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Q8N3C0 (ASCC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activating signal cointegrator 1 complex subunit 3

EC=3.6.4.12
Alternative name(s):
ASC-1 complex subunit p200
Short name=ASC1p200
Helicase, ATP binding 1
Trip4 complex subunit p200
Gene names
Name:ASCC3
Synonyms:HELIC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3, enabling ALKHB3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions. Enhances NF-kappa-B, SRF and AP1 transactivation. Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.10

Subunit structure

Part of TRIP4 complex, that contains ASCC1, ASCC2 and ASCC3. The TRIP4 complex interacts with ALKBH3. Ref.6 Ref.10

Subcellular location

Nucleus. Cytoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the helicase family.

Contains 2 helicase ATP-binding domains.

Contains 2 helicase C-terminal domains.

Contains 2 SEC63 domains.

Sequence caution

The sequence AAG45474.1 differs from that shown. Reason: Frameshift at position 2175.

The sequence CAA11679.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA11679.1 differs from that shown. Reason: Frameshift at position 2175.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N3C0-1)

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: Q8N3C0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     81-111: VGTDNGREAIESGAAFLFMTFHLKDSVGHKE → EVNCPFQKRRLDGKEEDEKMSRASDRFRGLR
     112-2202: Missing.
Isoform 3 (identifier: Q8N3C0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     719-731: MVFVHARNATVRT → HLFYLLLHLFICF
     732-2202: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22022202Activating signal cointegrator 1 complex subunit 3
PRO_0000102093

Regions

Domain486 – 669184Helicase ATP-binding 1
Domain728 – 914187Helicase C-terminal 1
Domain978 – 1287310SEC63 1
Domain1336 – 1511176Helicase ATP-binding 2
Domain1544 – 1739196Helicase C-terminal 2
Domain1812 – 2176365SEC63 2
Nucleotide binding499 – 5068ATP Potential
Nucleotide binding1349 – 13568ATP Potential
Coiled coil18 – 7962 Potential
Coiled coil328 – 35629 Potential
Motif611 – 6144DEVH box
Motif1453 – 14564DEIH box

Amino acid modifications

Modified residue5721N6-acetyllysine Ref.8

Natural variations

Alternative sequence81 – 11131VGTDN…VGHKE → EVNCPFQKRRLDGKEEDEKM SRASDRFRGLR in isoform 2.
VSP_042955
Alternative sequence112 – 22022091Missing in isoform 2.
VSP_042956
Alternative sequence719 – 73113MVFVH…ATVRT → HLFYLLLHLFICF in isoform 3.
VSP_042957
Alternative sequence732 – 22021471Missing in isoform 3.
VSP_042958
Natural variant1461L → F. Ref.1
Corresponds to variant rs9390698 [ dbSNP | Ensembl ].
VAR_034859
Natural variant3441E → K.
Corresponds to variant rs6918004 [ dbSNP | Ensembl ].
VAR_049339
Natural variant4781N → S.
Corresponds to variant rs7750940 [ dbSNP | Ensembl ].
VAR_049340
Natural variant10161S → C.
Corresponds to variant rs57534235 [ dbSNP | Ensembl ].
VAR_061212
Natural variant10501V → I.
Corresponds to variant rs9497983 [ dbSNP | Ensembl ].
VAR_034860
Natural variant14251V → A.
Corresponds to variant rs17246013 [ dbSNP | Ensembl ].
VAR_049341
Natural variant14971R → T.
Corresponds to variant rs17305382 [ dbSNP | Ensembl ].
VAR_049342
Natural variant18001C → W.
Corresponds to variant rs35011147 [ dbSNP | Ensembl ].
VAR_034861
Natural variant19301V → M.
Corresponds to variant rs3213542 [ dbSNP | Ensembl ].
VAR_034862
Natural variant19951S → C. Ref.6 Ref.7
Corresponds to variant rs240780 [ dbSNP | Ensembl ].
VAR_034863
Natural variant21761Y → C.
Corresponds to variant rs240768 [ dbSNP | Ensembl ].
VAR_034864

Experimental info

Mutagenesis13541G → D: Abolishes 3'-5' DNA helicase activity and ability to promote DNA repair. Ref.10
Sequence conflict861G → E in AAH26066. Ref.5
Sequence conflict269 – 2779Missing in CAH73862. Ref.2
Sequence conflict269 – 2779Missing in CAI16190. Ref.2
Sequence conflict269 – 2779Missing in CAI19454. Ref.2
Sequence conflict269 – 2779Missing in CAI19627. Ref.2
Sequence conflict269 – 2779Missing in CAI21439. Ref.2
Sequence conflict4441P → S in CAD39122. Ref.1
Sequence conflict5821V → A in AAH26066. Ref.5
Sequence conflict7501P → S in CAD39122. Ref.1
Sequence conflict11871S → F in CAA11679. Ref.7
Sequence conflict13431C → S in CAA11679. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 11, 2007. Version 3.
Checksum: 9F074E6E5853399C

FASTA2,202251,460
        10         20         30         40         50         60 
MALPRLTGAL RSFSNVTKQD NYNEEVADLK IKRSKLHEQV LDLGLTWKKI IKFLNEKLEK 

        70         80         90        100        110        120 
SKMQSINEDL KDILHAAKQI VGTDNGREAI ESGAAFLFMT FHLKDSVGHK ETKAIKQMFG 

       130        140        150        160        170        180 
PFPSSSATAA CNATNRIISH FSQDDLTALV QMTEKEHGDR VFFGKNLAFS FDMHDLDHFD 

       190        200        210        220        230        240 
ELPINGETQK TISLDYKKFL NEHLQEACTP ELKPVEKTNG SFLWCEVEKY LNSTLKEMTE 

       250        260        270        280        290        300 
VPRVEDLCCT LYDMLASIKS GDELQDELFE LLGPEGLELI EKLLQNRITI VDRFLNSSND 

       310        320        330        340        350        360 
HRFQALQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDLEV 

       370        380        390        400        410        420 
SEGLMCFDPK ELRIQREQAL LNARSVPILS RQRDADVEKI HYPHVYDSQA EAMKTSAFIA 

       430        440        450        460        470        480 
GAKMILPEGI QRENNKLYEE VRIPYSEPMP LSFEEKPVYI QDLDEIGQLA FKGMKRLNRI 

       490        500        510        520        530        540 
QSIVFETAYN TNENMLICAP TGAGKTNIAM LTVLHEIRQH FQQGVIKKNE FKIVYVAPMK 

       550        560        570        580        590        600 
ALAAEMTDYF SRRLEPLGII VKELTGDMQL SKSEILRTQM LVTTPEKWDV VTRKSVGDVA 

       610        620        630        640        650        660 
LSQIVRLLIL DEVHLLHEDR GPVLESIVAR TLRQVESTQS MIRILGLSAT LPNYLDVATF 

       670        680        690        700        710        720 
LHVNPYIGLF FFDGRFRPVP LGQTFLGIKC ANKMQQLNNM DEVCYENVLK QVKAGHQVMV 

       730        740        750        760        770        780 
FVHARNATVR TAMSLIERAK NCGHIPFFFP TQGHDYVLAE KQVQRSRNKQ VRELFPDGFS 

       790        800        810        820        830        840 
IHHAGMLRQD RNLVENLFSN GHIKVLVCTA TLAWGVNLPA HAVIIKGTQI YAAKRGSFVD 

       850        860        870        880        890        900 
LGILDVMQIF GRAGRPQFDK FGEGIIITTH DKLSHYLTLL TQRNPIESQF LESLADNLNA 

       910        920        930        940        950        960 
EIALGTVTNV EEAVKWISYT YLYVRMRANP LAYGISHKAY QIDPTLRKHR EQLVIEVGRK 

       970        980        990       1000       1010       1020 
LDKAQMIRFE ERTGYFSSTD LGRTASHYYI KYNTIETFNE LFDAHKTEGD IFAIVSKAEE 

      1030       1040       1050       1060       1070       1080 
FDQIKVREEE IEELDTLLSN FCELSTPGGV ENSYGKINIL LQTYISRGEM DSFSLISDSA 

      1090       1100       1110       1120       1130       1140 
YVAQNAARIV RALFEIALRK RWPTMTYRLL NLSKVIDKRL WGWASPLRQF SILPPHILTR 

      1150       1160       1170       1180       1190       1200 
LEEKKLTVDK LKDMRKDEIG HILHHVNIGL KVKQCVHQIP SVMMEASIQP ITRTVLRVTL 

      1210       1220       1230       1240       1250       1260 
SIYADFTWND QVHGTVGEPW WIWVEDPTND HIYHSEYFLA LKKQVISKEA QLLVFTIPIF 

      1270       1280       1290       1300       1310       1320 
EPLPSQYYIR AVSDRWLGAE AVCIINFQHL ILPERHPPHT ELLDLQPLPI TALGCKAYEA 

      1330       1340       1350       1360       1370       1380 
LYNFSHFNPV QTQIFHTLYH TDCNVLLGAP TGSGKTVAAE LAIFRVFNKY PTSKAVYIAP 

      1390       1400       1410       1420       1430       1440 
LKALVRERMD DWKVRIEEKL GKKVIELTGD VTPDMKSIAK ADLIVTTPEK WDGVSRSWQN 

      1450       1460       1470       1480       1490       1500 
RNYVQQVTIL IIDEIHLLGE ERGPVLEVIV SRTNFISSHT EKPVRIVGLS TALANARDLA 

      1510       1520       1530       1540       1550       1560 
DWLNIKQMGL FNFRPSVRPV PLEVHIQGFP GQHYCPRMAS MNKPAFQAIR SHSPAKPVLI 

      1570       1580       1590       1600       1610       1620 
FVSSRRQTRL TALELIAFLA TEEDPKQWLN MDEREMENII ATVRDSNLKL TLAFGIGMHH 

      1630       1640       1650       1660       1670       1680 
AGLHERDRKT VEELFVNCKV QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI 

      1690       1700       1710       1720       1730       1740 
TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA 

      1750       1760       1770       1780       1790       1800 
GGTITSKQDA LDYITWTYFF RRLIMNPSYY NLGDVSHDSV NKFLSHLIEK SLIELELSYC 

      1810       1820       1830       1840       1850       1860 
IEIGEDNRSI EPLTYGRIAS YYYLKHQTVK MFKDRLKPEC STEELLSILS DAEEYTDLPV 

      1870       1880       1890       1900       1910       1920 
RHNEDHMNSE LAKCLPIESN PHSFDSPHTK AHLLLQAHLS RAMLPCPDYD TDTKTVLDQA 

      1930       1940       1950       1960       1970       1980 
LRVCQAMLDV AANQGWLVTV LNITNLIQMV IQGRWLKDSS LLTLPNIENH HLHLFKKWKP 

      1990       2000       2010       2020       2030       2040 
IMKGPHARGR TSIESLPELI HACGGKDHVF SSMVESELHA AKTKQAWNFL SHLPVINVGI 

      2050       2060       2070       2080       2090       2100 
SVKGSWDDLV EGHNELSVST LTADKRDDNK WIKLHADQEY VLQVSLQRVH FGFHKGKPES 

      2110       2120       2130       2140       2150       2160 
CAVTPRFPKS KDEGWFLILG EVDKRELIAL KRVGYIRNHH VASLSFYTPE IPGRYIYTLY 

      2170       2180       2190       2200 
FMSDCYLGLD QQYDIYLNVT QASLSAQVNT KVSDSLTDLA LK 

« Hide

Isoform 2 [UniParc].

Checksum: F3D84693464682F3
Show »

FASTA11113,014
Isoform 3 [UniParc].

Checksum: E82CDB32BEC21AF3
Show »

FASTA73183,675

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-146.
Tissue: Melanoma.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Thymus.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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].
[5]"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 2 AND 3).
Tissue: Skin and Testis.
[6]"Novel transcription coactivator complex containing activating signal cointegrator 1."
Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.
Mol. Cell. Biol. 22:5203-5211(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 277-2202, PARTIAL PROTEIN SEQUENCE, VARIANT CYS-1995, INTERACTION WITH ASCC1 AND ASCC2.
Tissue: Cervix carcinoma.
[7]"The immunodominant antigen recognized by autologous CTL on a human melanoma is generated by a point mutation in a new member of the RNA helicase gene family."
Baurain J.-F.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1012-2202, VARIANT CYS-1995.
Tissue: Melanoma.
[8]"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-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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].
[10]"DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation."
Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K., Rubin M., Gygi S., Harper J.W., Shi Y.
Mol. Cell 44:373-384(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ALKBH3, MUTAGENESIS OF GLY-1354.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL834463 mRNA. Translation: CAD39122.1.
AK315197 mRNA. Translation: BAG37637.1.
AL591585 expand/collapse EMBL AC list , AL121965, AL133338, AL356122, Z86062 Genomic DNA. Translation: CAH73862.1.
AL356122 expand/collapse EMBL AC list , AL121965, AL133338, AL591585, Z86062 Genomic DNA. Translation: CAI16190.1.
Z86062 expand/collapse EMBL AC list , AL121965, AL133338, AL356122, AL591585 Genomic DNA. Translation: CAI19454.1.
AL121965 expand/collapse EMBL AC list , AL133338, AL356122, AL591585, Z86062 Genomic DNA. Translation: CAI19627.1.
AL133338 expand/collapse EMBL AC list , AL121965, AL356122, AL591585, Z86062 Genomic DNA. Translation: CAI21439.1.
AL133338 Genomic DNA. Translation: CAC07337.1.
CH471051 Genomic DNA. Translation: EAW48449.1.
BC050681 mRNA. Translation: AAH50681.1.
BC125211 mRNA. Translation: AAI25212.1.
BC125212 mRNA. Translation: AAI25213.1.
BC026066 mRNA. Translation: AAH26066.1.
AY013288 mRNA. Translation: AAG45474.1. Frameshift.
AJ223948 mRNA. Translation: CAA11679.1. Sequence problems.
CCDSCCDS5046.1. [Q8N3C0-1]
CCDS5047.1. [Q8N3C0-3]
RefSeqNP_001271200.1. NM_001284271.1. [Q8N3C0-4]
NP_006819.2. NM_006828.3. [Q8N3C0-1]
NP_071374.1. NM_022091.4. [Q8N3C0-3]
UniGeneHs.486031.
Hs.733060.

3D structure databases

ProteinModelPortalQ8N3C0.
SMRQ8N3C0. Positions 472-925, 971-1280, 1327-2182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116170. 16 interactions.
IntActQ8N3C0. 7 interactions.
MINTMINT-1183138.
STRING9606.ENSP00000320252.

PTM databases

PhosphoSiteQ8N3C0.

Polymorphism databases

DMDM158518649.

Proteomic databases

MaxQBQ8N3C0.
PaxDbQ8N3C0.
PRIDEQ8N3C0.

Protocols and materials databases

DNASU10973.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369143; ENSP00000358139; ENSG00000112249. [Q8N3C0-3]
ENST00000369162; ENSP00000358159; ENSG00000112249. [Q8N3C0-1]
ENST00000522650; ENSP00000430769; ENSG00000112249. [Q8N3C0-4]
GeneID10973.
KEGGhsa:10973.
UCSCuc003pqk.3. human. [Q8N3C0-1]
uc003pql.3. human. [Q8N3C0-4]
uc003pqm.3. human. [Q8N3C0-3]

Organism-specific databases

CTD10973.
GeneCardsGC06M100956.
H-InvDBHIX0021958.
HGNCHGNC:18697. ASCC3.
HPAHPA031608.
HPA031609.
HPA031610.
MIM614217. gene.
neXtProtNX_Q8N3C0.
PharmGKBPA134890913.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1204.
HOGENOMHOG000152625.
HOVERGENHBG051896.
InParanoidQ8N3C0.
KOK01529.
OMAVHMLHDE.
OrthoDBEOG7PGDPQ.
PhylomeDBQ8N3C0.
TreeFamTF105778.

Gene expression databases

ArrayExpressQ8N3C0.
BgeeQ8N3C0.
CleanExHS_ASCC3.
GenevestigatorQ8N3C0.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProIPR003593. AAA+_ATPase.
IPR000008. C2_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
[Graphical view]
PfamPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 2 hits.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM00487. DEXDc. 2 hits.
SM00490. HELICc. 2 hits.
SM00611. SEC63. 2 hits.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSASCC3. human.
GeneWikiASCC3.
GenomeRNAi10973.
NextBio41694.
PROQ8N3C0.
SOURCESearch...

Entry information

Entry nameASCC3_HUMAN
AccessionPrimary (citable) accession number: Q8N3C0
Secondary accession number(s): E7EW23 expand/collapse secondary AC list , O43738, Q4G1A0, Q5VTN2, Q9H1I9, Q9H5A2, Q9NTR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM