Q8N3C0 (HELC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Activating signal cointegrator 1 complex subunit 3
EC=3.6.4.-

Alternative name(s):
ASC-1 complex subunit p200
Helicase, ATP binding 1
Trip4 complex subunit p200

Gene names

Name:	ASCC3
Synonyms:	HELIC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Enhances NF-kappa-B, SRF and AP1 transactivation.
Subunit structure	Part of TRIP4 complex, that contains ASCC1, ASCC2 and ASCC3.
Subcellular location	Cytoplasm.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the helicase family. Contains 2 helicase ATP-binding domains. Contains 2 helicase C-terminal domains. Contains 3 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2202	2202	Activating signal cointegrator 1 complex subunit 3		PRO_0000102093
Regions
	Domain	486 – 669	184	Helicase ATP-binding 1
	Domain	728 – 914	187	Helicase C-terminal 1
	Domain	978 – 1287	310	SEC63 1
	Domain	1336 – 1511	176	Helicase ATP-binding 2
	Domain	1544 – 1739	196	Helicase C-terminal 2
	Domain	1812 – 1972	161	SEC63 2
	Domain	2103 – 2177	75	SEC63 3
	Nucleotide binding	499 – 506	8	ATP Potential
	Nucleotide binding	1349 – 1356	8	ATP Potential
	Coiled coil	18 – 79	62	Potential
	Coiled coil	328 – 356	29	Potential
	Motif	611 – 614	4	DEVH box
	Motif	1453 – 1456	4	DEIH box
Amino acid modifications
	Modified residue	234	1	Phosphothreonine Ref.5
	Modified residue	572	1	N6-acetyllysine Ref.6
Natural variations
	Natural variant	146	1	L → F. Ref.1 Corresponds to variant rs9390698 [ dbSNP | Ensembl ].		VAR_034859
	Natural variant	344	1	E → K. Corresponds to variant rs6918004 [ dbSNP | Ensembl ].		VAR_049339
	Natural variant	478	1	N → S. Corresponds to variant rs7750940 [ dbSNP | Ensembl ].		VAR_049340
	Natural variant	1016	1	S → C. Corresponds to variant rs57534235 [ dbSNP | Ensembl ].		VAR_061212
	Natural variant	1050	1	V → I. Corresponds to variant rs9497983 [ dbSNP | Ensembl ].		VAR_034860
	Natural variant	1425	1	V → A. Corresponds to variant rs17246013 [ dbSNP | Ensembl ].		VAR_049341
	Natural variant	1497	1	R → T. Corresponds to variant rs17305382 [ dbSNP | Ensembl ].		VAR_049342
	Natural variant	1800	1	C → W. Corresponds to variant rs35011147 [ dbSNP | Ensembl ].		VAR_034861
	Natural variant	1930	1	V → M. Corresponds to variant rs3213542 [ dbSNP | Ensembl ].		VAR_034862
	Natural variant	1995	1	S → C. Ref.3 Ref.4 Corresponds to variant rs240780 [ dbSNP | Ensembl ].		VAR_034863
	Natural variant	2176	1	Y → C. Corresponds to variant rs240768 [ dbSNP | Ensembl ].		VAR_034864
Experimental info
	Sequence conflict	269 – 277	9	Missing in CAH73862. Ref.2
	Sequence conflict	269 – 277	9	Missing in CAI16190. Ref.2
	Sequence conflict	269 – 277	9	Missing in CAI19454. Ref.2
	Sequence conflict	269 – 277	9	Missing in CAI19627. Ref.2
	Sequence conflict	269 – 277	9	Missing in CAI21439. Ref.2
	Sequence conflict	444	1	P → S in CAD39122. Ref.1
	Sequence conflict	750	1	P → S in CAD39122. Ref.1
	Sequence conflict	1187	1	S → F in CAA11679. Ref.4
	Sequence conflict	1343	1	C → S in CAA11679. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8N3C0 [UniParc]. Last modified September 11, 2007. Version 3. Checksum: 9F074E6E5853399C	FASTA	2,202	251,460
	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

References

	« Hide 'large scale' referencesShow '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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-146. Tissue: Melanoma.
[2]	"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. , 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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 12077347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 277-2202, PARTIAL PROTEIN SEQUENCE, VARIANT CYS-1995, INTERACTION WITH ASCC1 AND ASCC2. Tissue: Cervix carcinoma.
[4]	"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.
[5]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-572, MASS SPECTROMETRY.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL834463 mRNA. Translation: CAD39122.1. AL591585 , AL121965, AL133338, AL356122, Z86062 Genomic DNA. Translation: CAH73862.1. AL356122 , AL121965, AL133338, AL591585, Z86062 Genomic DNA. Translation: CAI16190.1. Z86062 , AL121965, AL133338, AL356122, AL591585 Genomic DNA. Translation: CAI19454.1. AL121965 , AL133338, AL356122, AL591585, Z86062 Genomic DNA. Translation: CAI19627.1. AL133338 , AL121965, AL356122, AL591585, Z86062 Genomic DNA. Translation: CAI21439.1. AY013288 mRNA. Translation: AAG45474.1. Frameshift. AJ223948 mRNA. Translation: CAA11679.1. Sequence problems.
IPI	IPI00430472.
RefSeq	NP_006819.2. NM_006828.2.
UniGene	Hs.486031.
3D structure databases
ProteinModelPortal	Q8N3C0.
SMR	Q8N3C0. Positions 463-1163, 1272-2182.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N3C0. 6 interactions.
MINT	MINT-1183138.
STRING	Q8N3C0.
PTM databases
PhosphoSite	Q8N3C0.
Polymorphism databases
DMDM	158518649.
Proteomic databases
PRIDE	Q8N3C0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324696; ENSP00000320252; ENSG00000112249.
GeneID	10973.
KEGG	hsa:10973.
UCSC	uc003pqk.1. human.
Organism-specific databases
CTD	10973.
GeneCards	GC06M100956.
H-InvDB	HIX0021958.
HGNC	HGNC:18697. ASCC3.
HPA	HPA031608. HPA031609. HPA031610.
MIM	614217. gene.
neXtProt	NX_Q8N3C0.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04583.
GeneTree	ENSGT00550000074613.
HOGENOM	HBG736699.
HOVERGEN	HBG051896.
InParanoid	Q8N3C0.
OMA	FPGKHYC.
PhylomeDB	Q8N3C0.
Gene expression databases
ArrayExpress	Q8N3C0.
Bgee	Q8N3C0.
CleanEx	HS_ASCC3.
Genevestigator	Q8N3C0.
GermOnline	ENSG00000112249. Homo sapiens.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR014001. DEAD-like_helicase. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR001650. Helicase_C. IPR004179. Sec63-dom. [Graphical view]
KO	K01529.
Pfam	PF00270. DEAD. 2 hits. PF00271. Helicase_C. 2 hits. PF02889. Sec63. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. SM00487. DEXDc. 2 hits. SM00490. HELICc. 2 hits. SM00611. SEC63. 2 hits. SM00973. Sec63. 2 hits. [Graphical view]
PROSITE	PS51192. HELICASE_ATP_BIND_1. 2 hits. PS51194. HELICASE_CTER. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	41694.
SOURCE	Search...

Entry information

Entry name

HELC1_HUMAN

Accession

Primary (citable) accession number: Q8N3C0
Secondary accession number(s): O43738 , Q5VTN2, Q9H1I9, Q9NTR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.