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Q9NTI5 (PDS5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sister chromatid cohesion protein PDS5 homolog B
Alternative name(s):
Androgen-induced proliferation inhibitor
Androgen-induced prostate proliferative shutoff-associated protein AS3
Gene names
Name:PDS5B
Synonyms:APRIN, AS3, KIAA0979
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.19

Subunit structure

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. Ref.10 Ref.19 Ref.22

Subcellular location

Nucleus By similarity UniProtKB Q6TRW4.

Tissue specificity

Widely expressed. Ref.1

Induction

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

Sequence similarities

Belongs to the PDS5 family.

Contains 3 A.T hook DNA-binding domains.

Contains 1 HEAT repeat.

Sequence caution

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q9NTI5-1)

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.
Isoform 2 Ref.2 (identifier: Q9NTI5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1392-1447: Missing.
Isoform 3 Ref.8 (identifier: Q9NTI5-3)

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.
Isoform 4 Ref.8 (identifier: Q9NTI5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     105-122: DIFMFITRQLKGLEDTKS → ASTDLNNSKIDRYFDLSF
     123-1447: Missing.
Note: No experimental confirmation available.
Isoform 5 Ref.5 (identifier: Q9NTI5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1230: Missing.
     1356-1447: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14471447Sister chromatid cohesion protein PDS5 homolog B
PRO_0000287424

Regions

Repeat383 – 41937HEAT
DNA binding1249 – 126113A.T hook 1
DNA binding1287 – 129913A.T hook 2
DNA binding1372 – 138413A.T hook 3

Amino acid modifications

Modified residue11361N6-acetyllysine Ref.21
Modified residue11621Phosphoserine Ref.20
Modified residue11661Phosphoserine Ref.20 Ref.23 Ref.25 PubMed 15302935
Modified residue11761Phosphoserine Ref.20
Modified residue11821Phosphoserine Ref.15 Ref.20 Ref.23 Ref.25
Modified residue11911Phosphoserine Ref.20
Modified residue12551Phosphothreonine By similarity
Modified residue12571Phosphoserine Ref.11 Ref.16 Ref.20
Modified residue12591Phosphoserine By similarity
Modified residue12831Phosphoserine Ref.15 Ref.20 Ref.23 Ref.25
Modified residue13341Phosphoserine Ref.16
Modified residue13581Phosphoserine Ref.12 Ref.14 Ref.15 Ref.20 Ref.23 Ref.25 PubMed 15302935
Modified residue13671Phosphothreonine Ref.13
Modified residue13701Phosphothreonine Ref.12 Ref.20
Modified residue13791Phosphoserine Ref.5 Ref.17
Modified residue13811Phosphothreonine Ref.25
Modified residue13831Phosphoserine Ref.11 Ref.25

Natural variations

Alternative sequence1 – 12301230Missing in isoform 5. Ref.5
VSP_052396
Alternative sequence105 – 12218DIFMF…EDTKS → ASTDLNNSKIDRYFDLSF in isoform 4. Ref.8
VSP_052397
Alternative sequence123 – 14471325Missing in isoform 4. Ref.8
VSP_052398
Alternative sequence491 – 52939ALNEM…IFSKV → YVSNIKFCSFHPLQYIGFYG KETTNTCILKCNLCSVNIV in isoform 3. Ref.8
VSP_052399
Alternative sequence530 – 1447918Missing in isoform 3. Ref.8
VSP_052400
Alternative sequence1356 – 144792Missing in isoform 5. Ref.5
VSP_052401
Alternative sequence1392 – 144756Missing in isoform 2. Ref.2
VSP_052402

Experimental info

Sequence conflict2561F → S in AAD22134. Ref.2
Sequence conflict3261H → N in AAH39256. Ref.8
Sequence conflict3941R → G in AAD22134. Ref.2
Sequence conflict5351N → S in AAD22134. Ref.2
Sequence conflict7421T → A in AAD22134. Ref.2
Sequence conflict11151E → G in AAD22134. Ref.2
Sequence conflict11561S → G in AAD22134. Ref.2
Sequence conflict11971K → R in AAD22134. Ref.2
Sequence conflict12251Q → R in AAD22134. Ref.2
Sequence conflict12421K → R in AAD22134. Ref.2
Sequence conflict13591P → S in AAD22134. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 145C30308EA3EFD5

FASTA1,447164,667
        10         20         30         40         50         60 
MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA 

        70         80         90        100        110        120 
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT 

       130        140        150        160        170        180 
KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL 

       190        200        210        220        230        240 
MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV 

       250        260        270        280        290        300 
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF 

       310        320        330        340        350        360 
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH 

       370        380        390        400        410        420 
DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYA 

       430        440        450        460        470        480 
LQSAAGKDAA KQIAWIKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL 

       490        500        510        520        530        540 
YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG 

       550        560        570        580        590        600 
KAQDFMKKFT QVLEDDEKIR KQLEVLVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM 

       610        620        630        640        650        660 
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH 

       670        680        690        700        710        720 
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK 

       730        740        750        760        770        780 
GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ 

       790        800        810        820        830        840 
FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK 

       850        860        870        880        890        900 
NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT 

       910        920        930        940        950        960 
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ 

       970        980        990       1000       1010       1020 
CLVKNINVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC 

      1030       1040       1050       1060       1070       1080 
LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDAK MNEKLYTVCD VAMNIIMSKS 

      1090       1100       1110       1120       1130       1140 
TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTTNV LGAVNKPLSS 

      1150       1160       1170       1180       1190       1200 
AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK 

      1210       1220       1230       1240       1250       1260 
RDDSDLVRSE LEKPRGRKKT PVTEQEEKLG MDDLTKLVQE QKPKGSQRSR KRGHTASESD 

      1270       1280       1290       1300       1310       1320 
EQQWPEEKRL KEDILENEDE QNSPPKKGKR GRPPKPLGGG TPKEEPTMKT SKKGSKKKSG 

      1330       1340       1350       1360       1370       1380 
PPAPEEEEEE ERQSGNTEQK SKSKQHRVSR RAQQRAESPE SSAIESTQST PQKGRGRPSK 

      1390       1400       1410       1420       1430       1440 
TPSPSQPKKN VRVGRSKQAA TKENDSSEEV DVFQGSSPVD DIPQEETEEE EVSTVNVRRR 


SAKRERR 

« Hide

Isoform 2 [UniParc].

Checksum: 9C5FD7A7F8C4A18F
Show »

FASTA1,391158,280
Isoform 3 [UniParc].

Checksum: 05CDB3E2A92F46DD
Show »

FASTA52961,437
Isoform 4 [UniParc].

Checksum: B8EAB2D511A217CB
Show »

FASTA12214,108
Isoform 5 [UniParc].

Checksum: 492809836D3665D3
Show »

FASTA12514,281

References

« Hide 'large scale' references
[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: Prostate.
[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: Brain.
[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. expand/collapse author list , 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: Colon.
[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. expand/collapse author list , 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: Prostate and Testis.
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Sororin mediates sister chromatid cohesion by antagonizing wapl."
Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.
Cell 143:737-749(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055847.1. NM_015032.3.
UniGeneHs.744901.

3D structure databases

ProteinModelPortalQ9NTI5.
SMRQ9NTI5. Positions 68-95, 365-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116685. 19 interactions.
IntActQ9NTI5. 18 interactions.
MINTMINT-3073997.
STRING9606.ENSP00000313851.

PTM databases

PhosphoSiteQ9NTI5.

Polymorphism databases

DMDM74725312.

Proteomic databases

PaxDbQ9NTI5.
PRIDEQ9NTI5.

Protocols and materials databases

DNASU23047.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315596; ENSP00000313851; ENSG00000083642. [Q9NTI5-1]
ENST00000450460; ENSP00000401619; ENSG00000083642. [Q9NTI5-2]
GeneID23047.
KEGGhsa:23047.
UCSCuc001uun.3. human. [Q9NTI5-4]
uc001uuo.3. human. [Q9NTI5-3]
uc010abf.3. human. [Q9NTI5-1]

Organism-specific databases

CTD23047.
GeneCardsGC13P033160.
HGNCHGNC:20418. PDS5B.
HPAHPA039513.
HPA040015.
MIM605333. gene.
neXtProtNX_Q9NTI5.
PharmGKBPA162399098.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268017.
HOVERGENHBG108241.
KOK11267.
OMAAKKGPPR.
OrthoDBEOG73Z2SD.
PhylomeDBQ9NTI5.
TreeFamTF106415.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9NTI5.
BgeeQ9NTI5.
CleanExHS_PDS5B.
GenevestigatorQ9NTI5.

Family and domain databases

Gene3D1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR017956. AT_hook_DNA-bd_motif.
[Graphical view]
SMARTSM00384. AT_hook. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

ChiTaRSPDS5B. human.
GeneWikiPDS5B.
GenomeRNAi23047.
NextBio44084.
PROQ9NTI5.
SOURCESearch...

Entry information

Entry namePDS5B_HUMAN
AccessionPrimary (citable) accession number: Q9NTI5
Secondary accession number(s): Q5R3S3 expand/collapse secondary AC list , Q5W0K8, Q6NSC3, Q8IXT6, Q9H5N8, Q9Y2I5, Q9Y451
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM