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Q9H6T3

- RPAP3_HUMAN

UniProt

Q9H6T3 - RPAP3_HUMAN

Protein

RNA polymerase II-associated protein 3

Gene

RPAP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II-associated protein 3
    Gene namesi
    Name:RPAP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:26151. RPAP3.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162401982.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 665664RNA polymerase II-associated protein 3PRO_0000302794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei87 – 871Phosphoserine1 Publication
    Modified residuei116 – 1161Phosphoserine2 Publications
    Modified residuei119 – 1191Phosphoserine2 Publications
    Modified residuei121 – 1211Phosphoserine2 Publications
    Modified residuei481 – 4811Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H6T3.
    PaxDbiQ9H6T3.
    PRIDEiQ9H6T3.

    PTM databases

    PhosphoSiteiQ9H6T3.

    Miscellaneous databases

    PMAP-CutDBQ9H6T3.

    Expressioni

    Gene expression databases

    BgeeiQ9H6T3.
    CleanExiHS_RPAP3.
    GenevestigatoriQ9H6T3.

    Organism-specific databases

    HPAiHPA038311.
    HPA038312.

    Interactioni

    Subunit structurei

    Tightly associated with the RNA polymerase II complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AA1P079003EBI-356928,EBI-296047
    PFDN2Q9UHV92EBI-356928,EBI-359873
    URI1O947632EBI-356928,EBI-357067
    UXTQ9UBK92EBI-356928,EBI-357355
    WDR92Q96MX65EBI-356928,EBI-2434101

    Protein-protein interaction databases

    BioGridi122783. 50 interactions.
    IntActiQ9H6T3. 32 interactions.
    MINTiMINT-1140426.
    STRINGi9606.ENSP00000005386.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi130 – 14516
    Helixi149 – 16214
    Helixi168 – 17912
    Helixi183 – 19614
    Helixi201 – 21313
    Helixi217 – 23014
    Helixi235 – 24915
    Helixi268 – 27710
    Helixi278 – 2803
    Helixi281 – 29414
    Helixi298 – 31013
    Helixi317 – 32812
    Helixi333 – 34513
    Helixi350 – 36314
    Helixi366 – 37914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CGVX-ray2.54A/B/C/D120-255[»]
    4CGWX-ray3.00A/B265-381[»]
    ProteinModelPortaliQ9H6T3.
    SMRiQ9H6T3. Positions 89-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati8 – 4134TPR 1Add
    BLAST
    Repeati133 – 16634TPR 2Add
    BLAST
    Repeati168 – 20033TPR 3Add
    BLAST
    Repeati201 – 23434TPR 4Add
    BLAST
    Repeati282 – 31534TPR 5Add
    BLAST
    Repeati317 – 34933TPR 6Add
    BLAST
    Repeati350 – 38334TPR 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 708Poly-Lys

    Sequence similaritiesi

    Belongs to the RPAP3 family.Curated
    Contains 7 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000154181.
    HOVERGENiHBG059892.
    InParanoidiQ9H6T3.
    OMAiECYTRGM.
    OrthoDBiEOG7KSX8F.
    PhylomeDBiQ9H6T3.
    TreeFamiTF106243.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR025986. RPAP3-like_C.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF13877. RPAP3_C. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 6 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H6T3-1) [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

    MTSANKAIEL QLQVKQNAEE LQDFMRDLEN WEKDIKQKDM ELRRQNGVPE    50
    ENLPPIRNGN FRKKKKGKAK ESSKKTREEN TKNRIKSYDY EAWAKLDVDR 100
    ILDELDKDDS THESLSQESE SEEDGIHVDS QKALVLKEKG NKYFKQGKYD 150
    EAIDCYTKGM DADPYNPVLP TNRASAYFRL KKFAVAESDC NLAVALNRSY 200
    TKAYSRRGAA RFALQKLEEA KKDYERVLEL EPNNFEATNE LRKISQALAS 250
    KENSYPKEAD IVIKSTEGER KQIEAQQNKQ QAISEKDRGN GFFKEGKYER 300
    AIECYTRGIA ADGANALLPA NRAMAYLKIQ KYEEAEKDCT QAILLDGSYS 350
    KAFARRGTAR TFLGKLNEAK QDFETVLLLE PGNKQAVTEL SKIKKELIEK 400
    GHWDDVFLDS TQRQNVVKPI DNPPHPGSTK PLKKVIIEET GNLIQTIDVP 450
    DSTTAAAPEN NPINLANVIA ATGTTSKKNS SQDDLFPTSD TPRAKVLKIE 500
    EVSDTSSLQP QASLKQDVCQ SYSEKMPIEI EQKPAQFATT VLPPIPANSF 550
    QLESDFRQLK SSPDMLYQYL KQIEPSLYPK LFQKNLDPDV FNQIVKILHD 600
    FYIEKEKPLL IFEILQRLSE LKRFDMAVMF MSETEKKIAR ALFNHIDKSG 650
    LKDSSVEELK KRYGG 665
    Length:665
    Mass (Da):75,719
    Last modified:September 11, 2007 - v2
    Checksum:i70D5A965E4F1EE35
    GO
    Isoform 2 (identifier: Q9H6T3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         396-429: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:631
    Mass (Da):71,866
    Checksum:iB175E5AE9E55FC08
    GO
    Isoform 3 (identifier: Q9H6T3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-159: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:506
    Mass (Da):57,108
    Checksum:i5E45C03E06E599EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti484 – 4841D → V in BAB15170. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti564 – 5641D → Y.
    Corresponds to variant rs11168196 [ dbSNP | Ensembl ].
    VAR_057354

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 159159Missing in isoform 3. 1 PublicationVSP_044882Add
    BLAST
    Alternative sequencei396 – 42934Missing in isoform 2. 1 PublicationVSP_027957Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025561 mRNA. Translation: BAB15170.1.
    AK299465 mRNA. Translation: BAG61431.1.
    AC004241 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57938.1.
    BC056415 mRNA. Translation: AAH56415.1.
    CCDSiCCDS53782.1. [Q9H6T3-3]
    CCDS53783.1. [Q9H6T3-2]
    CCDS8753.1. [Q9H6T3-1]
    RefSeqiNP_001139547.1. NM_001146075.1. [Q9H6T3-2]
    NP_001139548.1. NM_001146076.1. [Q9H6T3-3]
    NP_078880.2. NM_024604.2. [Q9H6T3-1]
    UniGeneiHs.437855.

    Genome annotation databases

    EnsembliENST00000005386; ENSP00000005386; ENSG00000005175. [Q9H6T3-1]
    ENST00000380650; ENSP00000370024; ENSG00000005175. [Q9H6T3-2]
    ENST00000432584; ENSP00000401823; ENSG00000005175. [Q9H6T3-3]
    GeneIDi79657.
    KEGGihsa:79657.
    UCSCiuc001rpr.3. human. [Q9H6T3-1]
    uc001rps.3. human. [Q9H6T3-2]

    Polymorphism databases

    DMDMi158564023.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025561 mRNA. Translation: BAB15170.1 .
    AK299465 mRNA. Translation: BAG61431.1 .
    AC004241 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57938.1 .
    BC056415 mRNA. Translation: AAH56415.1 .
    CCDSi CCDS53782.1. [Q9H6T3-3 ]
    CCDS53783.1. [Q9H6T3-2 ]
    CCDS8753.1. [Q9H6T3-1 ]
    RefSeqi NP_001139547.1. NM_001146075.1. [Q9H6T3-2 ]
    NP_001139548.1. NM_001146076.1. [Q9H6T3-3 ]
    NP_078880.2. NM_024604.2. [Q9H6T3-1 ]
    UniGenei Hs.437855.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CGV X-ray 2.54 A/B/C/D 120-255 [» ]
    4CGW X-ray 3.00 A/B 265-381 [» ]
    ProteinModelPortali Q9H6T3.
    SMRi Q9H6T3. Positions 89-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122783. 50 interactions.
    IntActi Q9H6T3. 32 interactions.
    MINTi MINT-1140426.
    STRINGi 9606.ENSP00000005386.

    PTM databases

    PhosphoSitei Q9H6T3.

    Polymorphism databases

    DMDMi 158564023.

    Proteomic databases

    MaxQBi Q9H6T3.
    PaxDbi Q9H6T3.
    PRIDEi Q9H6T3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000005386 ; ENSP00000005386 ; ENSG00000005175 . [Q9H6T3-1 ]
    ENST00000380650 ; ENSP00000370024 ; ENSG00000005175 . [Q9H6T3-2 ]
    ENST00000432584 ; ENSP00000401823 ; ENSG00000005175 . [Q9H6T3-3 ]
    GeneIDi 79657.
    KEGGi hsa:79657.
    UCSCi uc001rpr.3. human. [Q9H6T3-1 ]
    uc001rps.3. human. [Q9H6T3-2 ]

    Organism-specific databases

    CTDi 79657.
    GeneCardsi GC12M048057.
    H-InvDB HIX0010575.
    HGNCi HGNC:26151. RPAP3.
    HPAi HPA038311.
    HPA038312.
    MIMi 611477. gene.
    neXtProti NX_Q9H6T3.
    PharmGKBi PA162401982.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000154181.
    HOVERGENi HBG059892.
    InParanoidi Q9H6T3.
    OMAi ECYTRGM.
    OrthoDBi EOG7KSX8F.
    PhylomeDBi Q9H6T3.
    TreeFami TF106243.

    Miscellaneous databases

    GenomeRNAii 79657.
    NextBioi 68830.
    PMAP-CutDB Q9H6T3.
    PROi Q9H6T3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H6T3.
    CleanExi HS_RPAP3.
    Genevestigatori Q9H6T3.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR025986. RPAP3-like_C.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF13877. RPAP3_C. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 6 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 AND 3).
      Tissue: Tongue.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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 2).
      Tissue: Blood.
    5. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
      Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
      Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-116; SER-119; SER-121 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-119 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPAP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H6T3
    Secondary accession number(s): B4DRW9, Q6PHR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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