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Q29RF7

- PDS5A_HUMAN

UniProt

Q29RF7 - PDS5A_HUMAN

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Protein
Sister chromatid cohesion protein PDS5 homolog A
Gene
PDS5A, KIAA0648, PDS5, PIG54
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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:PDS5A
Synonyms:KIAA0648, PDS5
ORF Names:PIG54
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:29088. PDS5A.

Subcellular locationi

Nucleus
Note: Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase.3 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
Complete GO annotation...

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 A
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati393 – 42937HEAT
Add
BLAST

Sequence similaritiesi

Belongs to the PDS5 family.
Contains 1 HEAT repeat.

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 21 Publication (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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei591 – 60010REIARKLANP → VSKSYFTLFL in isoform 2. 1 Publication
VSP_052491
Alternative sequencei601 – 1337737Missing in isoform 2. 1 Publication
VSP_052492Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: Uterus.
  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: Eye and Testis.
  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: Brain.
  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: September 3, 2014
This is version 86 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

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