPA162395974.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320478.
HOVERGENHBG057358.
InParanoidQ96T76.
KOK15075.
OMALYPVAFS.
PhylomeDBQ96T76.
TreeFamTF314469.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ96T76.
BgeeQ96T76.
CleanExHS_MMS19.
GenevestigatorQ96T76.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024687. MMS19_C.
[Graphical view]
PfamPF12460. MMS19_C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

ChiTaRSMMS19. human.
GeneWikiMMS19.
GenomeRNAi64210.
NextBio66115.
PROQ96T76.
SOURCESearch...

Entry information

Entry nameMMS19_HUMAN
AccessionPrimary (citable) accession number: Q96T76
Secondary accession number(s): B0QZ75 expand/collapse secondary AC list , B3KPE5, B4DQX2, B4E2I3, D3DR55, F8W9Y2, Q17RZ8, Q5T455, Q66K82, Q7L4W8, Q969Z1, Q96DF1, Q96MR1, Q96RK5, Q96SK1, Q9BUE2, Q9BYS9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM