Q96T76 (MMS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MMS19 nucleotide excision repair protein homolog
Short name=hMMS19

Alternative name(s):
MET18 homolog
MMS19-like protein

Gene names

Name:	MMS19
Synonyms:	MMS19L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1030 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle 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 process	Chromosome partition DNA damage DNA repair Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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_component	CIA 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_function	estrogen receptor binding Inferred from physical interaction Ref.2. Source: UniProtKB protein binding Inferred from physical interaction Ref.2Ref.11. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 1030	1029	MMS19 nucleotide excision repair protein homolog		PRO_0000096514
Regions
	Repeat	43 – 81	39	HEAT 1
	Repeat	253 – 291	39	HEAT 2
	Repeat	387 – 426	40	HEAT 3
	Repeat	866 – 904	39	HEAT 4
	Repeat	908 – 946	39	HEAT 5
	Repeat	949 – 987	39	HEAT 6
	Repeat	990 – 1028	39	HEAT 7
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9
	Modified residue	496	1	N6-acetyllysine Ref.10
	Modified residue	1027	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	1	1	M → MRGEPVSSHRPYPLPRSLVR VM in isoform 5.		VSP_044182
	Alternative sequence	38 – 40	3	DVK → GPL in isoform 3.		VSP_040310
	Alternative sequence	41 – 1030	990	Missing in isoform 3.		VSP_040311
	Alternative sequence	165 – 207	43	Missing in isoform 6.		VSP_044183
	Alternative sequence	309 – 406	98	Missing in isoform 4.		VSP_015565
	Alternative sequence	309 – 318	10	VFQTASERVE → TAGTTCVNRT in isoform 2.		VSP_040312
	Alternative sequence	319 – 1030	712	Missing in isoform 2.		VSP_040313
	Natural variant	68	1	A → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Corresponds to variant rs2275586 [ dbSNP | Ensembl ].		VAR_023448
	Natural variant	98	1	R → W. Ref.5 Corresponds to variant rs29001280 [ dbSNP | Ensembl ].		VAR_023449
	Natural variant	197	1	V → I. Ref.5 Corresponds to variant rs29001285 [ dbSNP | Ensembl ].		VAR_023450
	Natural variant	306	1	R → H. Ref.5 Corresponds to variant rs29001306 [ dbSNP | Ensembl ].		VAR_023451
	Natural variant	365	1	M → V. Ref.5 Corresponds to variant rs29001309 [ dbSNP | Ensembl ].		VAR_023452
	Natural variant	409	1	Q → P. Ref.5 Corresponds to variant rs29001311 [ dbSNP | Ensembl ].		VAR_023453
	Natural variant	434	1	Q → E. Ref.5 Corresponds to variant rs29001314 [ dbSNP | Ensembl ].		VAR_023454
	Natural variant	526	1	V → I. Ref.5 Corresponds to variant rs17112809 [ dbSNP | Ensembl ].		VAR_023455
	Natural variant	558	1	A → V. Ref.5 Corresponds to variant rs12360068 [ dbSNP | Ensembl ].		VAR_023456
	Natural variant	790	1	G → D. Ref.4 Ref.5 Ref.8 Corresponds to variant rs3740526 [ dbSNP | Ensembl ].		VAR_023457
	Natural variant	983	1	R → H. Ref.5 Corresponds to variant rs29001332 [ dbSNP | Ensembl ].		VAR_023458
Experimental info
	Sequence conflict	179	1	Q → H in AAK70402. Ref.2
	Sequence conflict	389	1	V → D in AAK70402. Ref.2
	Sequence conflict	394	1	L → P in AAK70402. Ref.2
	Sequence conflict	473	1	Q → R in BAG51657. Ref.4
	Sequence conflict	502 – 503	2	CR → W in BAG51657. Ref.4
	Sequence conflict	607	1	E → K in BAG65145. Ref.4
	Sequence conflict	640	1	E → G in BAB55315. Ref.4
	Sequence conflict	661	1	I → V in BAG65145. Ref.4
	Sequence conflict	741	1	L → F in AAK70402. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 7EC22CF0E38EFE1D	FASTA	1,030	113,290
	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
	Isoform 2 [UniParc]. Checksum: 26BF6FED00AB85D4	FASTA	318	35,203
	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 LWASIRRETA GTTCVNRT
	Isoform 3 [UniParc]. Checksum: 9AE881188641ECFA	FASTA	40	3,888
	10 20 30 40 MAAAAAVEAA APMGALWGLV HDFVVGQQEG PADQVAAGPL
	Isoform 4 [UniParc]. Checksum: D55192BDBC190D1A	FASTA	932	102,639
	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 LWASIRRESS QRRTILEMLL GFLKLQQKWS YEDKDQRPLN GFKDQLCSLV FMALTDPSTQ 370 380 390 400 410 420 LQLVGIRTLT VLGAQPDLLS YEDLELAVGH LYRLSFLKED SQSCRVAALE ASGTLAALYP 430 440 450 460 470 480 VAFSSHLVPK LAEELRVGES NLTNGDEPTQ CSRHLCCLQA LSAVSTHPSI VKETLPLLLQ 490 500 510 520 530 540 HLWQVNRGNM VAQSSDVIAV CQSLRQMAEK CQQDPESCWY FHQTAIPCLL ALAVQASMPE 550 560 570 580 590 600 KEPSVLRKVL LEDEVLAAMV SVIGTATTHL SPELAAQSVT HIVPLFLDGN VSFLPENSFP 610 620 630 640 650 660 SRFQPFQDGS SGQRRLIALL MAFVCSLPRN VEIPQLNQLM RELLELSCCH SCPFSSTAAA 670 680 690 700 710 720 KCFAGLLNKH PAGQQLDEFL QLAVDKVEAG LGSGPCRSQA FTLLLWVTKA LVLRYHPLSS 730 740 750 760 770 780 CLTARLMGLL SDPELGPAAA DGFSLLMSDC TDVLTRAGHA EVRIMFRQRF FTDNVPALVQ 790 800 810 820 830 840 GFHAAPQDVK PNYLKGLSHV LNRLPKPVLL PELPTLLSLL LEALSCPDCV VQLSTLSCLQ 850 860 870 880 890 900 PLLLEAPQVM SLHVDTLVTK FLNLSSSPSM AVRIAALQCM HALTRLPTPV LLPYKPQVIR 910 920 930 ALAKPLDDKK RLVRKEAVSA RGEWFLLGSP GS
	Isoform 5 [UniParc]. Checksum: 1E9C9F27F55B9F62	FASTA	1,051	115,705
	10 20 30 40 50 60 MRGEPVSSHR PYPLPRSLVR VMAAAAAVEA AAPMGALWGL VHDFVVGQQE GPADQVAADV 70 80 90 100 110 120 KSGNYTVLQV VEALGSSLEN PEPRTRARAI QLLSQVLLHC HTLLLEKEVV HLILFYENRL 130 140 150 160 170 180 KDHHLVIPSV LQGLKALSLC VALPPGLAVS VLKAIFQEVH VQSLPQVDRH TVYNIITNFM 190 200 210 220 230 240 RTREEELKSL GADFTFGFIQ VMDGEKDPRN LLVAFRIVHD LISRDYSLGP FVEELFEVTS 250 260 270 280 290 300 CYFPIDFTPP PNDPHGIQRE DLILSLRAVL ASTPRFAEFL LPLLIEKVDS EVLSAKLDSL 310 320 330 340 350 360 QTLNACCAVY GQKELKDFLP SLWASIRREV FQTASERVEA EGLAALHSLT ACLSRSVLRA 370 380 390 400 410 420 DAEDLLDSFL SNILQDCRHH LCEPDMKLVW PSAKLLQAAA GASARACDSV TSNVLPLLLE 430 440 450 460 470 480 QFHKHSQSSQ RRTILEMLLG FLKLQQKWSY EDKDQRPLNG FKDQLCSLVF MALTDPSTQL 490 500 510 520 530 540 QLVGIRTLTV LGAQPDLLSY EDLELAVGHL YRLSFLKEDS QSCRVAALEA SGTLAALYPV 550 560 570 580 590 600 AFSSHLVPKL AEELRVGESN LTNGDEPTQC SRHLCCLQAL SAVSTHPSIV KETLPLLLQH 610 620 630 640 650 660 LWQVNRGNMV AQSSDVIAVC QSLRQMAEKC QQDPESCWYF HQTAIPCLLA LAVQASMPEK 670 680 690 700 710 720 EPSVLRKVLL EDEVLAAMVS VIGTATTHLS PELAAQSVTH IVPLFLDGNV SFLPENSFPS 730 740 750 760 770 780 RFQPFQDGSS GQRRLIALLM AFVCSLPRNV EIPQLNQLMR ELLELSCCHS CPFSSTAAAK 790 800 810 820 830 840 CFAGLLNKHP AGQQLDEFLQ LAVDKVEAGL GSGPCRSQAF TLLLWVTKAL VLRYHPLSSC 850 860 870 880 890 900 LTARLMGLLS DPELGPAAAD GFSLLMSDCT DVLTRAGHAE VRIMFRQRFF TDNVPALVQG 910 920 930 940 950 960 FHAAPQDVKP NYLKGLSHVL NRLPKPVLLP ELPTLLSLLL EALSCPDCVV QLSTLSCLQP 970 980 990 1000 1010 1020 LLLEAPQVMS LHVDTLVTKF LNLSSSPSMA VRIAALQCMH ALTRLPTPVL LPYKPQVIRA 1030 1040 1050 LAKPLDDKKR LVRKEAVSAR GEWFLLGSPG S
	Isoform 6 [UniParc]. Checksum: 5BDE355AA44E8D1B	FASTA	987	108,380
	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 TREEGPFVEE LFEVTSCYFP 190 200 210 220 230 240 IDFTPPPNDP HGIQREDLIL SLRAVLASTP RFAEFLLPLL IEKVDSEVLS AKLDSLQTLN 250 260 270 280 290 300 ACCAVYGQKE LKDFLPSLWA SIRREVFQTA SERVEAEGLA ALHSLTACLS RSVLRADAED 310 320 330 340 350 360 LLDSFLSNIL QDCRHHLCEP DMKLVWPSAK LLQAAAGASA RACDSVTSNV LPLLLEQFHK 370 380 390 400 410 420 HSQSSQRRTI LEMLLGFLKL QQKWSYEDKD QRPLNGFKDQ LCSLVFMALT DPSTQLQLVG 430 440 450 460 470 480 IRTLTVLGAQ PDLLSYEDLE LAVGHLYRLS FLKEDSQSCR VAALEASGTL AALYPVAFSS 490 500 510 520 530 540 HLVPKLAEEL RVGESNLTNG DEPTQCSRHL CCLQALSAVS THPSIVKETL PLLLQHLWQV 550 560 570 580 590 600 NRGNMVAQSS DVIAVCQSLR QMAEKCQQDP ESCWYFHQTA IPCLLALAVQ ASMPEKEPSV 610 620 630 640 650 660 LRKVLLEDEV LAAMVSVIGT ATTHLSPELA AQSVTHIVPL FLDGNVSFLP ENSFPSRFQP 670 680 690 700 710 720 FQDGSSGQRR LIALLMAFVC SLPRNVEIPQ LNQLMRELLE LSCCHSCPFS STAAAKCFAG 730 740 750 760 770 780 LLNKHPAGQQ LDEFLQLAVD KVEAGLGSGP CRSQAFTLLL WVTKALVLRY HPLSSCLTAR 790 800 810 820 830 840 LMGLLSDPEL GPAAADGFSL LMSDCTDVLT RAGHAEVRIM FRQRFFTDNV PALVQGFHAA 850 860 870 880 890 900 PQDVKPNYLK GLSHVLNRLP KPVLLPELPT LLSLLLEALS CPDCVVQLST LSCLQPLLLE 910 920 930 940 950 960 APQVMSLHVD TLVTKFLNLS SSPSMAVRIA ALQCMHALTR LPTPVLLPYK PQVIRALAKP 970 980 LDDKKRLVRK EAVSARGEWF LLGSPGS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

NIEHS-SNPs

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.
CCDS	CCDS7464.1. [Q96T76-1]
RefSeq	NP_001276332.1. NM_001289403.1. [Q96T76-9] NP_001276333.1. NM_001289404.1. NP_001276334.1. NM_001289405.1. [Q96T76-1] NP_071757.4. NM_022362.4. [Q96T76-1]
UniGene	Hs.500721.
3D structure databases
ProteinModelPortal	Q96T76.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	122103. 181 interactions.
IntAct	Q96T76. 5 interactions.
PTM databases
PhosphoSite	Q96T76.
Polymorphism databases
DMDM	150421597.
Proteomic databases
MaxQB	Q96T76.
PaxDb	Q96T76.
PRIDE	Q96T76.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000327238; 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]
GeneID	64210.
KEGG	hsa:64210.
UCSC	uc001knr.3. human. [Q96T76-1] uc009xvt.3. human. [Q96T76-5] uc010qox.3. human. [Q96T76-9]
Organism-specific databases
CTD	64210.
GeneCards	GC10M099209.
H-InvDB	HIX0009091.
HGNC	HGNC:13824. MMS19.
HPA	HPA051936. HPA056299.
MIM	614777. gene.
neXtProt	NX_Q96T76.
PharmGKB	PA162395974.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG320478.
HOVERGEN	HBG057358.
InParanoid	Q96T76.
KO	K15075.
OMA	DHITSNV.
PhylomeDB	Q96T76.
TreeFam	TF314469.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q96T76.
Bgee	Q96T76.
CleanEx	HS_MMS19.
Genevestigator	Q96T76.
Family and domain databases
Gene3D	1.25.10.10. 2 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR024687. MMS19_C. [Graphical view]
Pfam	PF12460. MMS19_C. 1 hit. [Graphical view]
SUPFAM	SSF48371. SSF48371. 5 hits.
ProtoNet	Search...
Other
ChiTaRS	MMS19. human.
GeneWiki	MMS19.
GenomeRNAi	64210.
NextBio	66115.
PRO	Q96T76.
SOURCE	Search...

Entry information

Entry name

MMS19_HUMAN

Accession

Primary (citable) accession number: Q96T76
Secondary accession number(s): B0QZ75 , 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:	July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.