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Q9H1I8

- ASCC2_HUMAN

UniProt

Q9H1I8 - ASCC2_HUMAN

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
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    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

    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

    ArrayExpressiQ9H1I8.
    BgeeiQ9H1I8.
    CleanExiHS_ASCC2.
    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. 39 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 – 47813
    Helixi484 – 49310
    Turni494 – 4963
    Helixi498 – 5069
    Turni512 – 5165

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA    50
    LVEEYLERAT FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR 100
    KFDEGVASAP EVVDMQKRLH RSVFLTFLRM STHKESKDHF ISPSAFGEIL 150
    YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI GNIFTQQPSY YSDLDETLPT 200
    ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL ELKDIVLYLC 250
    DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE 300
    DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF 350
    LQIFSSLLQE KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE 400
    SAWEGVDRRK ATDAKDPSVI EEPNGEPNGV TVTAEAVSQA SSHPENSEEE 450
    ECMGAAAAVG PAMCGVELDS LISQVKDLLP DLGEGFILAC LEYYHYDPEQ 500
    VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF QNDEFDVFSR 550
    DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ 600
    PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT 650
    KVPREGQEED DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK 700
    GYRHDSSTAV AGSPRGHGQS RETTQERRKK EANKATRANH NRRTMADRKR 750
    SKGMIPS 757
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 39 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.
    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

    ArrayExpressi Q9H1I8.
    Bgeei Q9H1I8.
    CleanExi HS_ASCC2.
    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

    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: October 1, 2014
    This is version 105 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