O08811 (ERCC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TFIIH basal transcription factor complex helicase XPD subunit
EC=3.6.4.12

Alternative name(s):
CXPD
DNA excision repair protein ERCC-2
DNA repair protein complementing XP-D cells
Xeroderma pigmentosum group D-complementing protein

Gene names

Name:	Ercc2
Synonyms:	Xpd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	ATP-dependent 5'-3' DNA helicase, component of the core-TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers By similarity.
Catalytic activity	ATP + H2O = ADP + phosphate.
Cofactor	Magnesium By similarity. Binds 1 4Fe-4S cluster By similarity.
Subunit structure	One of the six subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with FAM196B; the interaction is direct By similarity. Interacts with ATF7IP By similarity.
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › spindle By similarity.
Post-translational modification	ISGylated By similarity.
Sequence similarities	Belongs to the helicase family. RAD3/XPD subfamily. Contains 1 helicase ATP-binding domain.
Sequence caution	The sequence BAB23443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Chromosome partition DNA damage DNA repair Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	4Fe-4S ATP-binding DNA-binding Iron Iron-sulfur Magnesium Metal-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from sequence or structural similarity. Source: GOC DNA duplex unwinding Inferred from sequence or structural similarity. Source: GOC DNA repair Inferred from mutant phenotype PubMed 11950998. Source: MGI UV protection Inferred from mutant phenotype PubMed 9651581. Source: MGI aging Inferred from mutant phenotype PubMed 11950998PubMed 17020410PubMed 18545656. Source: MGI apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB bone mineralization Inferred from mutant phenotype PubMed 17020410. Source: MGI cell cycle checkpoint Inferred from electronic annotation. Source: Ensembl cell proliferation Inferred from mutant phenotype PubMed 17554309. Source: MGI central nervous system myelin formation Inferred from mutant phenotype PubMed 17952069. Source: MGI chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB embryonic cleavage Inferred from mutant phenotype Ref.1. Source: MGI erythrocyte maturation Inferred from mutant phenotype PubMed 17020410. Source: MGI extracellular matrix organization Inferred from mutant phenotype PubMed 9651581. Source: MGI hair cell differentiation Inferred from mutant phenotype PubMed 17020410. Source: MGI hair cycle process Inferred from mutant phenotype PubMed 17020410. Source: MGI hair follicle maturation Inferred from mutant phenotype PubMed 9651581. Source: MGI hematopoietic stem cell differentiation Inferred from mutant phenotype PubMed 17554309. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 17020410. Source: MGI multicellular organism growth Inferred from mutant phenotype PubMed 17020410. Source: MGI nucleotide-excision repair Inferred from mutant phenotype PubMed 11950998PubMed 9651581. Source: MGI nucleotide-excision repair, DNA incision Inferred from electronic annotation. Source: Ensembl positive regulation of DNA binding Inferred from mutant phenotype PubMed 17952069. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl post-embryonic development Inferred from mutant phenotype PubMed 11950998PubMed 17020410. Source: MGI response to UV Inferred from mutant phenotype PubMed 17020410. Source: MGI response to hypoxia Inferred from electronic annotation. Source: Ensembl response to oxidative stress Inferred from mutant phenotype PubMed 11950998. Source: MGI skin development Inferred from mutant phenotype PubMed 17020410PubMed 9651581. Source: MGI spinal cord development Inferred from mutant phenotype PubMed 17020410. Source: MGI transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	MMXD complex Inferred from sequence or structural similarity. Source: UniProtKB SSL2-core TFIIH complex Inferred from electronic annotation. Source: Ensembl cyclin-dependent protein kinase activating kinase holoenzyme complex Inferred from electronic annotation. Source: Ensembl cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB holo TFIIH complex Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay PubMed 17952069. Source: MGI spindle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 5'-3' DNA helicase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: Ensembl metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 760	760	TFIIH basal transcription factor complex helicase XPD subunit		PRO_0000101981
Regions
	Domain	7 – 283	277	Helicase ATP-binding
	Nucleotide binding	42 – 49	8	ATP By similarity
	Region	438 – 637	200	Mediates interaction with MMS19 By similarity
	Motif	234 – 237	4	DEAH box
Sites
	Metal binding	116	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	134	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	155	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	190	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	285	1	Y → C in BAB23443. Ref.2
	Sequence conflict	595	1	I → V in AAB58296. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O08811 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 02B2E116792D4E44	FASTA	760	86,842
	10 20 30 40 50 60 MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV SLLALIVAYQ 70 80 90 100 110 120 RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE KLPFLGLALS SRKNLCIHPE 130 140 150 160 170 180 VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA SLPHCRFYEE FDIHGRQMPL PAGIYNLDDL 190 200 210 220 230 240 KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID 250 260 270 280 290 300 NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASVARE 310 320 330 340 350 360 TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG 370 380 390 400 410 420 LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL ANFATLVSTY AKGFTIIIEP 430 440 450 460 470 480 FDDRTPTIAN PVLHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT 490 500 510 520 530 540 FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT 550 560 570 580 590 600 SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 610 620 630 640 650 660 RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA 670 680 690 700 710 720 AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH LTDSNLNLTV DEGVQVAKYF 730 740 750 760 LRQMAQPFHR EDQLGLSLLS LEQLQSEETL QRIEQIAQQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Disruption of the mouse xeroderma pigmentosum group D DNA repair/basal transcription gene results in preimplantation lethality." de Boer J., Donker I., de Wit J., Hoeijmakers J.H.J., Weeda G. Cancer Res. 58:89-94(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U97572 mRNA. Translation: AAB58296.1. AK004652 mRNA. Translation: BAB23443.1. Different initiation. AK082761 mRNA. Translation: BAC38607.1. CH466639 Genomic DNA. Translation: EDL23140.1.
RefSeq	NP_031975.2. NM_007949.4.
UniGene	Mm.36524.
3D structure databases
ProteinModelPortal	O08811.
SMR	O08811. Positions 26-258.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
IntAct	O08811. 1 interaction.
MINT	MINT-4114299.
STRING	10090.ENSMUSP00000054380.
PTM databases
PhosphoSite	O08811.
Proteomic databases
PaxDb	O08811.
PRIDE	O08811.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000062831; ENSMUSP00000054380; ENSMUSG00000030400.
GeneID	13871.
KEGG	mmu:13871.
UCSC	uc009flq.1. mouse.
Organism-specific databases
CTD	2068.
MGI	MGI:95413. Ercc2.
Phylogenomic databases
eggNOG	COG1199.
GeneTree	ENSGT00550000075092.
HOGENOM	HOG000205390.
HOVERGEN	HBG051498.
InParanoid	Q8C487.
KO	K10844.
OMA	PHCRFYE.
OrthoDB	EOG70W3CM.
TreeFam	TF101232.
Gene expression databases
Bgee	O08811.
Genevestigator	O08811.
Family and domain databases
Gene3D	3.40.50.300. 2 hits.
InterPro	IPR006555. ATP-dep_Helicase_C. IPR010614. DEAD_2. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR013020. DNA_helicase_DNA-repair_Rad3. IPR010643. DUF1227. IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3. IPR006554. Helicase-like_DEXD_c2. IPR027417. P-loop_NTPase. IPR001945. XPGD_DNA_repair. [Graphical view]
Pfam	PF06733. DEAD_2. 1 hit. PF06777. DUF1227. 1 hit. PF13307. Helicase_C_2. 1 hit. [Graphical view]
PRINTS	PR00852. XRODRMPGMNTD.
SMART	SM00488. DEXDc2. 1 hit. SM00491. HELICc2. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 4 hits.
TIGRFAMs	TIGR00604. rad3. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51193. HELICASE_ATP_BIND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284788.
PRO	O08811.
SOURCE	Search...

Entry information

Entry name

ERCC2_MOUSE

Accession

Primary (citable) accession number: O08811
Secondary accession number(s): Q8C487, Q9DC01

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program