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Q15435 (PP1R7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1 regulatory subunit 7
Alternative name(s):
Protein phosphatase 1 regulatory subunit 22
Gene names
Name:PPP1R7
Synonyms:SDS22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of protein phosphatase 1 By similarity.

Subunit structure

Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1. Ref.7

Subcellular location

Nucleus By similarity.

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Belongs to the SDS22 family.

Contains 11 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15435-1)

Also known as: sds22alpha1;

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: Q15435-2)

Also known as: sds22alpha2;

The sequence of this isoform differs from the canonical sequence as follows:
     18-60: Missing.
Isoform 3 (identifier: Q15435-3)

Also known as: sds22beta1;

The sequence of this isoform differs from the canonical sequence as follows:
     274-280: NKLTMLD → VQDSLTY
     281-360: Missing.
Isoform 4 (identifier: Q15435-4)

Also known as: sds22beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     18-60: Missing.
     274-280: NKLTMLD → VQDSLTY
     281-360: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 360359Protein phosphatase 1 regulatory subunit 7
PRO_0000239613

Regions

Repeat77 – 9822LRR 1
Repeat99 – 12022LRR 2
Repeat121 – 14222LRR 3
Repeat143 – 16422LRR 4
Repeat165 – 18622LRR 5
Repeat187 – 20822LRR 6
Repeat209 – 23022LRR 7
Repeat231 – 25222LRR 8
Repeat253 – 27422LRR 9
Repeat275 – 29622LRR 10
Repeat297 – 31822LRR 11
Domain331 – 36030LRRCT

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue121Phosphoserine Ref.12
Modified residue241Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue271Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue441Phosphoserine Ref.10
Modified residue471Phosphoserine Ref.10

Natural variations

Alternative sequence18 – 6043Missing in isoform 2 and isoform 4.
VSP_019244
Alternative sequence274 – 2807NKLTMLD → VQDSLTY in isoform 3 and isoform 4.
VSP_019245
Alternative sequence281 – 36080Missing in isoform 3 and isoform 4.
VSP_019246

Experimental info

Mutagenesis1481D → V: Completely abolishes the interaction with protein phosphatase 1. Ref.7
Mutagenesis1701F → A: Severely impaired the binding of protein phosphatase 1. Ref.7
Mutagenesis1921E → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
Mutagenesis2141F → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
Mutagenesis2801D → A: Severely impairs the binding of protein phosphatase 1. Ref.7
Mutagenesis3001E → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
Mutagenesis3021W → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
Mutagenesis3271Y → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (sds22alpha1) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 49BCCF675EAA94D1

FASTA36041,564
        10         20         30         40         50         60 
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD GEERGEEDPE 

        70         80         90        100        110        120 
EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV KTLCLRQNLI KCIENLEELQ 

       130        140        150        160        170        180 
SLRELDLYDN QIKKIENLEA LTELEILDIS FNLLRNIEGV DKLTRLKKLF LVNNKISKIE 

       190        200        210        220        230        240 
NLSNLHQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN 

       250        260        270        280        290        300 
RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE 

       310        320        330        340        350        360 
FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV RQIDATFVRF 

« Hide

Isoform 2 (sds22alpha2) [UniParc].

Checksum: 9AC120B3C729CF8B
Show »

FASTA31736,837
Isoform 3 (sds22beta1) [UniParc].

Checksum: 4FE43AE30C65AB72
Show »

FASTA28032,053
Isoform 4 (sds22beta2) [UniParc].

Checksum: 627A59386B5763BB
Show »

FASTA23727,326

References

« Hide 'large scale' references
[1]"Molecular cloning of a human polypeptide related to yeast sds22, a regulator of protein phosphatase-1."
Renouf S., Beullens M., Wera S., Van Eynde A., Sikela J., Stalmans W., Bollen M.
FEBS Lett. 375:75-78(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Structure and splice products of the human gene encoding sds22, a putative mitotic regulator of protein phosphatase-1."
Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M., Stalmans W., Bollen M.
Eur. J. Biochem. 262:36-42(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
[4]"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: Cerebellum.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 3).
Tissue: Cervix.
[7]"Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC ISOFORM 1, MUTAGENESIS OF ASP-148; PHE-170; GLU-192; PHE-214; ASP-280; GLU-300; TRP-302 AND TYR-327.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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-24; SER-27; SER-44 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-12; SER-24 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50749 mRNA. Translation: CAA90626.1.
AF067136 expand/collapse EMBL AC list , AF067130, AF067132, AF067133, AF067134, AF067135 Genomic DNA. Translation: AAD26610.1.
AF067136 expand/collapse EMBL AC list , AF067130, AF067132, AF067134, AF067135, AF067133, AF067131 Genomic DNA. Translation: AAD26611.1.
AF067134 expand/collapse EMBL AC list , AF067130, AF067131, AF067132, AF067133 Genomic DNA. Translation: AAD26612.1.
AF067134 expand/collapse EMBL AC list , AF067132, AF067130, AF067133 Genomic DNA. Translation: AAD26613.1.
BT007296 mRNA. Translation: AAP35960.1.
BT020134 mRNA. Translation: AAV38936.1.
AK294043 mRNA. Translation: BAG57395.1.
CH471063 Genomic DNA. Translation: EAW71243.1.
BC000910 mRNA. Translation: AAH00910.1.
BC012397 mRNA. Translation: AAH12397.1.
BC013001 mRNA. Translation: AAH13001.1.
PIRS68209.
RefSeqNP_001269338.1. NM_001282409.1.
NP_001269339.1. NM_001282410.1.
NP_001269340.1. NM_001282411.1.
NP_001269341.1. NM_001282412.1.
NP_001269342.1. NM_001282413.1.
NP_001269343.1. NM_001282414.1.
NP_002703.1. NM_002712.2.
UniGeneHs.36587.

3D structure databases

ProteinModelPortalQ15435.
SMRQ15435. Positions 77-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111502. 17 interactions.
DIPDIP-1005N.
IntActQ15435. 11 interactions.
MINTMINT-5004667.
STRING9606.ENSP00000234038.

PTM databases

PhosphoSiteQ15435.

Polymorphism databases

DMDM74762145.

2D gel databases

REPRODUCTION-2DPAGEIPI00033600.

Proteomic databases

PaxDbQ15435.
PRIDEQ15435.

Protocols and materials databases

DNASU5510.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234038; ENSP00000234038; ENSG00000115685. [Q15435-1]
ENST00000272983; ENSP00000272983; ENSG00000115685. [Q15435-2]
ENST00000401987; ENSP00000385466; ENSG00000115685. [Q15435-4]
ENST00000406106; ENSP00000385022; ENSG00000115685. [Q15435-3]
ENST00000407025; ENSP00000385657; ENSG00000115685. [Q15435-1]
GeneID5510.
KEGGhsa:5510.
UCSCuc002was.3. human. [Q15435-3]
uc002wat.1. human. [Q15435-1]
uc002wau.1. human. [Q15435-2]

Organism-specific databases

CTD5510.
GeneCardsGC02P242088.
HGNCHGNC:9295. PPP1R7.
HPAHPA034500.
HPA034501.
MIM602877. gene.
neXtProtNX_Q15435.
PharmGKBPA33658.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000211189.
HOVERGENHBG082161.
InParanoidQ15435.
KOK17550.
OMAQRICLRQ.
PhylomeDBQ15435.
TreeFamTF105538.

Gene expression databases

ArrayExpressQ15435.
BgeeQ15435.
CleanExHS_PPP1R7.
GenevestigatorQ15435.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR027733. PPP1R7.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
PANTHERPTHR10588:SF96. PTHR10588:SF96. 1 hit.
PfamPF12799. LRR_4. 2 hits.
[Graphical view]
SMARTSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 12 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1R7. human.
GeneWikiPPP1R7.
GenomeRNAi5510.
NextBio21312.
PROQ15435.
SOURCESearch...

Entry information

Entry namePP1R7_HUMAN
AccessionPrimary (citable) accession number: Q15435
Secondary accession number(s): B4DFD4 expand/collapse secondary AC list , Q9UQE5, Q9UQE6, Q9Y6K4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 127 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 2

Human chromosome 2: entries, gene names and cross-references to MIM