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Q29RF7

- PDS5A_HUMAN

UniProt

Q29RF7 - PDS5A_HUMAN

Protein

Sister chromatid cohesion protein PDS5 homolog A

Gene

PDS5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    2. mitotic nuclear division Source: UniProtKB-KW
    3. negative regulation of DNA replication Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sister chromatid cohesion protein PDS5 homolog A
    Alternative name(s):
    Cell proliferation-inducing gene 54 protein
    Sister chromatid cohesion protein 112
    Short name:
    SCC-112
    Gene namesi
    Name:PDS5AImported
    Synonyms:KIAA0648Imported, PDS51 Publication
    ORF Names:PIG54
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:29088. PDS5A.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase.2 Publications

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. chromosome Source: Reactome
    3. chromosome, centromeric region Source: Reactome
    4. cytosol Source: Reactome
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162399027.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13371337Sister chromatid cohesion protein PDS5 homolog APRO_0000296341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei1146 – 11461N6-acetyllysine1 Publication
    Modified residuei1195 – 11951Phosphoserine3 Publications
    Modified residuei1208 – 12081Phosphothreonine3 Publications
    Modified residuei1211 – 12111N6-acetyllysine1 Publication
    Modified residuei1290 – 12901N6-acetyllysine1 Publication
    Modified residuei1305 – 13051Phosphoserine6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ29RF7.
    PaxDbiQ29RF7.
    PRIDEiQ29RF7.

    PTM databases

    PhosphoSiteiQ29RF7.

    Expressioni

    Tissue specificityi

    Highest level in colon. Low levels in lung, ovary, breast and kidney. Reduced level in renal tumor tissue. Isoform 2 is expressed in kidney.1 Publication

    Developmental stagei

    Cell cycle-regulated with highest level in G2 phase.1 Publication

    Gene expression databases

    ArrayExpressiQ29RF7.
    BgeeiQ29RF7.
    CleanExiHS_PDS5A.
    GenevestigatoriQ29RF7.

    Organism-specific databases

    HPAiHPA036661.
    HPA036662.

    Interactioni

    Subunit structurei

    Interacts with the cohesin complex. Interacts with WAPAL (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, cohesin-dependent and competitive. Interacts with SMC3. Interacts with TP63.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDCA5Q96FF92EBI-1175454,EBI-718805
    RAD21O602163EBI-1175454,EBI-80739
    SMC3Q9UQE74EBI-1175454,EBI-80718
    STAG1Q8WVM73EBI-1175454,EBI-1175097
    STAG2Q8N3U43EBI-1175454,EBI-1057252

    Protein-protein interaction databases

    BioGridi116848. 31 interactions.
    DIPiDIP-35419N.
    IntActiQ29RF7. 14 interactions.
    STRINGi9606.ENSP00000303427.

    Structurei

    3D structure databases

    ProteinModelPortaliQ29RF7.
    SMRiQ29RF7. Positions 78-122, 292-350, 360-428, 682-711.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati393 – 42937HEATSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDS5 family.Curated
    Contains 1 HEAT repeat.Sequence Analysis

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG268017.
    HOGENOMiHOG000230672.
    HOVERGENiHBG108241.
    InParanoidiQ29RF7.
    KOiK11267.
    OMAiNLNKQAF.
    OrthoDBiEOG73Z2SD.
    PhylomeDBiQ29RF7.
    TreeFamiTF106415.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 4 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q29RF7-1) [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

    MDFTAQPKPA TALCGVVSAD GKIAYPPGVK EITDKITTDE MIKRLKMVVK     50
    TFMDMDQDSE DEKQQYLPLA LHLASEFFLR NPNKDVRLLV ACCLADIFRI 100
    YAPEAPYTSH DKLKDIFLFI TRQLKGLEDT KSPQFNRYFY LLENLAWVKS 150
    YNICFELEDC NEIFIQLFRT LFSVINNSHN KKVQMHMLDL MSSIIMEGDG 200
    VTQELLDSIL INLIPAHKNL NKQSFDLAKV LLKRTVQTIE ACIANFFNQV 250
    LVLGRSSVSD LSEHVFDLIQ ELFAIDPHLL LSVMPQLEFK LKSNDGEERL 300
    AVVRLLAKLF GSKDSDLATQ NRPLWQCFLG RFNDIHVPVR LESVKFASHC 350
    LMNHPDLAKD LTEYLKVRSH DPEEAIRHDV IVTIITAAKR DLALVNDQLL 400
    GFVRERTLDK RWRVRKEAMM GLAQLYKKYC LHGEAGKEAA EKVSWIKDKL 450
    LHIYYQNSID DKLLVEKIFA QYLVPHNLET EERMKCLYYL YASLDPNAVK 500
    ALNEMWKCQN MLRSHVRELL DLHKQPTSEA NCSAMFGKLM TIAKNLPDPG 550
    KAQDFVKKFN QVLGDDEKLR SQLELLISPT CSCKQADICV REIARKLANP 600
    KQPTNPFLEM VKFLLERIAP VHIDSEAISA LVKLMNKSIE GTADDEEEGV 650
    SPDTAIRSGL ELLKVLSFTH PTSFHSAETY ESLLQCLRME DDKVAEAAIQ 700
    IFRNTGHKIE TDLPQIRSTL IPILHQKAKR GTPHQAKQAV HCIHAIFTNK 750
    EVQLAQIFEP LSRSLNADVP EQLITPLVSL GHISMLAPDQ FASPMKSVVA 800
    NFIVKDLLMN DRSTGEKNGK LWSPDEEVSP EVLAKVQAIK LLVRWLLGMK 850
    NNQSKSANST LRLLSAMLVS EGDLTEQKRI SKSDMSRLRL AAGSAIMKLA 900
    QEPCYHEIIT PEQFQLCALV INDECYQVRQ IFAQKLHKAL VKLLLPLEYM 950
    AIFALCAKDP VKERRAHARQ CLLKNISIRR EYIKQNPMAT EKLLSLLPEY 1000
    VVPYMIHLLA HDPDFTRSQD VDQLRDIKEC LWFMLEVLMT KNENNSHAFM 1050
    KKMAENIKLT RDAQSPDESK TNEKLYTVCD VALCVINSKS ALCNADSPKD 1100
    PVLPMKFFTQ PEKDFCNDKS YISEETRVLL LTGKPKPAGV LGAVNKPLSA 1150
    TGRKPYVRST GTETGSNINV NSELNPSTGN RSREQSSEAA ETGVSENEEN 1200
    PVRIISVTPV KNIDPVKNKE INSDQATQGN ISSDRGKKRT VTAAGAENIQ 1250
    QKTDEKVDES GPPAPSKPRR GRRPKSESQG NATKNDDLNK PINKGRKRAA 1300
    VGQESPGGLE AGNAKAPKLQ DLAKKAAPAE RQIDLQR 1337
    Length:1,337
    Mass (Da):150,830
    Last modified:April 4, 2006 - v1
    Checksum:iFA28EA9EF77499D9
    GO
    Isoform 2 (identifier: Q29RF7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         591-600: REIARKLANP → VSKSYFTLFL
         601-1337: Missing.

    Show »
    Length:600
    Mass (Da):69,000
    Checksum:i12917E7912C86BFD
    GO

    Sequence cautioni

    The sequence AAM82347.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAI26226.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAH18263.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071D → G in AAM82347. (PubMed:15019998)Curated
    Sequence conflicti471 – 4711Q → R in AAT52214. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei591 – 60010REIARKLANP → VSKSYFTLFL in isoform 2. 4 PublicationsVSP_052491
    Alternative sequencei601 – 1337737Missing in isoform 2. 4 PublicationsVSP_052492Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY550968 mRNA. Translation: AAT52214.1.
    AK098331 mRNA. Translation: BAC05286.1.
    BC041361 mRNA. Translation: AAH41361.1.
    BC114218 mRNA. Translation: AAI14219.1.
    BC126225 mRNA. Translation: AAI26226.1. Different initiation.
    AF294791 mRNA. Translation: AAM82347.1. Sequence problems.
    CR749425 mRNA. Translation: CAH18263.1. Different initiation.
    AB014548 mRNA. Translation: BAA31623.1.
    CCDSiCCDS47045.1. [Q29RF7-1]
    CCDS54759.1. [Q29RF7-3]
    RefSeqiNP_001093869.1. NM_001100399.1. [Q29RF7-1]
    NP_001093870.1. NM_001100400.1. [Q29RF7-3]
    XP_005262709.1. XM_005262652.1. [Q29RF7-1]
    UniGeneiHs.331431.

    Genome annotation databases

    EnsembliENST00000303538; ENSP00000303427; ENSG00000121892. [Q29RF7-1]
    ENST00000503396; ENSP00000426749; ENSG00000121892. [Q29RF7-3]
    GeneIDi23244.
    KEGGihsa:23244.
    UCSCiuc003guv.4. human. [Q29RF7-1]
    uc003guw.4. human. [Q29RF7-3]

    Polymorphism databases

    DMDMi121947590.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY550968 mRNA. Translation: AAT52214.1 .
    AK098331 mRNA. Translation: BAC05286.1 .
    BC041361 mRNA. Translation: AAH41361.1 .
    BC114218 mRNA. Translation: AAI14219.1 .
    BC126225 mRNA. Translation: AAI26226.1 . Different initiation.
    AF294791 mRNA. Translation: AAM82347.1 . Sequence problems.
    CR749425 mRNA. Translation: CAH18263.1 . Different initiation.
    AB014548 mRNA. Translation: BAA31623.1 .
    CCDSi CCDS47045.1. [Q29RF7-1 ]
    CCDS54759.1. [Q29RF7-3 ]
    RefSeqi NP_001093869.1. NM_001100399.1. [Q29RF7-1 ]
    NP_001093870.1. NM_001100400.1. [Q29RF7-3 ]
    XP_005262709.1. XM_005262652.1. [Q29RF7-1 ]
    UniGenei Hs.331431.

    3D structure databases

    ProteinModelPortali Q29RF7.
    SMRi Q29RF7. Positions 78-122, 292-350, 360-428, 682-711.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116848. 31 interactions.
    DIPi DIP-35419N.
    IntActi Q29RF7. 14 interactions.
    STRINGi 9606.ENSP00000303427.

    PTM databases

    PhosphoSitei Q29RF7.

    Polymorphism databases

    DMDMi 121947590.

    Proteomic databases

    MaxQBi Q29RF7.
    PaxDbi Q29RF7.
    PRIDEi Q29RF7.

    Protocols and materials databases

    DNASUi 23244.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303538 ; ENSP00000303427 ; ENSG00000121892 . [Q29RF7-1 ]
    ENST00000503396 ; ENSP00000426749 ; ENSG00000121892 . [Q29RF7-3 ]
    GeneIDi 23244.
    KEGGi hsa:23244.
    UCSCi uc003guv.4. human. [Q29RF7-1 ]
    uc003guw.4. human. [Q29RF7-3 ]

    Organism-specific databases

    CTDi 23244.
    GeneCardsi GC04M039824.
    HGNCi HGNC:29088. PDS5A.
    HPAi HPA036661.
    HPA036662.
    MIMi 613200. gene.
    neXtProti NX_Q29RF7.
    PharmGKBi PA162399027.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268017.
    HOGENOMi HOG000230672.
    HOVERGENi HBG108241.
    InParanoidi Q29RF7.
    KOi K11267.
    OMAi NLNKQAF.
    OrthoDBi EOG73Z2SD.
    PhylomeDBi Q29RF7.
    TreeFami TF106415.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Miscellaneous databases

    ChiTaRSi PDS5A. human.
    GeneWikii PDS5A.
    GenomeRNAii 23244.
    NextBioi 44916.
    PROi Q29RF7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q29RF7.
    Bgeei Q29RF7.
    CleanExi HS_PDS5A.
    Genevestigatori Q29RF7.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human cell proliferation inducing gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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] (ISOFORM 2).
      Tissue: UterusImported.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: EyeImported and TestisImported.
    4. "SCC-112, a novel cell cycle-regulated molecule, exhibits reduced expression in human renal carcinomas."
      Kumar D., Sakabe I., Patel S., Zhang Y., Ahmad I., Gehan E.A., Whiteside T.L., Kasid U.
      Gene 328:187-196(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-1337 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-1337 (ISOFORM 2).
      Tissue: Salivary gland.
    6. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1337 (ISOFORM 1).
      Tissue: BrainImported.
    7. "Characterization of vertebrate cohesin complexes and their regulation in prophase."
      Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.
      J. Cell Biol. 151:749-762(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THE COHESIN COMPLEX.
    8. "Functional contribution of Pds5 to cohesin-mediated cohesion in human cells and Xenopus egg extracts."
      Losada A., Yokochi T., Hirano T.
      J. Cell Sci. 118:2133-2141(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHROMATIN.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Wapl controls the dynamic association of cohesin with chromatin."
      Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A., Mechtler K., Peters J.M.
      Cell 127:955-967(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WAPAL.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "SCC-112 gene is involved in tumor progression and promotes the cell proliferation in G2/M phase."
      Zheng M.Z., Zheng L.M., Zeng Y.X.
      J. Cancer Res. Clin. Oncol. 134:453-462(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP63.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195 AND THR-1208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Cohesin acetylation speeds the replication fork."
      Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.
      Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMC3.
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1146; LYS-1211 AND LYS-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: INTERACTION WITH WAPAL AND CDCA5.
    21. "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-1195; THR-1208 AND SER-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-1305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDS5A_HUMAN
    AccessioniPrimary (citable) accession number: Q29RF7
    Secondary accession number(s): Q2TTR5
    , Q68DF7, Q8N7J4, Q8NG14, Q9Y4D4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 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

    Miscellaneous

    HeLa cells with a reduced level of PDS5A show a mild defect in sister chromatid cohesion. HeLa cells with a reduced level of RAD21 show reduced association of PDS5A with chromatin.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3