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HELQ_MOUSE
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   03-AUG-2022, entry version 126.
DE   RecName: Full=Helicase POLQ-like {ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8TDG4};
DE   AltName: Full=Mus308-like helicase {ECO:0000303|PubMed:11751861};
DE   AltName: Full=POLQ-like helicase {ECO:0000303|PubMed:11751861};
GN   Name=Helq {ECO:0000303|PubMed:24005329};
GN   Synonyms=Hel308 {ECO:0000303|PubMed:11751861};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [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 project:
RT   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 protein
RT   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION, INTERACTION WITH RAD51C, AND DISRUPTION PHENOTYPE.
RX   PubMed=24005329; DOI=10.1038/nature12565;
RA   Adelman C.A., Lolo R.L., Birkbak N.J., Murina O., Matsuzaki K., Horejsi Z.,
RA   Parmar K., Borel V., Skehel J.M., Stamp G., D'Andrea A., Sartori A.A.,
RA   Swanton C., Boulton S.J.;
RT   "HELQ promotes RAD51 paralogue-dependent repair to avert germ cell loss and
RT   tumorigenesis.";
RL   Nature 502:381-384(2013).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24005041; DOI=10.1093/nar/gkt676;
RA   Luebben S.W., Kawabata T., Akre M.K., Lee W.L., Johnson C.S.,
RA   O'Sullivan M.G., Shima N.;
RT   "Helq acts in parallel to Fancc to suppress replication-associated genome
RT   instability.";
RL   Nucleic Acids Res. 41:10283-10297(2013).
CC   -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC       homology-driven double-strand break (DSB) repair (PubMed:24005329,
CC       PubMed:24005041). Involved in different DSB repair mechanisms that are
CC       guided by annealing of extensive stretches of complementary bases at
CC       break ends, such as microhomology-mediated end-joining (MMEJ), single-
CC       strand annealing (SSA) or synthesis-dependent strand annealing (SDSA)
CC       (By similarity). Possesses both DNA unwinding and annealing activities
CC       (By similarity). Forms a complex with RAD51, stimulating HELQ DNA
CC       helicase activity and ability to unwing DNA (By similarity).
CC       Efficiently unwinds substrates containing 3' overhangs or a D-loop (By
CC       similarity). In contrast, interaction with the replication protein A
CC       (RPA/RP-A) complex inhibits DNA unwinding by HELQ but strongly
CC       stimulates DNA strand annealing (By similarity). Triggers displacement
CC       of RPA from single-stranded DNA to facilitate annealing of
CC       complementary sequences (By similarity). {ECO:0000250|UniProtKB:Q8TDG4,
CC       ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24005329}.
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         Evidence={ECO:0000250|UniProtKB:Q8TDG4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:Q8TDG4};
CC   -!- SUBUNIT: Hexamer (By similarity). Interacts with POLN (By similarity).
CC       Interacts with RAD51B (By similarity). Interacts with RAD51C; promoting
CC       association with the BCDX2 complex (PubMed:24005329). Interacts with
CC       the replication protein A (RPA/RP-A) complex (By similarity). Interacts
CC       with RAD51; stimulating HELQ DNA helicase activity and ability to
CC       unwing DNA (By similarity). {ECO:0000250|UniProtKB:Q8TDG4,
CC       ECO:0000269|PubMed:24005329}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDG4}.
CC       Chromosome {ECO:0000250|UniProtKB:Q8TDG4}. Note=Localizes to sites of
CC       DNA damage; localizes to damaged replication forks.
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   -!- DISRUPTION PHENOTYPE: Mice display Fanconi anemia-like phenotypes,
CC       characterized by subfertility, germ cell attrition, interstrand cross-
CC       links (ICLs) sensitivity and cancer susceptibility.
CC       {ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24005329}.
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000305}.
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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   AlphaFoldDB; Q2VPA6; -.
DR   SMR; Q2VPA6; -.
DR   BioGRID; 228629; 5.
DR   STRING; 10090.ENSMUSP00000041599; -.
DR   iPTMnet; Q2VPA6; -.
DR   PhosphoSitePlus; Q2VPA6; -.
DR   EPD; Q2VPA6; -.
DR   MaxQB; Q2VPA6; -.
DR   PaxDb; Q2VPA6; -.
DR   PRIDE; Q2VPA6; -.
DR   ProteomicsDB; 269731; -. [Q2VPA6-1]
DR   ProteomicsDB; 269732; -. [Q2VPA6-2]
DR   ProteomicsDB; 269733; -. [Q2VPA6-3]
DR   Antibodypedia; 25213; 61 antibodies from 16 providers.
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   VEuPathDB; HostDB:ENSMUSG00000035266; -.
DR   eggNOG; KOG0950; Eukaryota.
DR   GeneTree; ENSGT00940000157350; -.
DR   HOGENOM; CLU_006553_1_0_1; -.
DR   InParanoid; Q2VPA6; -.
DR   OMA; MFLNANI; -.
DR   OrthoDB; 179246at2759; -.
DR   PhylomeDB; Q2VPA6; -.
DR   TreeFam; TF105018; -.
DR   BioGRID-ORCS; 191578; 18 hits in 107 CRISPR screens.
DR   ChiTaRS; Helq; mouse.
DR   PRO; PR:Q2VPA6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q2VPA6; protein.
DR   Bgee; ENSMUSG00000035266; Expressed in animal zygote and 162 other tissues.
DR   ExpressionAtlas; Q2VPA6; baseline and differential.
DR   Genevisible; Q2VPA6; MM.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; ISO:MGI.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISS:UniProtKB.
DR   GO; GO:0006259; P:DNA metabolic process; ISO:MGI.
DR   GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; ISS:UniProtKB.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
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; Chromosome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1069
FT                   /note="Helicase POLQ-like"
FT                   /id="PRO_0000329061"
FT   DOMAIN          305..477
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          525..717
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           422..425
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        42..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         318..325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VAR_SEQ         725..766
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11751861"
FT                   /id="VSP_032949"
FT   VAR_SEQ         851..866
FT                   /note="FGQLSPTEQNVAALLG -> VTEQVSWAETSLDFVT (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11751861"
FT                   /id="VSP_032950"
FT   VAR_SEQ         867..1069
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11751861"
FT                   /id="VSP_032951"
FT   VAR_SEQ         884..979
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032952"
FT   CONFLICT        428
FT                   /note="G -> C (in Ref. 1; AAI09170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="L -> Q (in Ref. 3; AAL85275)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        533
FT                   /note="V -> A (in Ref. 3; AAL85275)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="A -> S (in Ref. 1; AAH82601)"
FT                   /evidence="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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