Q29RF7 (PDS5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sister chromatid cohesion protein PDS5 homolog A

Alternative name(s):
Cell proliferation-inducing gene 54 protein
Sister chromatid cohesion protein 112
Short name=SCC-112

Gene names

Name:	PDS5A
Synonyms:	KIAA0648, PDS5
ORF Names:	PIG54

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1337 AA.
Sequence status	Complete.
Protein existence	Evidence 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.16
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.16 Ref.19
Subcellular location	Nucleus. Note: Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase. 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of DNA replication Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular_component	chromatin Inferred from direct assay PubMed 16682347. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDCA5	Q96FF9	2	EBI-1175454,EBI-718805
RAD21	O60216	3	EBI-1175454,EBI-80739
SMC3	Q9UQE7	4	EBI-1175454,EBI-80718
STAG1	Q8WVM7	3	EBI-1175454,EBI-1175097
STAG2	Q8N3U4	3	EBI-1175454,EBI-1057252

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1337	1337	Sister chromatid cohesion protein PDS5 homolog A		PRO_0000296341
Regions
	Repeat	393 – 429	37	HEAT
Amino acid modifications
	Modified residue	1146	1	N6-acetyllysine Ref.18
	Modified residue	1195	1	Phosphoserine Ref.15 Ref.17 Ref.20
	Modified residue	1208	1	Phosphothreonine Ref.11 Ref.15 Ref.20
	Modified residue	1211	1	N6-acetyllysine Ref.18
	Modified residue	1290	1	N6-acetyllysine Ref.18
	Modified residue	1305	1	Phosphoserine Ref.3 Ref.9 Ref.11 Ref.12 Ref.14 Ref.20 Ref.22
Natural variations
	Alternative sequence	591 – 600	10	REIARKLANP → VSKSYFTLFL in isoform 2. Ref.19		VSP_052491
	Alternative sequence	601 – 1337	737	Missing in isoform 2. Ref.19		VSP_052492
Experimental info
	Sequence conflict	207	1	D → G in AAM82347. Ref.4
	Sequence conflict	471	1	Q → R in AAT52214. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: FA28EA9EF77499D9	FASTA	1,337	150,830
	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
	Isoform 2 [UniParc]. Checksum: 12917E7912C86BFD	FASTA	600	69,000
	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 VSKSYFTLFL

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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, MASS SPECTROMETRY.

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.
IPI	IPI00854642. IPI00854687.
RefSeq	NP_001093869.1. NM_001100399.1. NP_001093870.1. NM_001100400.1.
UniGene	Hs.331431.
3D structure databases
ProteinModelPortal	Q29RF7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q29RF7. 13 interactions.
STRING	9606.ENSP00000303427.
PTM databases
PhosphoSite	Q29RF7.
Polymorphism databases
DMDM	121947590.
Proteomic databases
PaxDb	Q29RF7.
PRIDE	Q29RF7.
Protocols and materials databases
DNASU	23244.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303538; ENSP00000303427; ENSG00000121892. ENST00000503396; ENSP00000426749; ENSG00000121892.
GeneID	23244.
KEGG	hsa:23244.
UCSC	uc003guv.4. human. uc003guw.4. human.
Organism-specific databases
CTD	23244.
GeneCards	GC04M039824.
HGNC	HGNC:29088. PDS5A.
HPA	HPA036662.
MIM	613200. gene.
neXtProt	NX_Q29RF7.
PharmGKB	PA162399027.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG268017.
HOGENOM	HOG000230672.
HOVERGEN	HBG108241.
InParanoid	Q29RF7.
KO	K11267.
OMA	TKDAQSP.
OrthoDB	EOG46T30N.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q29RF7.
Bgee	Q29RF7.
CleanEx	HS_PDS5A.
Genevestigator	Q29RF7.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDS5A. human.
GenomeRNAi	23244.
NextBio	44916.
SOURCE	Search...

Entry information

Entry name

PDS5A_HUMAN

Accession

Primary (citable) accession number: Q29RF7
Secondary accession number(s): Q2TTR5 , Q68DF7, Q8N7J4, Q8NG14, Q9Y4D4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	April 4, 2006
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.