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Protein

Sister chromatid cohesion protein PDS5 homolog B

Gene

PDS5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • ATP binding Source: ProtInc
  • DNA binding Source: ProtInc

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • mitotic sister chromatid cohesion Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • regulation of cell proliferation Source: MGI
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2468052. Establishment of Sister Chromatid Cohesion.
R-HSA-2470946. Cohesin Loading onto Chromatin.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20418. PDS5B.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • chromosome Source: Reactome
  • chromosome, centromeric region Source: Reactome
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162399098.

Polymorphism and mutation databases

BioMutaiPDS5B.
DMDMi74725312.

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-acetyllysineCombined sources
Modified residuei1140 – 11401PhosphoserineCombined sources
Modified residuei1162 – 11621PhosphoserineCombined sources
Modified residuei1166 – 11661PhosphoserineCombined sources
Modified residuei1176 – 11761PhosphoserineCombined sources
Modified residuei1182 – 11821PhosphoserineCombined sources
Modified residuei1191 – 11911PhosphoserineCombined sources
Modified residuei1255 – 12551PhosphothreonineCombined sources
Modified residuei1257 – 12571PhosphoserineCombined sources
Modified residuei1259 – 12591PhosphoserineCombined sources
Modified residuei1283 – 12831PhosphoserineCombined sources
Modified residuei1319 – 13191PhosphoserineCombined sources
Modified residuei1334 – 13341PhosphoserineCombined sources
Modified residuei1358 – 13581PhosphoserineCombined sources
Modified residuei1366 – 13661PhosphoserineBy similarity
Modified residuei1367 – 13671PhosphothreonineCombined sources
Modified residuei1369 – 13691PhosphoserineBy similarity
Modified residuei1370 – 13701PhosphothreonineCombined sources
Modified residuei1381 – 13811PhosphothreonineCombined sources
Modified residuei1383 – 13831PhosphoserineCombined sources
Modified residuei1417 – 14171PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NTI5.
MaxQBiQ9NTI5.
PaxDbiQ9NTI5.
PeptideAtlasiQ9NTI5.
PRIDEiQ9NTI5.

PTM databases

iPTMnetiQ9NTI5.
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

BgeeiQ9NTI5.
CleanExiHS_PDS5B.
ExpressionAtlasiQ9NTI5. baseline and differential.
GenevisibleiQ9NTI5. HS.

Organism-specific databases

HPAiHPA039513.
HPA040015.

Interactioni

Subunit structurei

Interacts with the cohesin complex. Interacts with RAD21; the interaction is direct. Interacts with WAPL (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
WAPLQ7Z5K29EBI-1175604,EBI-1022242

Protein-protein interaction databases

BioGridi116685. 52 interactions.
DIPiDIP-35420N.
IntActiQ9NTI5. 23 interactions.
MINTiMINT-3073997.
STRINGi9606.ENSP00000313851.

Structurei

Secondary structure

1
1447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263Combined sources
Helixi28 – 4417Combined sources
Helixi50 – 6314Combined sources
Helixi66 – 694Combined sources
Helixi74 – 9118Combined sources
Helixi100 – 11314Combined sources
Helixi114 – 1185Combined sources
Helixi125 – 13814Combined sources
Helixi140 – 1467Combined sources
Helixi150 – 16415Combined sources
Helixi171 – 18616Combined sources
Beta strandi187 – 1893Combined sources
Helixi193 – 2008Combined sources
Helixi201 – 2033Combined sources
Helixi205 – 2106Combined sources
Helixi212 – 22413Combined sources
Helixi226 – 24015Combined sources
Helixi252 – 2543Combined sources
Helixi255 – 26511Combined sources
Helixi267 – 2704Combined sources
Turni271 – 2733Combined sources
Helixi274 – 2807Combined sources
Helixi286 – 30116Combined sources
Helixi307 – 3104Combined sources
Helixi312 – 3198Combined sources
Helixi320 – 3234Combined sources
Helixi327 – 34317Combined sources
Helixi345 – 3506Combined sources
Helixi352 – 3587Combined sources
Helixi364 – 38017Combined sources
Helixi382 – 3843Combined sources
Helixi387 – 39610Combined sources
Helixi402 – 41918Combined sources
Helixi427 – 4326Combined sources
Turni433 – 4353Combined sources
Helixi436 – 4427Combined sources
Helixi443 – 4453Combined sources
Helixi449 – 46113Combined sources
Helixi470 – 48112Combined sources
Helixi486 – 51429Combined sources
Helixi519 – 53315Combined sources
Helixi539 – 55517Combined sources
Helixi557 – 56711Combined sources
Helixi573 – 58513Combined sources
Helixi596 – 60813Combined sources
Helixi615 – 62915Combined sources
Helixi634 – 6385Combined sources
Helixi642 – 65918Combined sources
Helixi662 – 6643Combined sources
Helixi667 – 67711Combined sources
Helixi682 – 69514Combined sources
Helixi699 – 7024Combined sources
Helixi704 – 72017Combined sources
Helixi723 – 73614Combined sources
Helixi740 – 75415Combined sources
Helixi761 – 7633Combined sources
Helixi764 – 77613Combined sources
Turni778 – 7814Combined sources
Helixi782 – 79110Combined sources
Helixi794 – 7974Combined sources
Helixi815 – 8173Combined sources
Helixi820 – 83920Combined sources
Helixi846 – 85914Combined sources
Turni860 – 8623Combined sources
Helixi872 – 89019Combined sources
Helixi893 – 8964Combined sources
Helixi901 – 9088Combined sources
Helixi909 – 9124Combined sources
Helixi916 – 93116Combined sources
Helixi937 – 9393Combined sources
Helixi941 – 9488Combined sources
Helixi952 – 97524Combined sources
Helixi980 – 9845Combined sources
Helixi988 – 9903Combined sources
Helixi991 – 100010Combined sources
Helixi1011 – 102818Combined sources
Helixi1036 – 104712Combined sources
Beta strandi1053 – 10553Combined sources
Helixi1059 – 107921Combined sources
Beta strandi1081 – 10855Combined sources
Turni1095 – 10973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5HDTX-ray2.71A/B21-1120[»]
ProteinModelPortaliQ9NTI5.
SMRiQ9NTI5. Positions 272-301, 357-417, 670-695.
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

eggNOGiKOG1525. Eukaryota.
ENOG410XQW7. LUCA.
GeneTreeiENSGT00390000012488.
HOVERGENiHBG108241.
InParanoidiQ9NTI5.
KOiK11267.
OMAiMFRIVND.
OrthoDBiEOG73Z2SD.
PhylomeDBiQ9NTI5.
TreeFamiTF106415.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE
60 70 80 90 100
EEKELYLNLA LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP
110 120 130 140 150
DKLKDIFMFI TRQLKGLEDT KSPQFNRYFY LLENIAWVKS YNICFELEDS
160 170 180 190 200
NEIFTQLYRT LFSVINNGHN QKVHMHMVDL MSSIICEGDT VSQELLDTVL
210 220 230 240 250
VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV LMLGKTSISD
260 270 280 290 300
LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
310 320 330 340 350
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD
360 370 380 390 400
LTEYLKVRSH DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK
410 420 430 440 450
RWRVRKEAMM GLAQIYKKYA LQSAAGKDAA KQIAWIKDKL LHIYYQNSID
460 470 480 490 500
DRLLVERIFA QYMVPHNLET TERMKCLYYL YATLDLNAVK ALNEMWKCQN
510 520 530 540 550
LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG KAQDFMKKFT
560 570 580 590 600
QVLEDDEKIR KQLEVLVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
610 620 630 640 650
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL
660 670 680 690 700
ELLKVLSFTH PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE
710 720 730 740 750
EDFPHIRSAL LPVLHHKSKK GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP
760 770 780 790 800
LHKSLDPSNL EHLITPLVTI GHIALLAPDQ FAAPLKSLVA TFIVKDLLMN
810 820 830 840 850
DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK NNHSKSGTST
860 870 880 890 900
LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
910 920 930 940 950
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP
960 970 980 990 1000
VKERRAHARQ CLVKNINVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA
1010 1020 1030 1040 1050
HDPDYVKVQD IEQLKDVKEC LWFVLEILMA KNENNSHAFI RKMVENIKQT
1060 1070 1080 1090 1100
KDAQGPDDAK MNEKLYTVCD VAMNIIMSKS TTYSLESPKD PVLPARFFTQ
1110 1120 1130 1140 1150
PDKNFSNTKN YLPPEMKSFF TPGKPKTTNV LGAVNKPLSS AGKQSQTKSS
1160 1170 1180 1190 1200
RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK
1210 1220 1230 1240 1250
RDDSDLVRSE LEKPRGRKKT PVTEQEEKLG MDDLTKLVQE QKPKGSQRSR
1260 1270 1280 1290 1300
KRGHTASESD EQQWPEEKRL KEDILENEDE QNSPPKKGKR GRPPKPLGGG
1310 1320 1330 1340 1350
TPKEEPTMKT SKKGSKKKSG PPAPEEEEEE ERQSGNTEQK SKSKQHRVSR
1360 1370 1380 1390 1400
RAQQRAESPE SSAIESTQST PQKGRGRPSK TPSPSQPKKN VRVGRSKQAA
1410 1420 1430 1440
TKENDSSEEV DVFQGSSPVD DIPQEETEEE EVSTVNVRRR SAKRERR
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. Curated

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:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc010abf.4. human. [Q9NTI5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5HDTX-ray2.71A/B21-1120[»]
ProteinModelPortaliQ9NTI5.
SMRiQ9NTI5. Positions 272-301, 357-417, 670-695.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116685. 52 interactions.
DIPiDIP-35420N.
IntActiQ9NTI5. 23 interactions.
MINTiMINT-3073997.
STRINGi9606.ENSP00000313851.

PTM databases

iPTMnetiQ9NTI5.
PhosphoSiteiQ9NTI5.

Polymorphism and mutation databases

BioMutaiPDS5B.
DMDMi74725312.

Proteomic databases

EPDiQ9NTI5.
MaxQBiQ9NTI5.
PaxDbiQ9NTI5.
PeptideAtlasiQ9NTI5.
PRIDEiQ9NTI5.

Protocols and materials databases

DNASUi23047.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315596; ENSP00000313851; ENSG00000083642. [Q9NTI5-1]
ENST00000450460; ENSP00000401619; ENSG00000083642. [Q9NTI5-2]
GeneIDi23047.
KEGGihsa:23047.
UCSCiuc010abf.4. human. [Q9NTI5-1]

Organism-specific databases

CTDi23047.
GeneCardsiPDS5B.
HGNCiHGNC:20418. PDS5B.
HPAiHPA039513.
HPA040015.
MIMi605333. gene.
neXtProtiNX_Q9NTI5.
PharmGKBiPA162399098.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1525. Eukaryota.
ENOG410XQW7. LUCA.
GeneTreeiENSGT00390000012488.
HOVERGENiHBG108241.
InParanoidiQ9NTI5.
KOiK11267.
OMAiMFRIVND.
OrthoDBiEOG73Z2SD.
PhylomeDBiQ9NTI5.
TreeFamiTF106415.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2468052. Establishment of Sister Chromatid Cohesion.
R-HSA-2470946. Cohesin Loading onto Chromatin.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

ChiTaRSiPDS5B. human.
GeneWikiiPDS5B.
GenomeRNAii23047.
PROiQ9NTI5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NTI5.
CleanExiHS_PDS5B.
ExpressionAtlasiQ9NTI5. baseline and differential.
GenevisibleiQ9NTI5. HS.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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].
  18. "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 WAPL AND RAD21.
  19. "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.
  20. "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].
  21. Cited for: INTERACTION WITH WAPL AND CDCA5.
  22. "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.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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].
  25. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140; SER-1166; SER-1176; SER-1182; THR-1255; SER-1257; SER-1259; SER-1283; SER-1319; SER-1358 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  26. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 6, 2016
This is version 135 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.