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Q9NTI5

- PDS5B_HUMAN

UniProt

Q9NTI5 - PDS5B_HUMAN

Protein

Sister chromatid cohesion protein PDS5 homolog B

Gene

PDS5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    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. Plays a role in androgen-induced proliferative arrest in prostate cells.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi1249 – 126113A.T hook 1Sequence AnalysisAdd
    BLAST
    DNA bindingi1287 – 129913A.T hook 2Sequence AnalysisAdd
    BLAST
    DNA bindingi1372 – 138413A.T hook 3Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. DNA binding Source: ProtInc
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. mitotic cell cycle Source: Reactome
    3. mitotic sister chromatid cohesion Source: UniProtKB
    4. negative regulation of cell proliferation Source: UniProtKB
    5. regulation of cell proliferation Source: MGI

    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 B
    Alternative name(s):
    Androgen-induced proliferation inhibitor
    Androgen-induced prostate proliferative shutoff-associated protein AS3
    Gene namesi
    Name:PDS5B
    Synonyms:APRIN, AS3Imported, KIAA0979Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:20418. PDS5B.

    Subcellular locationi

    Nucleus By similarity

    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: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162399098.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14471447Sister chromatid cohesion protein PDS5 homolog BPRO_0000287424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1136 – 11361N6-acetyllysine1 Publication
    Modified residuei1162 – 11621Phosphoserine1 Publication
    Modified residuei1166 – 11661Phosphoserine3 Publications
    Modified residuei1176 – 11761Phosphoserine1 Publication
    Modified residuei1182 – 11821Phosphoserine4 Publications
    Modified residuei1191 – 11911Phosphoserine1 Publication
    Modified residuei1255 – 12551PhosphothreonineBy similarity
    Modified residuei1257 – 12571Phosphoserine3 Publications
    Modified residuei1259 – 12591PhosphoserineBy similarity
    Modified residuei1283 – 12831Phosphoserine4 Publications
    Modified residuei1334 – 13341Phosphoserine1 Publication
    Modified residuei1358 – 13581Phosphoserine6 Publications
    Modified residuei1367 – 13671Phosphothreonine1 Publication
    Modified residuei1370 – 13701Phosphothreonine2 Publications
    Modified residuei1379 – 13791Phosphoserine1 Publication
    Modified residuei1381 – 13811Phosphothreonine1 Publication
    Modified residuei1383 – 13831Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NTI5.
    PaxDbiQ9NTI5.
    PRIDEiQ9NTI5.

    PTM databases

    PhosphoSiteiQ9NTI5.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    By the synthetic androgen R1881 in prostate carcinoma cells undergoing proliferative arrest. Maximum levels occur 18-20 hours after androgen exposure.1 Publication

    Gene expression databases

    ArrayExpressiQ9NTI5.
    BgeeiQ9NTI5.
    CleanExiHS_PDS5B.
    GenevestigatoriQ9NTI5.

    Organism-specific databases

    HPAiHPA039513.
    HPA040015.

    Interactioni

    Subunit structurei

    Interacts with the cohesin complex. Interacts with RAD21; the interaction is direct. Interacts with WAPAL (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, cohesin-dependent and competitive Probable.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA2P5158726EBI-1175604,EBI-79792
    RAD21O602164EBI-1175604,EBI-80739
    SMC3Q9UQE77EBI-1175604,EBI-80718
    STAG1Q8WVM73EBI-1175604,EBI-1175097
    STAG2Q8N3U43EBI-1175604,EBI-1057252
    WAPALQ7Z5K29EBI-1175604,EBI-1022242

    Protein-protein interaction databases

    BioGridi116685. 21 interactions.
    DIPiDIP-35420N.
    IntActiQ9NTI5. 18 interactions.
    MINTiMINT-3073997.
    STRINGi9606.ENSP00000313851.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NTI5.
    SMRiQ9NTI5. Positions 68-95, 365-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati383 – 41937HEATSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDS5 family.Curated
    Contains 3 A.T hook DNA-binding domains.Sequence Analysis
    Contains 1 HEAT repeat.Sequence Analysis

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG268017.
    HOVERGENiHBG108241.
    KOiK11267.
    OMAiAKKGPPR.
    OrthoDBiEOG73Z2SD.
    PhylomeDBiQ9NTI5.
    TreeFamiTF106415.

    Family and domain databases

    Gene3Di1.25.10.10. 4 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR017956. AT_hook_DNA-bd_motif.
    [Graphical view]
    SMARTiSM00384. AT_hook. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9NTI5-1) [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

    MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE     50
    EEKELYLNLA LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP 100
    DKLKDIFMFI TRQLKGLEDT KSPQFNRYFY LLENIAWVKS YNICFELEDS 150
    NEIFTQLYRT LFSVINNGHN QKVHMHMVDL MSSIICEGDT VSQELLDTVL 200
    VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV LMLGKTSISD 250
    LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF 300
    GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD 350
    LTEYLKVRSH DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK 400
    RWRVRKEAMM GLAQIYKKYA LQSAAGKDAA KQIAWIKDKL LHIYYQNSID 450
    DRLLVERIFA QYMVPHNLET TERMKCLYYL YATLDLNAVK ALNEMWKCQN 500
    LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG KAQDFMKKFT 550
    QVLEDDEKIR KQLEVLVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM 600
    IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL 650
    ELLKVLSFTH PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE 700
    EDFPHIRSAL LPVLHHKSKK GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP 750
    LHKSLDPSNL EHLITPLVTI GHIALLAPDQ FAAPLKSLVA TFIVKDLLMN 800
    DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK NNHSKSGTST 850
    LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT 900
    LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP 950
    VKERRAHARQ CLVKNINVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA 1000
    HDPDYVKVQD IEQLKDVKEC LWFVLEILMA KNENNSHAFI RKMVENIKQT 1050
    KDAQGPDDAK MNEKLYTVCD VAMNIIMSKS TTYSLESPKD PVLPARFFTQ 1100
    PDKNFSNTKN YLPPEMKSFF TPGKPKTTNV LGAVNKPLSS AGKQSQTKSS 1150
    RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK 1200
    RDDSDLVRSE LEKPRGRKKT PVTEQEEKLG MDDLTKLVQE QKPKGSQRSR 1250
    KRGHTASESD EQQWPEEKRL KEDILENEDE QNSPPKKGKR GRPPKPLGGG 1300
    TPKEEPTMKT SKKGSKKKSG PPAPEEEEEE ERQSGNTEQK SKSKQHRVSR 1350
    RAQQRAESPE SSAIESTQST PQKGRGRPSK TPSPSQPKKN VRVGRSKQAA 1400
    TKENDSSEEV DVFQGSSPVD DIPQEETEEE EVSTVNVRRR SAKRERR 1447
    Length:1,447
    Mass (Da):164,667
    Last modified:October 1, 2000 - v1
    Checksum:i145C30308EA3EFD5
    GO
    Isoform 21 Publication (identifier: Q9NTI5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1392-1447: Missing.

    Show »
    Length:1,391
    Mass (Da):158,280
    Checksum:i9C5FD7A7F8C4A18F
    GO
    Isoform 31 Publication (identifier: Q9NTI5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-529: ALNEMWKCQN...ASVKAIFSKV → YVSNIKFCSF...KCNLCSVNIV
         530-1447: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:529
    Mass (Da):61,437
    Checksum:i05CDB3E2A92F46DD
    GO
    Isoform 41 Publication (identifier: Q9NTI5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         105-122: DIFMFITRQLKGLEDTKS → ASTDLNNSKIDRYFDLSF
         123-1447: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:122
    Mass (Da):14,108
    Checksum:iB8EAB2D511A217CB
    GO
    Isoform 51 Publication (identifier: Q9NTI5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1230: Missing.
         1356-1447: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:125
    Mass (Da):14,281
    Checksum:i492809836D3665D3
    GO

    Sequence cautioni

    The sequence BAA76823.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561F → S in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti326 – 3261H → N in AAH39256. (PubMed:15489334)Curated
    Sequence conflicti394 – 3941R → G in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti535 – 5351N → S in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti742 – 7421T → A in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1115 – 11151E → G in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1156 – 11561S → G in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1197 – 11971K → R in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1225 – 12251Q → R in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1242 – 12421K → R in AAD22134. (PubMed:10215036)Curated
    Sequence conflicti1359 – 13591P → S in AAD22134. (PubMed:10215036)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 12301230Missing in isoform 5. 1 PublicationVSP_052396Add
    BLAST
    Alternative sequencei105 – 12218DIFMF…EDTKS → ASTDLNNSKIDRYFDLSF in isoform 4. 1 PublicationVSP_052397Add
    BLAST
    Alternative sequencei123 – 14471325Missing in isoform 4. 1 PublicationVSP_052398Add
    BLAST
    Alternative sequencei491 – 52939ALNEM…IFSKV → YVSNIKFCSFHPLQYIGFYG KETTNTCILKCNLCSVNIV in isoform 3. 1 PublicationVSP_052399Add
    BLAST
    Alternative sequencei530 – 1447918Missing in isoform 3. 1 PublicationVSP_052400Add
    BLAST
    Alternative sequencei1356 – 144792Missing in isoform 5. 1 PublicationVSP_052401Add
    BLAST
    Alternative sequencei1392 – 144756Missing in isoform 2. 1 PublicationVSP_052402Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U95825 mRNA. Translation: AAD22134.2.
    AB023196 mRNA. Translation: BAA76823.2. Different initiation.
    AK026889 mRNA. Translation: BAB15584.1.
    AL137201 mRNA. Translation: CAB69911.1.
    AL138820, Z75889 Genomic DNA. Translation: CAH73160.2.
    Z75889, AL138820 Genomic DNA. Translation: CAI10806.2.
    BC039256 mRNA. Translation: AAH39256.1.
    BC070274 mRNA. Translation: AAH70274.1.
    CCDSiCCDS41878.1. [Q9NTI5-1]
    RefSeqiNP_055847.1. NM_015032.3. [Q9NTI5-1]
    UniGeneiHs.744901.

    Genome annotation databases

    EnsembliENST00000315596; ENSP00000313851; ENSG00000083642. [Q9NTI5-1]
    ENST00000450460; ENSP00000401619; ENSG00000083642. [Q9NTI5-2]
    GeneIDi23047.
    KEGGihsa:23047.
    UCSCiuc001uun.3. human. [Q9NTI5-4]
    uc001uuo.3. human. [Q9NTI5-3]
    uc010abf.3. human. [Q9NTI5-1]

    Polymorphism databases

    DMDMi74725312.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U95825 mRNA. Translation: AAD22134.2 .
    AB023196 mRNA. Translation: BAA76823.2 . Different initiation.
    AK026889 mRNA. Translation: BAB15584.1 .
    AL137201 mRNA. Translation: CAB69911.1 .
    AL138820 , Z75889 Genomic DNA. Translation: CAH73160.2 .
    Z75889 , AL138820 Genomic DNA. Translation: CAI10806.2 .
    BC039256 mRNA. Translation: AAH39256.1 .
    BC070274 mRNA. Translation: AAH70274.1 .
    CCDSi CCDS41878.1. [Q9NTI5-1 ]
    RefSeqi NP_055847.1. NM_015032.3. [Q9NTI5-1 ]
    UniGenei Hs.744901.

    3D structure databases

    ProteinModelPortali Q9NTI5.
    SMRi Q9NTI5. Positions 68-95, 365-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116685. 21 interactions.
    DIPi DIP-35420N.
    IntActi Q9NTI5. 18 interactions.
    MINTi MINT-3073997.
    STRINGi 9606.ENSP00000313851.

    PTM databases

    PhosphoSitei Q9NTI5.

    Polymorphism databases

    DMDMi 74725312.

    Proteomic databases

    MaxQBi Q9NTI5.
    PaxDbi Q9NTI5.
    PRIDEi Q9NTI5.

    Protocols and materials databases

    DNASUi 23047.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315596 ; ENSP00000313851 ; ENSG00000083642 . [Q9NTI5-1 ]
    ENST00000450460 ; ENSP00000401619 ; ENSG00000083642 . [Q9NTI5-2 ]
    GeneIDi 23047.
    KEGGi hsa:23047.
    UCSCi uc001uun.3. human. [Q9NTI5-4 ]
    uc001uuo.3. human. [Q9NTI5-3 ]
    uc010abf.3. human. [Q9NTI5-1 ]

    Organism-specific databases

    CTDi 23047.
    GeneCardsi GC13P033160.
    HGNCi HGNC:20418. PDS5B.
    HPAi HPA039513.
    HPA040015.
    MIMi 605333. gene.
    neXtProti NX_Q9NTI5.
    PharmGKBi PA162399098.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268017.
    HOVERGENi HBG108241.
    KOi K11267.
    OMAi AKKGPPR.
    OrthoDBi EOG73Z2SD.
    PhylomeDBi Q9NTI5.
    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 PDS5B. human.
    GeneWikii PDS5B.
    GenomeRNAii 23047.
    NextBioi 44084.
    PROi Q9NTI5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NTI5.
    Bgeei Q9NTI5.
    CleanExi HS_PDS5B.
    Genevestigatori Q9NTI5.

    Family and domain databases

    Gene3Di 1.25.10.10. 4 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR017956. AT_hook_DNA-bd_motif.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Expression of novel genes linked to the androgen-induced, proliferative shutoff in prostate cancer cells."
      Geck P., Szelei J., Jimenez J., Lin T.-M., Sonnenschein C., Soto A.M.
      J. Steroid Biochem. Mol. Biol. 63:211-218(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    2. "Early gene expression during androgen-induced inhibition of proliferation of prostate cancer cells: a new suppressor candidate on chromosome 13, in the BRCA2-Rb1 locus."
      Geck P., Szelei J., Jimenez J., Sonnenschein C., Soto A.M.
      J. Steroid Biochem. Mol. Biol. 68:41-50(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: ProstateImported.
    3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: BrainImported.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "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 5).
      Tissue: ColonImported.
    6. Rhodes S., Huckle E.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 3 AND 4).
      Tissue: ProstateImported and TestisImported.
    9. "Androgen-induced proliferative quiescence in prostate cancer cells: the role of AS3 as its mediator."
      Geck P., Maffini M.V., Szelei J., Sonnenschein C., Soto A.M.
      Proc. Natl. Acad. Sci. U.S.A. 97:10185-10190(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "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 COHESIN COMPLEX.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-1358 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    15. "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-1182; SER-1283 AND SER-1358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Carrascal M., Abian J.
      Submitted (JAN-2008) to UniProtKB
      Cited for: PHOSPHORYLATION AT SER-1379, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1."
      Shintomi K., Hirano T.
      Genes Dev. 23:2224-2236(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WAPAL AND RAD21.
    20. "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-1162; SER-1166; SER-1176; SER-1182; SER-1191; SER-1257; SER-1283; SER-1358 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "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-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: INTERACTION WITH WAPAL AND CDCA5.
    23. "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-1166; SER-1182; SER-1283 AND SER-1358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-1166; SER-1182; SER-1283; SER-1358; THR-1381 AND SER-1383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDS5B_HUMAN
    AccessioniPrimary (citable) accession number: Q9NTI5
    Secondary accession number(s): Q5R3S3
    , Q5W0K8, Q6NSC3, Q8IXT6, Q9H5N8, Q9Y2I5, Q9Y451
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 115 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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