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Q29RF7 (PDS5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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 A
Alternative name(s):
Cell proliferation-inducing gene 54 protein
Sister chromatid cohesion protein 112
Short name=SCC-112
Gene names
Name:PDS5A
Synonyms:KIAA0648, PDS5
ORF Names:PIG54
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.17

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.13 Ref.17 Ref.20

Subcellular location

Nucleus. Note: Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase. Ref.3 Ref.4 Ref.7

Tissue specificity

Highest level in colon. Low levels in lung, ovary, breast and kidney. Reduced level in renal tumor tissue. Isoform 2 is expressed in kidney. Ref.4

Developmental stage

Cell cycle-regulated with highest level in G2 phase. Ref.4

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. Ref.8

Sequence similarities

Belongs to the PDS5 family.

Contains 1 HEAT repeat.

Sequence caution

The sequence AAI26226.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM82347.1 differs from that shown. Reason: Probable cloning artifact.

The sequence CAH18263.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q29RF7-1)

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.4 (identifier: Q29RF7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13371337Sister chromatid cohesion protein PDS5 homolog A
PRO_0000296341

Regions

Repeat393 – 42937HEAT

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue11461N6-acetyllysine Ref.19
Modified residue11951Phosphoserine Ref.15 Ref.18 Ref.21
Modified residue12081Phosphothreonine Ref.11 Ref.15 Ref.21
Modified residue12111N6-acetyllysine Ref.19
Modified residue12901N6-acetyllysine Ref.19
Modified residue13051Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14 Ref.21 Ref.23

Natural variations

Alternative sequence591 – 60010REIARKLANP → VSKSYFTLFL in isoform 2. Ref.20
VSP_052491
Alternative sequence601 – 1337737Missing in isoform 2. Ref.20
VSP_052492

Experimental info

Sequence conflict2071D → G in AAM82347. Ref.4
Sequence conflict4711Q → R in AAT52214. Ref.1

Sequences

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

Last modified April 4, 2006. Version 1.
Checksum: FA28EA9EF77499D9

FASTA1,337150,830
        10         20         30         40         50         60 
MDFTAQPKPA TALCGVVSAD GKIAYPPGVK EITDKITTDE MIKRLKMVVK TFMDMDQDSE 

        70         80         90        100        110        120 
DEKQQYLPLA LHLASEFFLR NPNKDVRLLV ACCLADIFRI YAPEAPYTSH DKLKDIFLFI 

       130        140        150        160        170        180 
TRQLKGLEDT KSPQFNRYFY LLENLAWVKS YNICFELEDC NEIFIQLFRT LFSVINNSHN 

       190        200        210        220        230        240 
KKVQMHMLDL MSSIIMEGDG VTQELLDSIL INLIPAHKNL NKQSFDLAKV LLKRTVQTIE 

       250        260        270        280        290        300 
ACIANFFNQV LVLGRSSVSD LSEHVFDLIQ ELFAIDPHLL LSVMPQLEFK LKSNDGEERL 

       310        320        330        340        350        360 
AVVRLLAKLF GSKDSDLATQ NRPLWQCFLG RFNDIHVPVR LESVKFASHC LMNHPDLAKD 

       370        380        390        400        410        420 
LTEYLKVRSH DPEEAIRHDV IVTIITAAKR DLALVNDQLL GFVRERTLDK RWRVRKEAMM 

       430        440        450        460        470        480 
GLAQLYKKYC LHGEAGKEAA EKVSWIKDKL LHIYYQNSID DKLLVEKIFA QYLVPHNLET 

       490        500        510        520        530        540 
EERMKCLYYL YASLDPNAVK ALNEMWKCQN MLRSHVRELL DLHKQPTSEA NCSAMFGKLM 

       550        560        570        580        590        600 
TIAKNLPDPG KAQDFVKKFN QVLGDDEKLR SQLELLISPT CSCKQADICV REIARKLANP 

       610        620        630        640        650        660 
KQPTNPFLEM VKFLLERIAP VHIDSEAISA LVKLMNKSIE GTADDEEEGV SPDTAIRSGL 

       670        680        690        700        710        720 
ELLKVLSFTH PTSFHSAETY ESLLQCLRME DDKVAEAAIQ IFRNTGHKIE TDLPQIRSTL 

       730        740        750        760        770        780 
IPILHQKAKR GTPHQAKQAV HCIHAIFTNK EVQLAQIFEP LSRSLNADVP EQLITPLVSL 

       790        800        810        820        830        840 
GHISMLAPDQ FASPMKSVVA NFIVKDLLMN DRSTGEKNGK LWSPDEEVSP EVLAKVQAIK 

       850        860        870        880        890        900 
LLVRWLLGMK NNQSKSANST LRLLSAMLVS EGDLTEQKRI SKSDMSRLRL AAGSAIMKLA 

       910        920        930        940        950        960 
QEPCYHEIIT PEQFQLCALV INDECYQVRQ IFAQKLHKAL VKLLLPLEYM AIFALCAKDP 

       970        980        990       1000       1010       1020 
VKERRAHARQ CLLKNISIRR EYIKQNPMAT EKLLSLLPEY VVPYMIHLLA HDPDFTRSQD 

      1030       1040       1050       1060       1070       1080 
VDQLRDIKEC LWFMLEVLMT KNENNSHAFM KKMAENIKLT RDAQSPDESK TNEKLYTVCD 

      1090       1100       1110       1120       1130       1140 
VALCVINSKS ALCNADSPKD PVLPMKFFTQ PEKDFCNDKS YISEETRVLL LTGKPKPAGV 

      1150       1160       1170       1180       1190       1200 
LGAVNKPLSA TGRKPYVRST GTETGSNINV NSELNPSTGN RSREQSSEAA ETGVSENEEN 

      1210       1220       1230       1240       1250       1260 
PVRIISVTPV KNIDPVKNKE INSDQATQGN ISSDRGKKRT VTAAGAENIQ QKTDEKVDES 

      1270       1280       1290       1300       1310       1320 
GPPAPSKPRR GRRPKSESQG NATKNDDLNK PINKGRKRAA VGQESPGGLE AGNAKAPKLQ 

      1330 
DLAKKAAPAE RQIDLQR 

« Hide

Isoform 2 [UniParc].

Checksum: 12917E7912C86BFD
Show »

FASTA60069,000

References

« Hide 'large scale' references
[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. 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 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"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-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]"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.
[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]"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].
[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001093869.1. NM_001100399.1.
NP_001093870.1. NM_001100400.1.
XP_005262709.1. XM_005262652.1.
UniGeneHs.331431.

3D structure databases

ProteinModelPortalQ29RF7.
SMRQ29RF7. Positions 78-122, 292-350, 360-428, 682-711.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116848. 26 interactions.
IntActQ29RF7. 14 interactions.
STRING9606.ENSP00000303427.

PTM databases

PhosphoSiteQ29RF7.

Polymorphism databases

DMDM121947590.

Proteomic databases

PaxDbQ29RF7.
PRIDEQ29RF7.

Protocols and materials databases

DNASU23244.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303538; ENSP00000303427; ENSG00000121892. [Q29RF7-1]
ENST00000503396; ENSP00000426749; ENSG00000121892. [Q29RF7-3]
GeneID23244.
KEGGhsa:23244.
UCSCuc003guv.4. human. [Q29RF7-1]
uc003guw.4. human. [Q29RF7-3]

Organism-specific databases

CTD23244.
GeneCardsGC04M039824.
HGNCHGNC:29088. PDS5A.
HPAHPA036661.
HPA036662.
MIM613200. gene.
neXtProtNX_Q29RF7.
PharmGKBPA162399027.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268017.
HOGENOMHOG000230672.
HOVERGENHBG108241.
InParanoidQ29RF7.
KOK11267.
OMANLNKQAF.
OrthoDBEOG73Z2SD.
PhylomeDBQ29RF7.
TreeFamTF106415.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ29RF7.
BgeeQ29RF7.
CleanExHS_PDS5A.
GenevestigatorQ29RF7.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

ChiTaRSPDS5A. human.
GeneWikiPDS5A.
GenomeRNAi23244.
NextBio44916.
PROQ29RF7.
SOURCESearch...

Entry information

Entry namePDS5A_HUMAN
AccessionPrimary (citable) accession number: Q29RF7
Secondary accession number(s): Q2TTR5 expand/collapse secondary AC list , Q68DF7, Q8N7J4, Q8NG14, Q9Y4D4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 82 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 4

Human chromosome 4: entries, gene names and cross-references to MIM