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Q5H9R7 (PP6R3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Serine/threonine-protein phosphatase 6 regulatory subunit 3
Alternative name(s):
SAPS domain family member 3
Sporulation-induced transcript 4-associated protein SAPL
Gene names
Name:PPP6R3
Synonyms:C11orf23, KIAA1558, PP6R3, SAPL, SAPS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length873 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance. Ref.1 Ref.3

Subunit structure

Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6C and ANKRD28. Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.3 Ref.10.

Tissue specificity

Expressed in skeletal muscle, placenta, heart, pancreas, testis, brain, lung, liver, kidney, spleen, thymus, prostate, small intestine, colon and leukocytes. Ref.1 Ref.3

Sequence similarities

Belongs to the SAPS family.

Sequence caution

The sequence AAZ99639.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA91978.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB13384.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB71396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ANKRD28O150845EBI-355498,EBI-359567
PPP6CO007435EBI-355498,EBI-359751

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5H9R7-1)

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 (identifier: Q5H9R7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     544-549: Missing.
Isoform 3 (identifier: Q5H9R7-3)

Also known as: B; C11orf23b; SAPLb;

The sequence of this isoform differs from the canonical sequence as follows:
     326-376: Missing.
     516-544: Missing.
     857-873: RTGQPSAPGDTSVNGPV → SGVEIPALPGQWSQQ
Isoform 4 (identifier: Q5H9R7-4)

Also known as: A; C11orf23a; SAPLa;

The sequence of this isoform differs from the canonical sequence as follows:
     326-376: Missing.
     516-544: Missing.
Isoform 5 (identifier: Q5H9R7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     817-817: S → RVLKSYR
Isoform 6 (identifier: Q5H9R7-6)

The sequence of this isoform differs from the canonical sequence as follows:
     516-544: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 873873Serine/threonine-protein phosphatase 6 regulatory subunit 3
PRO_0000046100

Amino acid modifications

Modified residue5791Phosphoserine Ref.9 Ref.15 Ref.16 Ref.18
Modified residue6171Phosphoserine Ref.8 Ref.11 Ref.14 Ref.15 Ref.16 Ref.18
Modified residue7221Phosphoserine Ref.12
Modified residue8531Phosphoserine By similarity

Natural variations

Alternative sequence326 – 37651Missing in isoform 3 and isoform 4.
VSP_017140
Alternative sequence516 – 54429Missing in isoform 3, isoform 4 and isoform 6.
VSP_017141
Alternative sequence544 – 5496Missing in isoform 2.
VSP_017142
Alternative sequence8171S → RVLKSYR in isoform 5.
VSP_017143
Alternative sequence857 – 87317RTGQP…VNGPV → SGVEIPALPGQWSQQ in isoform 3.
VSP_017144
Natural variant8421A → V.
Corresponds to variant rs34009811 [ dbSNP | Ensembl ].
VAR_057720

Experimental info

Sequence conflict2921P → S in CAH18675. Ref.5
Sequence conflict4431M → V in BAB71396. Ref.7
Sequence conflict4771N → S in CAI45957. Ref.5
Sequence conflict6771L → P in CAI45957. Ref.5

Sequences

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

Last modified February 7, 2006. Version 2.
Checksum: 5B4C69991E7DE16F

FASTA87397,669
        10         20         30         40         50         60 
MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK AECLEDLVSF 

        70         80         90        100        110        120 
IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE SLLMKLYSFL LNDSPLNPLL 

       130        140        150        160        170        180 
ASFFSKVLSI LISRKPEQIV DFLKKKHDFV DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ 

       190        200        210        220        230        240 
DVLNWLNEEK IIQRLVEIVH PSQEEDRHSN ASQSLCEIVR LSRDQMLQIQ NSTEPDPLLA 

       250        260        270        280        290        300 
TLEKQEIIEQ LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS 

       310        320        330        340        350        360 
VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGVLDPPV GNTRLNVIRL ISSLLQTNTS 

       370        380        390        400        410        420 
SINGDLMELN SIGVILNMFF KYTWNNFLHT QVEICIALIL ASPFENTENA TITDQDSTGD 

       430        440        450        460        470        480 
NLLLKHLFQK CQLIERILEA WEMNEKKQAE GGRRHGYMGH LTRIANCIVH STDKGPNSAL 

       490        500        510        520        530        540 
VQQLIKDLPD EVRERWETFC TSSLGETNKR NTVDLVTTCH IHSSSDDEID FKETGFSQDS 

       550        560        570        580        590        600 
SLQQAFSDYQ MQQMTSNFID QFGFNDEKFA DQDDIGNVSF DRVSDINFTL NTNESGNIAL 

       610        620        630        640        650        660 
FEACCKERIQ QFDDGGSDEE DIWEEKHIAF TPESQRRSSS GSTDSEESTD SEEEDGAKQD 

       670        680        690        700        710        720 
LFEPSSANTE DKMEVDLSEP PNWSANFDVP METTHGAPLD SVGSDVWSTE EPMPTKETGW 

       730        740        750        760        770        780 
ASFSEFTSSL STKDSLRSNS PVEMETSTEP MDPLTPSAAA LAVQPEAAGS VAMEASSDGE 

       790        800        810        820        830        840 
EDAESTDKVT ETVMNGGMKE TLSLTVDAKT ETAVFKSEEG KLSTSQDAAC KDAEECPETA 

       850        860        870 
EAKCAAPRPP SSSPEQRTGQ PSAPGDTSVN GPV 

« Hide

Isoform 2 [UniParc].

Checksum: 9E76BCA0E23EE3DE
Show »

FASTA86796,957
Isoform 3 (B) (C11orf23b) (SAPLb) [UniParc].

Checksum: 1C936F03A484D53D
Show »

FASTA79188,909
Isoform 4 (A) (C11orf23a) (SAPLa) [UniParc].

Checksum: AC5BEE22285932F4
Show »

FASTA79388,952
Isoform 5 [UniParc].

Checksum: E0AE6571756853C1
Show »

FASTA87998,485
Isoform 6 [UniParc].

Checksum: ADB89AA9C567C580
Show »

FASTA84494,445

References

« Hide 'large scale' references
[1]"The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13."
Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.
Genomics 72:231-242(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, TISSUE SPECIFICITY.
[2]Guergnon J., Stefansson B., Brautigan D.L.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION.
[3]"Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon."
Stefansson B., Brautigan D.L.
J. Biol. Chem. 281:22624-22634(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-873 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[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] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-873 (ISOFORMS 1/2/4/6).
Tissue: Colon carcinoma, Melanoma and Seminal plasma.
[6]"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 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 650-873 (ISOFORMS 1/2/4/6).
Tissue: Muscle.
[7]"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] OF 221-873 (ISOFORM 1).
Tissue: Placenta and Testis.
[8]"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-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains."
Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.
Biochemistry 47:1442-1451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP6C AND ANKRD28.
[11]"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-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"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-579 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF264779 mRNA. Translation: AAG36934.1.
AF264780 mRNA. Translation: AAG36935.1.
DQ111954 mRNA. Translation: AAZ99639.2. Different initiation.
AB046778 mRNA. Translation: BAB13384.2. Different initiation.
AL834471 mRNA. Translation: CAD39130.1.
CR749815 mRNA. Translation: CAH18675.1.
CR933658 mRNA. Translation: CAI45957.1.
BC007738 mRNA. Translation: AAH07738.2.
BC105933 mRNA. Translation: AAI05934.1.
BC105934 mRNA. Translation: AAI05935.1.
BC107599 mRNA. Translation: AAI07600.1.
AK001920 mRNA. Translation: BAA91978.1. Different initiation.
AK057250 mRNA. Translation: BAB71396.1. Different initiation.
CCDSCCDS53671.1. [Q5H9R7-5]
CCDS53672.1. [Q5H9R7-1]
CCDS53673.1. [Q5H9R7-2]
CCDS53674.1. [Q5H9R7-6]
CCDS53675.1. [Q5H9R7-3]
CCDS8182.1. [Q5H9R7-4]
RefSeqNP_001157632.1. NM_001164160.1. [Q5H9R7-5]
NP_001157633.1. NM_001164161.1. [Q5H9R7-1]
NP_001157634.1. NM_001164162.1. [Q5H9R7-2]
NP_001157635.1. NM_001164163.1. [Q5H9R7-6]
NP_001157636.1. NM_001164164.1. [Q5H9R7-3]
NP_060782.2. NM_018312.4. [Q5H9R7-4]
XP_006718676.1. XM_006718613.1. [Q5H9R7-1]
XP_006718677.1. XM_006718614.1. [Q5H9R7-2]
XP_006718681.1. XM_006718618.1. [Q5H9R7-6]
XP_006718687.1. XM_006718624.1. [Q5H9R7-4]
UniGeneHs.503022.

3D structure databases

ProteinModelPortalQ5H9R7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120579. 51 interactions.
IntActQ5H9R7. 14 interactions.
MINTMINT-5004961.

PTM databases

PhosphoSiteQ5H9R7.

Polymorphism databases

DMDM88941982.

Proteomic databases

MaxQBQ5H9R7.
PaxDbQ5H9R7.
PRIDEQ5H9R7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265636; ENSP00000265636; ENSG00000110075. [Q5H9R7-4]
ENST00000393800; ENSP00000377389; ENSG00000110075. [Q5H9R7-1]
ENST00000393801; ENSP00000377390; ENSG00000110075. [Q5H9R7-5]
ENST00000524845; ENSP00000431415; ENSG00000110075. [Q5H9R7-6]
ENST00000524904; ENSP00000433058; ENSG00000110075. [Q5H9R7-2]
ENST00000529710; ENSP00000437329; ENSG00000110075. [Q5H9R7-3]
GeneID55291.
KEGGhsa:55291.
UCSCuc001onu.3. human. [Q5H9R7-4]
uc001onv.3. human. [Q5H9R7-5]
uc001onw.3. human. [Q5H9R7-1]
uc001onx.3. human. [Q5H9R7-2]
uc001ony.4. human. [Q5H9R7-6]
uc009ysh.3. human. [Q5H9R7-3]

Organism-specific databases

CTD55291.
GeneCardsGC11P068229.
HGNCHGNC:1173. PPP6R3.
HPACAB017183.
HPA038467.
HPA038468.
MIM610879. gene.
neXtProtNX_Q5H9R7.
PharmGKBPA25487.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303042.
HOVERGENHBG069733.
KOK15501.
OrthoDBEOG7PGDQ3.
PhylomeDBQ5H9R7.
TreeFamTF313227.

Gene expression databases

ArrayExpressQ5H9R7.
BgeeQ5H9R7.
GenevestigatorQ5H9R7.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR007587. SAPS.
[Graphical view]
PANTHERPTHR12634. PTHR12634. 1 hit.
PfamPF04499. SAPS. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPP6R3. human.
GenomeRNAi55291.
NextBio59478.
PROQ5H9R7.
SOURCESearch...

Entry information

Entry namePP6R3_HUMAN
AccessionPrimary (citable) accession number: Q5H9R7
Secondary accession number(s): Q3B7I1 expand/collapse secondary AC list , Q3I4Y0, Q3KR35, Q68CR3, Q7L4R8, Q8N3B2, Q96MB2, Q9H2K5, Q9H2K6, Q9HCL4, Q9NUY3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 94 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM