Q15435 (PP1R7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 1 regulatory subunit 7

Alternative name(s):
Protein phosphatase 1 regulatory subunit 22

Gene names

Name:	PPP1R7
Synonyms:	SDS22

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	360 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	protein phosphatase type 1 regulator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	Protein phosphatase 1 regulatory subunit 7		PRO_0000239613
Regions
	Repeat	77 – 98	22	LRR 1
	Repeat	99 – 120	22	LRR 2
	Repeat	121 – 142	22	LRR 3
	Repeat	143 – 164	22	LRR 4
	Repeat	165 – 186	22	LRR 5
	Repeat	187 – 208	22	LRR 6
	Repeat	209 – 230	22	LRR 7
	Repeat	231 – 252	22	LRR 8
	Repeat	253 – 274	22	LRR 9
	Repeat	275 – 296	22	LRR 10
	Repeat	297 – 318	22	LRR 11
	Domain	331 – 360	30	LRRCT
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.11
	Modified residue	24	1	Phosphoserine Ref.8 Ref.9 Ref.11
	Modified residue	27	1	Phosphoserine Ref.8 Ref.9 Ref.11
	Modified residue	44	1	Phosphoserine Ref.9
	Modified residue	47	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	18 – 60	43	Missing in isoform 2 and isoform 4.		VSP_019244
	Alternative sequence	274 – 280	7	NKLTMLD → VQDSLTY in isoform 3 and isoform 4.		VSP_019245
	Alternative sequence	281 – 360	80	Missing in isoform 3 and isoform 4.		VSP_019246
Experimental info
	Mutagenesis	148	1	D → V: Completely abolishes the interaction with protein phosphatase 1. Ref.7
	Mutagenesis	170	1	F → A: Severely impaired the binding of protein phosphatase 1. Ref.7
	Mutagenesis	192	1	E → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
	Mutagenesis	214	1	F → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
	Mutagenesis	280	1	D → A: Severely impairs the binding of protein phosphatase 1. Ref.7
	Mutagenesis	300	1	E → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
	Mutagenesis	302	1	W → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7
	Mutagenesis	327	1	Y → A: Completely abolishes the interaction with protein phosphatase 1. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (sds22alpha1) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 49BCCF675EAA94D1	FASTA	360	41,564
	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
	Isoform 2 (sds22alpha2) [UniParc]. Checksum: 9AC120B3C729CF8B	FASTA	317	36,837
	10 20 30 40 50 60 MAAERGAGQQ QSQEMMEEEH ELPVDMETIN LDRDAEDVDL NHYRIGKIEG FEVLKKVKTL 70 80 90 100 110 120 CLRQNLIKCI ENLEELQSLR ELDLYDNQIK KIENLEALTE LEILDISFNL LRNIEGVDKL 130 140 150 160 170 180 TRLKKLFLVN NKISKIENLS NLHQLQMLEL GSNRIRAIEN IDTLTNLESL FLGKNKITKL 190 200 210 220 230 240 QNLDALTNLT VLSMQSNRLT KIEGLQNLVN LRELYLSHNG IEVIEGLENN NKLTMLDIAS 250 260 270 280 290 300 NRIKKIENIS HLTELQEFWM NDNLLESWSD LDELKGARSL ETVYLERNPL QKDPQYRRKV 310 MLALPSVRQI DATFVRF
	Isoform 3 (sds22beta1) [UniParc]. Checksum: 4FE43AE30C65AB72	FASTA	280	32,053
	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 RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNVQDSLTY
	Isoform 4 (sds22beta2) [UniParc]. Checksum: 627A59386B5763BB	FASTA	237	27,326
	10 20 30 40 50 60 MAAERGAGQQ QSQEMMEEEH ELPVDMETIN LDRDAEDVDL NHYRIGKIEG FEVLKKVKTL 70 80 90 100 110 120 CLRQNLIKCI ENLEELQSLR ELDLYDNQIK KIENLEALTE LEILDISFNL LRNIEGVDKL 130 140 150 160 170 180 TRLKKLFLVN NKISKIENLS NLHQLQMLEL GSNRIRAIEN IDTLTNLESL FLGKNKITKL 190 200 210 220 230 QNLDALTNLT VLSMQSNRLT KIEGLQNLVN LRELYLSHNG IEVIEGLENN VQDSLTY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z50749 mRNA. Translation: CAA90626.1. AF067136 , AF067130, AF067132, AF067133, AF067134, AF067135 Genomic DNA. Translation: AAD26610.1. AF067136 , AF067130, AF067132, AF067134, AF067135, AF067133, AF067131 Genomic DNA. Translation: AAD26611.1. AF067134 , AF067130, AF067131, AF067132, AF067133 Genomic DNA. Translation: AAD26612.1. AF067134 , 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.
IPI	IPI00033600. IPI00395771. IPI00759705. IPI00759816.
PIR	S68209.
RefSeq	NP_002703.1. NM_002712.1.
UniGene	Hs.36587.
3D structure databases
ProteinModelPortal	Q15435.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1005N.
IntAct	Q15435. 9 interactions.
MINT	MINT-5004667.
STRING	9606.ENSP00000234038.
PTM databases
PhosphoSite	Q15435.
Polymorphism databases
DMDM	74762145.
2D gel databases
REPRODUCTION-2DPAGE	IPI00033600.
Proteomic databases
PaxDb	Q15435.
PRIDE	Q15435.
Protocols and materials databases
DNASU	5510.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000234038; ENSP00000234038; ENSG00000115685. ENST00000272983; ENSP00000272983; ENSG00000115685. ENST00000401987; ENSP00000385466; ENSG00000115685. ENST00000406106; ENSP00000385022; ENSG00000115685. ENST00000407025; ENSP00000385657; ENSG00000115685.
GeneID	5510.
KEGG	hsa:5510.
UCSC	uc002was.3. human. uc002wat.1. human. uc002wau.1. human.
Organism-specific databases
CTD	5510.
GeneCards	GC02P242088.
HGNC	HGNC:9295. PPP1R7.
HPA	HPA034501.
MIM	602877. gene.
neXtProt	NX_Q15435.
PharmGKB	PA33658.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000211189.
HOVERGEN	HBG082161.
InParanoid	Q15435.
OMA	PQYRRKI.
OrthoDB	EOG4894MX.
PhylomeDB	Q15435.
Gene expression databases
ArrayExpress	Q15435.
Bgee	Q15435.
CleanEx	HS_PPP1R7.
Genevestigator	Q15435.
GermOnline	ENSG00000115685. Homo sapiens.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR025875. Leu-rich_rpt_4. IPR003603. U2A'_phosphoprotein32A_C. [Graphical view]
Pfam	PF12799. LRR_4. 5 hits. [Graphical view]
SMART	SM00446. LRRcap. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 12 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPP1R7. human.
GenomeRNAi	5510.
NextBio	21312.
SOURCE	Search...

Entry information

Entry name

PP1R7_HUMAN

Accession

Primary (citable) accession number: Q15435
Secondary accession number(s): B4DFD4 , Q9UQE5, Q9UQE6, Q9Y6K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 118 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.