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Q9H1I8

- ASCC2_HUMAN

UniProt

Q9H1I8 - ASCC2_HUMAN

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Protein

Activating signal cointegrator 1 complex subunit 2

Gene

ASCC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Enhances NF-kappa-B, SRF and AP1 transactivation.

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Activating signal cointegrator 1 complex subunit 2
Alternative name(s):
ASC-1 complex subunit p100
Trip4 complex subunit p100
Gene namesi
Name:ASCC2
Synonyms:ASC1P100
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:24103. ASCC2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134916940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 757757Activating signal cointegrator 1 complex subunit 2PRO_0000064689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei713 – 7131Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H1I8.
PaxDbiQ9H1I8.
PeptideAtlasiQ9H1I8.
PRIDEiQ9H1I8.

PTM databases

PhosphoSiteiQ9H1I8.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9H1I8.
CleanExiHS_ASCC2.
ExpressionAtlasiQ9H1I8. baseline and differential.
GenevestigatoriQ9H1I8.

Organism-specific databases

HPAiHPA001439.

Interactioni

Subunit structurei

Part of TRIP4 complex, that contains ASCC1, ASCC2 and ASCC3. The TRIP4 complex interacts with ALKHB3.2 Publications

Protein-protein interaction databases

BioGridi123921. 41 interactions.
IntActiQ9H1I8. 34 interactions.
MINTiMINT-1182192.
STRINGi9606.ENSP00000305502.

Structurei

Secondary structure

1
757
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi466 – 47813Combined sources
Helixi484 – 49310Combined sources
Turni494 – 4963Combined sources
Helixi498 – 5069Combined sources
Turni512 – 5165Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DI0NMR-A463-526[»]
ProteinModelPortaliQ9H1I8.
SMRiQ9H1I8. Positions 463-525.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H1I8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini467 – 51044CUEPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ASCC2 family.Curated
Contains 1 CUE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG245009.
GeneTreeiENSGT00390000018806.
HOGENOMiHOG000234347.
HOVERGENiHBG050589.
InParanoidiQ9H1I8.
OMAiMPTILQV.
OrthoDBiEOG708VZP.
PhylomeDBiQ9H1I8.
TreeFamiTF323459.

Family and domain databases

InterProiIPR003892. CUE.
IPR009060. UBA-like.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H1I8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA
60 70 80 90 100
LVEEYLERAT FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR
110 120 130 140 150
KFDEGVASAP EVVDMQKRLH RSVFLTFLRM STHKESKDHF ISPSAFGEIL
160 170 180 190 200
YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI GNIFTQQPSY YSDLDETLPT
210 220 230 240 250
ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL ELKDIVLYLC
260 270 280 290 300
DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE
310 320 330 340 350
DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF
360 370 380 390 400
LQIFSSLLQE KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE
410 420 430 440 450
SAWEGVDRRK ATDAKDPSVI EEPNGEPNGV TVTAEAVSQA SSHPENSEEE
460 470 480 490 500
ECMGAAAAVG PAMCGVELDS LISQVKDLLP DLGEGFILAC LEYYHYDPEQ
510 520 530 540 550
VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF QNDEFDVFSR
560 570 580 590 600
DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ
610 620 630 640 650
PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT
660 670 680 690 700
KVPREGQEED DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK
710 720 730 740 750
GYRHDSSTAV AGSPRGHGQS RETTQERRKK EANKATRANH NRRTMADRKR

SKGMIPS
Length:757
Mass (Da):86,360
Last modified:March 7, 2006 - v3
Checksum:iBB1DCE21E3068E64
GO
Isoform 2 (identifier: Q9H1I8-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:370
Mass (Da):41,794
Checksum:iA89920B986C9E9B7
GO
Isoform 3 (identifier: Q9H1I8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-80: Missing.
     137-159: Missing.

Note: No experimental confirmation available.

Show »
Length:681
Mass (Da):77,369
Checksum:iB2D69EB5D82C311E
GO

Sequence cautioni

The sequence BAB15089.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti344 – 3441Q → H in BAB15089. (PubMed:14702039)Curated
Sequence conflicti526 – 5261K → N in BAB15089. (PubMed:14702039)Curated
Sequence conflicti586 – 5861R → C in BAB15089. (PubMed:14702039)Curated
Sequence conflicti639 – 6391R → G in BAH13926. (PubMed:14702039)Curated
Sequence conflicti645 – 6451P → L in AAG45475. (PubMed:12077347)Curated
Sequence conflicti653 – 6531P → L in AAG45475. (PubMed:12077347)Curated
Sequence conflicti661 – 6611D → G in BAH13926. (PubMed:14702039)Curated
Sequence conflicti744 – 7441T → I in BAH13926. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961R → C.
Corresponds to variant rs1894473 [ dbSNP | Ensembl ].
VAR_050675
Natural varianti123 – 1231V → I.
Corresponds to variant rs11549795 [ dbSNP | Ensembl ].
VAR_050676
Natural varianti407 – 4071D → H.
Corresponds to variant rs28265 [ dbSNP | Ensembl ].
VAR_025512
Natural varianti423 – 4231P → S.
Corresponds to variant rs36571 [ dbSNP | Ensembl ].
VAR_025513
Natural varianti509 – 5091R → Q.1 Publication
Corresponds to variant rs4823054 [ dbSNP | Ensembl ].
VAR_019464
Natural varianti546 – 5461D → G.
Corresponds to variant rs34833047 [ dbSNP | Ensembl ].
VAR_050677
Natural varianti588 – 5881E → K.
Corresponds to variant rs34062345 [ dbSNP | Ensembl ].
VAR_050678
Natural varianti639 – 6391R → L.
Corresponds to variant rs6006259 [ dbSNP | Ensembl ].
VAR_025514

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 114114Missing in isoform 2. 1 PublicationVSP_011009Add
BLAST
Alternative sequencei28 – 8053Missing in isoform 3. 1 PublicationVSP_045878Add
BLAST
Alternative sequencei137 – 15923Missing in isoform 3. 1 PublicationVSP_045879Add
BLAST
Alternative sequencei483 – 4842GE → EK in isoform 2. 1 PublicationVSP_011010
Alternative sequencei485 – 757273Missing in isoform 2. 1 PublicationVSP_011011Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY013289 mRNA. Translation: AAG45475.1.
AK022886 mRNA. Translation: BAB14293.1.
AK025241 mRNA. Translation: BAB15089.1. Different initiation.
AK303257 mRNA. Translation: BAH13926.1.
Z82171, AC004882 Genomic DNA. Translation: CAI95602.1.
BC025368 mRNA. Translation: AAH25368.1.
CCDSiCCDS13869.1. [Q9H1I8-1]
CCDS56226.1. [Q9H1I8-3]
RefSeqiNP_001229835.1. NM_001242906.1. [Q9H1I8-3]
NP_115580.2. NM_032204.4. [Q9H1I8-1]
XP_005261832.1. XM_005261775.1. [Q9H1I8-1]
XP_005261833.1. XM_005261776.1. [Q9H1I8-1]
XP_006724397.1. XM_006724334.1. [Q9H1I8-1]
UniGeneiHs.731754.

Genome annotation databases

EnsembliENST00000307790; ENSP00000305502; ENSG00000100325. [Q9H1I8-1]
ENST00000397771; ENSP00000380877; ENSG00000100325. [Q9H1I8-1]
ENST00000542393; ENSP00000437570; ENSG00000100325. [Q9H1I8-3]
GeneIDi84164.
KEGGihsa:84164.
UCSCiuc003agr.3. human. [Q9H1I8-1]

Polymorphism databases

DMDMi92090990.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY013289 mRNA. Translation: AAG45475.1 .
AK022886 mRNA. Translation: BAB14293.1 .
AK025241 mRNA. Translation: BAB15089.1 . Different initiation.
AK303257 mRNA. Translation: BAH13926.1 .
Z82171 , AC004882 Genomic DNA. Translation: CAI95602.1 .
BC025368 mRNA. Translation: AAH25368.1 .
CCDSi CCDS13869.1. [Q9H1I8-1 ]
CCDS56226.1. [Q9H1I8-3 ]
RefSeqi NP_001229835.1. NM_001242906.1. [Q9H1I8-3 ]
NP_115580.2. NM_032204.4. [Q9H1I8-1 ]
XP_005261832.1. XM_005261775.1. [Q9H1I8-1 ]
XP_005261833.1. XM_005261776.1. [Q9H1I8-1 ]
XP_006724397.1. XM_006724334.1. [Q9H1I8-1 ]
UniGenei Hs.731754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DI0 NMR - A 463-526 [» ]
ProteinModelPortali Q9H1I8.
SMRi Q9H1I8. Positions 463-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123921. 41 interactions.
IntActi Q9H1I8. 34 interactions.
MINTi MINT-1182192.
STRINGi 9606.ENSP00000305502.

PTM databases

PhosphoSitei Q9H1I8.

Polymorphism databases

DMDMi 92090990.

Proteomic databases

MaxQBi Q9H1I8.
PaxDbi Q9H1I8.
PeptideAtlasi Q9H1I8.
PRIDEi Q9H1I8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307790 ; ENSP00000305502 ; ENSG00000100325 . [Q9H1I8-1 ]
ENST00000397771 ; ENSP00000380877 ; ENSG00000100325 . [Q9H1I8-1 ]
ENST00000542393 ; ENSP00000437570 ; ENSG00000100325 . [Q9H1I8-3 ]
GeneIDi 84164.
KEGGi hsa:84164.
UCSCi uc003agr.3. human. [Q9H1I8-1 ]

Organism-specific databases

CTDi 84164.
GeneCardsi GC22M030184.
HGNCi HGNC:24103. ASCC2.
HPAi HPA001439.
MIMi 614216. gene.
neXtProti NX_Q9H1I8.
PharmGKBi PA134916940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245009.
GeneTreei ENSGT00390000018806.
HOGENOMi HOG000234347.
HOVERGENi HBG050589.
InParanoidi Q9H1I8.
OMAi MPTILQV.
OrthoDBi EOG708VZP.
PhylomeDBi Q9H1I8.
TreeFami TF323459.

Miscellaneous databases

ChiTaRSi ASCC2. human.
EvolutionaryTracei Q9H1I8.
GeneWikii ASCC2.
GenomeRNAii 84164.
NextBioi 73512.
PROi Q9H1I8.
SOURCEi Search...

Gene expression databases

Bgeei Q9H1I8.
CleanExi HS_ASCC2.
ExpressionAtlasi Q9H1I8. baseline and differential.
Genevestigatori Q9H1I8.

Family and domain databases

InterProi IPR003892. CUE.
IPR009060. UBA-like.
[Graphical view ]
Pfami PF02845. CUE. 1 hit.
[Graphical view ]
SMARTi SM00546. CUE. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS51140. CUE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Colon, Teratocarcinoma and Thymus.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: INTERACTION WITH ALKHB3.
  9. "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.

Entry informationi

Entry nameiASCC2_HUMAN
AccessioniPrimary (citable) accession number: Q9H1I8
Secondary accession number(s): B7Z8E0
, F5H6J9, Q4TT54, Q8TAZ0, Q9H711, Q9H9D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 107 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 22
    Human chromosome 22: 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