GenomeNet

Database: UniProt
Entry: Q2VPA6
LinkDB: Q2VPA6
Original site: Q2VPA6 
ID   HELQ_MOUSE              Reviewed;        1069 AA.
AC   Q2VPA6; Q2VPA7; Q640L4; Q8BWI5; Q8R4K9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   16-OCT-2019, entry version 112.
DE   RecName: Full=Helicase POLQ-like;
DE            EC=3.6.4.12;
DE   AltName: Full=Mus308-like helicase;
DE   AltName: Full=POLQ-like helicase;
GN   Name=Helq; Synonyms=Hel308;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 3-1069 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-749 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 298-1069 (ISOFORM 3).
RC   STRAIN=BALB/cJ;
RX   PubMed=11751861; DOI=10.1074/jbc.m110271200;
RA   Marini F., Wood R.D.;
RT   "A human DNA helicase homologous to the DNA cross-link sensitivity
RT   protein Mus308.";
RL   J. Biol. Chem. 277:8716-8723(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Single-stranded DNA-dependent ATPase and 5' to 3' DNA
CC       helicase. Involved in the repair of DNA cross-links and double-
CC       strand break (DSB) resistance. Participates in FANCD2-mediated
CC       repair. Forms a complex with POLN polymerase that participates in
CC       homologous recombination (HR) repair and is essential for cellular
CC       protection against DNA cross-links.
CC       {ECO:0000250|UniProtKB:Q8TDG4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Hexamer. Interacts with POLN.
CC       {ECO:0000250|UniProtKB:Q8TDG4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q2VPA6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2VPA6-2; Sequence=VSP_032952;
CC       Name=3;
CC         IsoId=Q2VPA6-3; Sequence=VSP_032949, VSP_032950, VSP_032951;
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000305}.
DR   EMBL; BC082601; AAH82601.1; -; mRNA.
DR   EMBL; BC109169; AAI09170.1; -; mRNA.
DR   EMBL; BC109170; AAI09171.2; -; mRNA.
DR   EMBL; AK052427; BAC34984.1; -; mRNA.
DR   EMBL; AF436846; AAL85275.1; -; mRNA.
DR   CCDS; CCDS39184.1; -. [Q2VPA6-1]
DR   RefSeq; NP_001074576.1; NM_001081107.1. [Q2VPA6-1]
DR   SMR; Q2VPA6; -.
DR   BioGrid; 228629; 1.
DR   STRING; 10090.ENSMUSP00000041599; -.
DR   iPTMnet; Q2VPA6; -.
DR   PhosphoSitePlus; Q2VPA6; -.
DR   EPD; Q2VPA6; -.
DR   MaxQB; Q2VPA6; -.
DR   PaxDb; Q2VPA6; -.
DR   PRIDE; Q2VPA6; -.
DR   Ensembl; ENSMUST00000044684; ENSMUSP00000041599; ENSMUSG00000035266. [Q2VPA6-1]
DR   GeneID; 191578; -.
DR   KEGG; mmu:191578; -.
DR   UCSC; uc008yhz.1; mouse. [Q2VPA6-1]
DR   UCSC; uc012dzs.1; mouse. [Q2VPA6-2]
DR   CTD; 113510; -.
DR   MGI; MGI:2176740; Helq.
DR   eggNOG; KOG0950; Eukaryota.
DR   eggNOG; COG1204; LUCA.
DR   GeneTree; ENSGT00940000157350; -.
DR   HOGENOM; HOG000110747; -.
DR   InParanoid; Q2VPA6; -.
DR   KO; K19178; -.
DR   OMA; NSNERGD; -.
DR   OrthoDB; 179246at2759; -.
DR   PhylomeDB; Q2VPA6; -.
DR   TreeFam; TF105018; -.
DR   ChiTaRS; Helq; mouse.
DR   PRO; PR:Q2VPA6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000035266; Expressed in 180 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q2VPA6; baseline and differential.
DR   Genevisible; Q2VPA6; MM.
DR   GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR   GO; GO:0006259; P:DNA metabolic process; ISO:MGI.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; DNA damage;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1   1069       Helicase POLQ-like.
FT                                /FTId=PRO_0000329061.
FT   DOMAIN      305    477       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      525    717       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     318    325       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       422    425       DEAH box.
FT   VAR_SEQ     725    766       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11751861}.
FT                                /FTId=VSP_032949.
FT   VAR_SEQ     851    866       FGQLSPTEQNVAALLG -> VTEQVSWAETSLDFVT (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:11751861}.
FT                                /FTId=VSP_032950.
FT   VAR_SEQ     867   1069       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11751861}.
FT                                /FTId=VSP_032951.
FT   VAR_SEQ     884    979       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_032952.
FT   CONFLICT    428    428       G -> C (in Ref. 1; AAI09170).
FT                                {ECO:0000305}.
FT   CONFLICT    440    440       L -> Q (in Ref. 3; AAL85275).
FT                                {ECO:0000305}.
FT   CONFLICT    533    533       V -> A (in Ref. 3; AAL85275).
FT                                {ECO:0000305}.
FT   CONFLICT    647    647       A -> S (in Ref. 1; AAH82601).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1069 AA;  119098 MW;  69E56935E9F65BCB CRC64;
     MEDGCPRIRR RVSVRKRNRG NLENLRASPT PAELQPAEDT EDEAAAGSRR RKTGSPEHAQ
     ENDSEEDMFG DYDSFTESSF LAHVDDLEQR YMQLPECGDR DADSGTKDLC SAGLKNNLRV
     TTVINLTDPE TSEHGQKQSH LDVPAEPEPG SDLSFDVPSS QILYFENPQN SPEALGDPCT
     KKTNGDPQKS SHEELVSSHT EQPEPNNDFS NVRAASESSR RKSLKDHLKS TMAGNARAQT
     PAFPRSKHLR EALLSEEISV AKKAIESPSD DLGPFYSLPS KVRDLYVQLK GIKKLYDWQH
     TCLTLRSVQE RKNLIYSLPT SGGKTLVAEI LMLQELLCRQ KDVLMILPYV AIVQEKISSL
     SSFGIELGFF VEEYAGSKGR FPPIKRREKK SLYIATIEKA HSLVNALIET SRLSTLGLVV
     VDELHMIGEG SRGAILEMTL AKVLYTSKTT QIIGMSATLN NVEDLQAFLK AEYYTSQFRP
     VELKEFLKVN DTIYEVDSQA ADGMTFSRLL SYKYSEALKK MDPDRLVALV TEVIPNYSCL
     VFCPSKKNCE NVAEMLCKFL SKDYLNHREK EKCEVIKSLR NIGNGKVCPV LKRTVPFGIA
     YHHSGLTSEE RKLLEEAYST GVLCLLTCTS TLAAGVNLPA RRVILRAPYV ANTFLKRNQY
     KQMVGRAGRA GIDTAGESIL LLQEKDKQQV LELISGPLET CCSHLVEEFT KGIQALFLSL
     IGLKIAASLG DIYQFMSGTF FGVQQKILLK EKSLWEITVD ALEHLTEKGL LQKDSCGDNE
     GLECHFRITK LGQASFKGAI DLAYCDTLYR DLKKGLEGLV LESLLHLIYL TTPYDLAAQS
     EPDWMVYFKQ FGQLSPTEQN VAALLGVSES FIGKKAAGQA VRKKVDKNVV NRLYLSFVLY
     SLLKETNVWS VSEKFNLPRG YIQNLLMGAA SFSSCVLHFC EELEEFWVYK ALLVELTKKL
     TYCVKAELIP LMEVTGVLEG RAKQLYNAGY RSIMHLANAN PEVLVKTIDH LSRRQARQIV
     SSAKMLLHEK AEALQGEAEE LLRLPADLPG LGGPSSERAG SHAGDVTLS
//
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