Reviewed, UniProtKB/Swiss-Prot Q9H1I8 (ASCC2_HUMAN)

Names and origin

Protein names

Recommended name:
    Activating signal cointegrator 1 complex subunit 2
Alternative name(s):
    ASC-1 complex subunit p100
    Trip4 complex subunit p100

Gene names

Name:	ASCC2
Synonyms:	ASC1P100

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the ASCC2 family. Contains 1 CUE domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H1I8-1)

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: Q9H1I8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.
     483-484: GE → EK
     485-757: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 757

757

Activating signal cointegrator 1 complex subunit 2

PRO_0000064689

Regions

Domain

467 – 510

44

CUE

Amino acid modifications

Modified residue

713

1

Phosphoserine Ref.5

Natural variations

Alternative sequence

1 – 114

114

Missing in isoform 2.

VSP_011009

Alternative sequence

483 – 484

2

GE → EK in isoform 2.

VSP_011010

Alternative sequence

485 – 757

273

Missing in isoform 2.

VSP_011011

Natural variant

96

1

R → C: dbSNP rs1894473.

VAR_050675

Natural variant

123

1

V → I: dbSNP rs11549795.

VAR_050676

Natural variant

407

1

D → H: dbSNP rs28265.

VAR_025512

Natural variant

423

1

P → S: dbSNP rs36571.

VAR_025513

Natural variant

509

1

R → Q: dbSNP rs4823054. Ref.1

VAR_019464

Natural variant

546

1

D → G: dbSNP rs34833047.

VAR_050677

Natural variant

588

1

E → K: dbSNP rs34062345.

VAR_050678

Natural variant

639

1

R → L: dbSNP rs6006259.

VAR_025514

Experimental info

Sequence conflict

344

1

Q → H in BAB15089. Ref.2

Sequence conflict

526

1

K → N in BAB15089. Ref.2

Sequence conflict

586

1

R → C in BAB15089. Ref.2

Sequence conflict

645

1

P → L in AAG45475. Ref.1

Sequence conflict

653

1

P → L in AAG45475. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

757

Helix Strand Turn

Details...

Helix

467 – 478

12

Helix

487 – 493

7

Turn

494 – 496

3

Helix

498 – 506

9

Turn

512 – 516

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: BB1DCE21E3068E64	FASTA	757	86,360
	10 20 30 40 50 60 MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA LVEEYLERAT 70 80 90 100 110 120 FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR KFDEGVASAP EVVDMQKRLH 130 140 150 160 170 180 RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI 190 200 210 220 230 240 GNIFTQQPSY YSDLDETLPT ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL 250 260 270 280 290 300 ELKDIVLYLC DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE 310 320 330 340 350 360 DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE 370 380 390 400 410 420 KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE SAWEGVDRRK ATDAKDPSVI 430 440 450 460 470 480 EEPNGEPNGV TVTAEAVSQA SSHPENSEEE ECMGAAAAVG PAMCGVELDS LISQVKDLLP 490 500 510 520 530 540 DLGEGFILAC LEYYHYDPEQ VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF 550 560 570 580 590 600 QNDEFDVFSR DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ 610 620 630 640 650 660 PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT KVPREGQEED 670 680 690 700 710 720 DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK GYRHDSSTAV AGSPRGHGQS 730 740 750 RETTQERRKK EANKATRANH NRRTMADRKR SKGMIPS
	Isoform 2. Checksum: A89920B986C9E9B7	FASTA	370	41,794
	10 20 30 40 50 60 MQKRLHRSVF LTFLRMSTHK ESKDHFISPS AFGEILYNNF LFDIPKILDL CVLFGKGNSP 70 80 90 100 110 120 LLQKMIGNIF TQQPSYYSDL DETLPTILQV FSNILQHCGL QGDGANTTPQ KLEERGRLTP 130 140 150 160 170 180 SDMPLLELKD IVLYLCDTCT TLWAFLDIFP LACQTFQKHD FCYRLASFYE AAIPEMESAI 190 200 210 220 230 240 KKRRLEDSKL LGDLWQRLSH SRKKLMEIFH IILNQICLLP ILESSCDNIQ GFIEEFLQIF 250 260 270 280 290 300 SSLLQEKRFL RDYDALFPVA EDISLLQQAS SVLDETRTAY ILQAVESAWE GVDRRKATDA 310 320 330 340 350 360 KDPSVIEEPN GEPNGVTVTA EAVSQASSHP ENSEEEECMG AAAAVGPAMC GVELDSLISQ 370 VKDLLPDLEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT GLN-509, INTERACTION WITH ASCC1 AND ASCC3. Tissue: Cervix carcinoma.
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Colon and Teratocarcinoma.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Solution structure of the CUE domain in the human activating signal cointegrator 1 complex subunit 2 (ASCC2)." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 463-525.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY013289 mRNA. Translation: AAG45475.1.
AK022886 mRNA. Translation: BAB14293.1.
AK025241 mRNA. Translation: BAB15089.1. Different initiation.
Z82171, AC004882 Genomic DNA. Translation: CAI95602.1.
BC025368 mRNA. Translation: AAH25368.1.

IPI

IPI00452803.
IPI00549736.

RefSeq

NP_115580.2.

UniGene

Hs.517438

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DI0	NMR	-	A	463-525	[»]

SMR

Q9H1I8. Positions 463-525.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H1I8. 31 interactions.

STRING

Q9H1I8.

PTM databases

PhosphoSite

Q9H1I8.

Proteomic databases

PeptideAtlas

Q9H1I8.

PRIDE

Q9H1I8.

Genome annotation databases

Ensembl

ENST00000307790; ENSP00000305502; ENSG00000100325; Homo sapiens. [Genome view]
ENST00000397771; ENSP00000380877; ENSG00000100325; Homo sapiens. [Genome view]

GeneID

84164.

KEGG

hsa:84164.

UCSC

uc003agr.1. human.

Organism-specific databases

CTD

84164.

GeneCards

GC22M028512.

H-InvDB

HIX0016358.

HGNC

HGNC:24103. ASCC2.

HPA

HPA001439.

PharmGKB

PA134916940.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9H1I8.

HOVERGEN

Q9H1I8.

OMA

LNQICLL

OrthoDB

EOG9QZB66

Gene expression databases

ArrayExpress

Q9H1I8.

Bgee

Q9H1I8.

CleanEx

HS_ASCC2.

Genevestigator

Q9H1I8.

GermOnline

ENSG00000100325. Homo sapiens.

Family and domain databases

InterPro

IPR003892. CUE.
[Graphical view]

Pfam

PF02845. CUE. 1 hit.
[Graphical view]

SMART

SM00546. CUE. 1 hit.
[Graphical view]

PROSITE

PS51140. CUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

73512.

Entry information

Entry name

ASCC2_HUMAN

Accession

Primary (citable) accession number: Q9H1I8
Secondary accession number(s): Q4TT54 , Q8TAZ0, Q9H711, Q9H9D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 7, 2006
Last modified:	November 24, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.