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P46063

- RECQ1_HUMAN

UniProt

P46063 - RECQ1_HUMAN

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Protein
ATP-dependent DNA helicase Q1
Gene
RECQL, RECQ1, RECQL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi113 – 1208ATP Inferred

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent 3'-5' DNA helicase activity Source: InterPro
  3. ATP-dependent DNA helicase activity Source: ProtInc
  4. DNA binding Source: UniProtKB-KW
  5. DNA helicase activity Source: UniProtKB
  6. annealing helicase activity Source: UniProtKB
  7. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA duplex unwinding Source: GOC
  2. DNA recombination Source: InterPro
  3. DNA repair Source: ProtInc
  4. DNA replication Source: InterPro
  5. DNA strand renaturation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase Q1 (EC:3.6.4.12)
Alternative name(s):
DNA helicase, RecQ-like type 1
Short name:
RecQ1
DNA-dependent ATPase Q1
RecQ protein-like 1
Gene namesi
Name:RECQL
Synonyms:RECQ1, RECQL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9948. RECQL.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191K → A: Abrogates helicase activity. 1 Publication

Organism-specific databases

PharmGKBiPA34315.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649ATP-dependent DNA helicase Q1
PRO_0000205049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei514 – 5141N6-acetyllysine1 Publication
Modified residuei522 – 5221N6-acetyllysine1 Publication
Modified residuei634 – 6341Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46063.
PaxDbiP46063.
PRIDEiP46063.

PTM databases

PhosphoSiteiP46063.

Expressioni

Tissue specificityi

High expression in heart, lung, skeletal muscle and kidney, low expression in brain.1 Publication

Gene expression databases

ArrayExpressiP46063.
BgeeiP46063.
CleanExiHS_RECQL.
GenevestigatoriP46063.

Organism-specific databases

HPAiCAB009743.
HPA030960.

Interactioni

Subunit structurei

Interacts with EXO1 and MLH1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA2P522922EBI-2823728,EBI-349938
KPNA4O006292EBI-2823728,EBI-396343

Protein-protein interaction databases

BioGridi111897. 11 interactions.
DIPiDIP-29216N.
IntActiP46063. 5 interactions.
MINTiMINT-3016374.
STRINGi9606.ENSP00000395449.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 684
Helixi76 – 8510
Helixi96 – 1049
Beta strandi109 – 1124
Helixi121 – 1288
Beta strandi130 – 1378
Helixi141 – 15414
Beta strandi158 – 1603
Helixi167 – 17812
Beta strandi186 – 1894
Helixi191 – 1955
Helixi198 – 20912
Beta strandi213 – 2197
Helixi221 – 2244
Helixi226 – 2283
Helixi233 – 2397
Helixi240 – 2445
Beta strandi248 – 2569
Helixi259 – 26810
Beta strandi275 – 2784
Beta strandi286 – 2927
Helixi297 – 30812
Turni309 – 3146
Beta strandi316 – 3205
Helixi324 – 33613
Beta strandi341 – 3444
Helixi350 – 36112
Beta strandi364 – 3707
Beta strandi383 – 3908
Helixi395 – 4028
Beta strandi412 – 4187
Helixi420 – 42910
Turni430 – 4323
Helixi436 – 44712
Beta strandi450 – 4523
Helixi454 – 4629
Helixi476 – 4794
Beta strandi484 – 4885
Helixi490 – 50516
Helixi512 – 5198
Helixi525 – 5273
Helixi539 – 55113
Beta strandi554 – 5618
Beta strandi566 – 5727
Helixi574 – 5807
Beta strandi587 – 5915

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V1XX-ray2.00A/B49-615[»]
2WWYX-ray2.90A/B49-616[»]
ProteinModelPortaliP46063.
SMRiP46063. Positions 64-593.

Miscellaneous databases

EvolutionaryTraceiP46063.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 275176Helicase ATP-binding
Add
BLAST
Domaini300 – 451152Helicase C-terminal
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi219 – 2224DEVH box

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0514.
HOGENOMiHOG000044388.
HOVERGENiHBG057654.
InParanoidiP46063.
KOiK10899.
OMAiQKFRPLQ.
OrthoDBiEOG7K0ZC0.
PhylomeDBiP46063.
TreeFamiTF323555.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46063-1 [UniParc]FASTAAdd to Basket

« Hide

MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL    50
EDSDAGASNE YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI 100
NVTMAGKEVF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV 150
LKQLGISATM LNASSSKEHV KWVHAEMVNK NSELKLIYVT PEKIAKSKMF 200
MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL 250
IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF 300
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP 350
EDKTTVHRKW SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ 400
ESGRAGRDDM KADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNI 450
SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK DSAFERKNIT EYCRDLIKIL 500
KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE DLEKIIAHFL 550
IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA 600
ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA 649
Length:649
Mass (Da):73,457
Last modified:December 16, 2008 - v3
Checksum:iF616DC3191F79391
GO

Sequence cautioni

The sequence AAA60261.1 differs from that shown. Reason: Frameshift at positions 615 and 649.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021V → I.
Corresponds to variant rs1065751 [ dbSNP | Ensembl ].
VAR_034679
Natural varianti372 – 3721V → I.
Corresponds to variant rs2230003 [ dbSNP | Ensembl ].
VAR_051732
Natural varianti487 – 4871K → T.1 Publication
Corresponds to variant rs6501 [ dbSNP | Ensembl ].
VAR_016140
Natural varianti495 – 4951D → H.
Corresponds to variant rs6499 [ dbSNP | Ensembl ].
VAR_016141

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → S in BAA07200. 1 Publication
Sequence conflicti175 – 1751A → D in AAA60261. 1 Publication
Sequence conflicti453 – 4531C → S in AAA60261. 1 Publication
Sequence conflicti566 – 5661T → A in AAA60261. 1 Publication
Sequence conflicti617 – 6171E → K in AAP35783. 1 Publication
Sequence conflicti617 – 6171E → K in AAH01052. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36140 mRNA. Translation: AAA60261.1. Frameshift.
D37984 mRNA. Translation: BAA07200.1.
BT007119 mRNA. Translation: AAP35783.1.
AK291627 mRNA. Translation: BAF84316.1.
AC006559 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96434.1.
BC001052 mRNA. Translation: AAH01052.1.
CCDSiCCDS31756.1.
PIRiA58836. A55311.
RefSeqiNP_002898.2. NM_002907.3.
NP_116559.1. NM_032941.2.
XP_005253518.1. XM_005253461.2.
XP_005253519.1. XM_005253462.2.
XP_005253520.1. XM_005253463.1.
XP_005253521.1. XM_005253464.1.
XP_006719196.1. XM_006719133.1.
UniGeneiHs.235069.

Genome annotation databases

EnsembliENST00000421138; ENSP00000395449; ENSG00000004700.
ENST00000444129; ENSP00000416739; ENSG00000004700.
GeneIDi5965.
KEGGihsa:5965.
UCSCiuc001rex.3. human.

Polymorphism databases

DMDMi218512113.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36140 mRNA. Translation: AAA60261.1 . Frameshift.
D37984 mRNA. Translation: BAA07200.1 .
BT007119 mRNA. Translation: AAP35783.1 .
AK291627 mRNA. Translation: BAF84316.1 .
AC006559 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96434.1 .
BC001052 mRNA. Translation: AAH01052.1 .
CCDSi CCDS31756.1.
PIRi A58836. A55311.
RefSeqi NP_002898.2. NM_002907.3.
NP_116559.1. NM_032941.2.
XP_005253518.1. XM_005253461.2.
XP_005253519.1. XM_005253462.2.
XP_005253520.1. XM_005253463.1.
XP_005253521.1. XM_005253464.1.
XP_006719196.1. XM_006719133.1.
UniGenei Hs.235069.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V1X X-ray 2.00 A/B 49-615 [» ]
2WWY X-ray 2.90 A/B 49-616 [» ]
ProteinModelPortali P46063.
SMRi P46063. Positions 64-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111897. 11 interactions.
DIPi DIP-29216N.
IntActi P46063. 5 interactions.
MINTi MINT-3016374.
STRINGi 9606.ENSP00000395449.

Chemistry

ChEMBLi CHEMBL1293236.

PTM databases

PhosphoSitei P46063.

Polymorphism databases

DMDMi 218512113.

Proteomic databases

MaxQBi P46063.
PaxDbi P46063.
PRIDEi P46063.

Protocols and materials databases

DNASUi 5965.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000421138 ; ENSP00000395449 ; ENSG00000004700 .
ENST00000444129 ; ENSP00000416739 ; ENSG00000004700 .
GeneIDi 5965.
KEGGi hsa:5965.
UCSCi uc001rex.3. human.

Organism-specific databases

CTDi 5965.
GeneCardsi GC12M021621.
H-InvDB HIX0010478.
HGNCi HGNC:9948. RECQL.
HPAi CAB009743.
HPA030960.
MIMi 600537. gene.
neXtProti NX_P46063.
PharmGKBi PA34315.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0514.
HOGENOMi HOG000044388.
HOVERGENi HBG057654.
InParanoidi P46063.
KOi K10899.
OMAi QKFRPLQ.
OrthoDBi EOG7K0ZC0.
PhylomeDBi P46063.
TreeFami TF323555.

Miscellaneous databases

ChiTaRSi RECQL. human.
EvolutionaryTracei P46063.
GeneWikii RECQL.
GenomeRNAii 5965.
NextBioi 23220.
PROi P46063.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46063.
Bgeei P46063.
CleanExi HS_RECQL.
Genevestigatori P46063.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of RECQL, a potential human homologue of the Escherichia coli DNA helicase RecQ."
    Puranam K.L., Blackshear P.J.
    J. Biol. Chem. 269:29838-29845(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-38; 186-193; 293-304; 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT THR-487.
    Tissue: Cervix carcinoma.
  2. "Molecular cloning of cDNA encoding human DNA helicase Q1 which has homology to Escherichia coli Rec Q helicase and localization of the gene at chromosome 12p12."
    Seki M., Miyazawa H., Tada S., Yanagisawa J., Yamaoka T., Hoshino S., Ozawa K., Eki T., Nogami M., Okumura K., Taguchi H., Hanaoka F., Enomoto T.
    Nucleic Acids Res. 22:4566-4573(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Lung.
  8. "Purification of two DNA-dependent adenosinetriphosphatases having DNA helicase activity from HeLa cells and comparison of the properties of the two enzymes."
    Seki M., Yanagisawa J., Kohda T., Sonoyama T., Ui M., Enomoto T.
    J. Biochem. 115:523-531(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "RECQ1 helicase interacts with human mismatch repair factors that regulate genetic recombination."
    Doherty K.M., Sharma S., Uzdilla L.A., Wilson T.M., Cui S., Vindigni A., Brosh R.M. Jr.
    J. Biol. Chem. 280:28085-28094(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EXO1 AND MLH1, MUTAGENESIS OF LYS-119.
  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-514 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRECQ1_HUMAN
AccessioniPrimary (citable) accession number: P46063
Secondary accession number(s): A8K6G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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