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Protein

Protein phosphatase 1 regulatory subunit 7

Gene

PPP1R7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of protein phosphatase 1.By similarity

GO - Molecular functioni

  1. enzyme regulator activity Source: UniProtKB
  2. protein phosphatase type 1 regulator activity Source: ProtInc

GO - Biological processi

  1. chromosome segregation Source: Ensembl
  2. positive regulation of protein dephosphorylation Source: MGI
  3. regulation of catalytic activity Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 7
Alternative name(s):
Protein phosphatase 1 regulatory subunit 22
Gene namesi
Name:PPP1R7
Synonyms:SDS22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9295. PPP1R7.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. chromosome Source: MGI
  2. cytoplasm Source: ProtInc
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481D → V: Completely abolishes the interaction with protein phosphatase 1. 1 Publication
Mutagenesisi170 – 1701F → A: Severely impaired the binding of protein phosphatase 1. 1 Publication
Mutagenesisi192 – 1921E → A: Completely abolishes the interaction with protein phosphatase 1. 1 Publication
Mutagenesisi214 – 2141F → A: Completely abolishes the interaction with protein phosphatase 1. 1 Publication
Mutagenesisi280 – 2801D → A: Severely impairs the binding of protein phosphatase 1. 1 Publication
Mutagenesisi300 – 3001E → A: Completely abolishes the interaction with protein phosphatase 1. 1 Publication
Mutagenesisi302 – 3021W → A: Completely abolishes the interaction with protein phosphatase 1. 1 Publication
Mutagenesisi327 – 3271Y → A: Completely abolishes the interaction with protein phosphatase 1. 1 Publication

Organism-specific databases

PharmGKBiPA33658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 360359Protein phosphatase 1 regulatory subunit 7PRO_0000239613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei12 – 121Phosphoserine1 Publication
Modified residuei24 – 241Phosphoserine3 Publications
Modified residuei27 – 271Phosphoserine4 Publications
Modified residuei44 – 441Phosphoserine2 Publications
Modified residuei47 – 471Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15435.
PaxDbiQ15435.
PRIDEiQ15435.

2D gel databases

REPRODUCTION-2DPAGEIPI00033600.

PTM databases

PhosphoSiteiQ15435.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ15435.
CleanExiHS_PPP1R7.
ExpressionAtlasiQ15435. baseline and differential.
GenevestigatoriQ15435.

Organism-specific databases

HPAiHPA034500.
HPA034501.

Interactioni

Subunit structurei

Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1.1 Publication

Protein-protein interaction databases

BioGridi111502. 23 interactions.
DIPiDIP-1005N.
IntActiQ15435. 12 interactions.
MINTiMINT-5004667.
STRINGi9606.ENSP00000234038.

Structurei

3D structure databases

ProteinModelPortaliQ15435.
SMRiQ15435. Positions 77-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati77 – 9822LRR 1Add
BLAST
Repeati99 – 12022LRR 2Add
BLAST
Repeati121 – 14222LRR 3Add
BLAST
Repeati143 – 16422LRR 4Add
BLAST
Repeati165 – 18622LRR 5Add
BLAST
Repeati187 – 20822LRR 6Add
BLAST
Repeati209 – 23022LRR 7Add
BLAST
Repeati231 – 25222LRR 8Add
BLAST
Repeati253 – 27422LRR 9Add
BLAST
Repeati275 – 29622LRR 10Add
BLAST
Repeati297 – 31822LRR 11Add
BLAST
Domaini331 – 36030LRRCTAdd
BLAST

Sequence similaritiesi

Belongs to the SDS22 family.Curated
Contains 11 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00730000110223.
HOGENOMiHOG000211189.
HOVERGENiHBG082161.
InParanoidiQ15435.
KOiK17550.
OMAiQRICLRQ.
PhylomeDBiQ15435.
TreeFamiTF105538.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
PfamiPF12799. LRR_4. 2 hits.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 12 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15435-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD
60 70 80 90 100
GEERGEEDPE EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV
110 120 130 140 150
KTLCLRQNLI KCIENLEELQ SLRELDLYDN QIKKIENLEA LTELEILDIS
160 170 180 190 200
FNLLRNIEGV DKLTRLKKLF LVNNKISKIE NLSNLHQLQM LELGSNRIRA
210 220 230 240 250
IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN RLTKIEGLQN
260 270 280 290 300
LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE
310 320 330 340 350
FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV
360
RQIDATFVRF
Length:360
Mass (Da):41,564
Last modified:November 1, 1996 - v1
Checksum:i49BCCF675EAA94D1
GO
Isoform 2 (identifier: Q15435-2) [UniParc]FASTAAdd to basket

Also known as: sds22alpha2

The sequence of this isoform differs from the canonical sequence as follows:
     18-60: Missing.

Show »
Length:317
Mass (Da):36,837
Checksum:i9AC120B3C729CF8B
GO
Isoform 3 (identifier: Q15435-3) [UniParc]FASTAAdd to basket

Also known as: sds22beta1

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

Show »
Length:280
Mass (Da):32,053
Checksum:i4FE43AE30C65AB72
GO
Isoform 4 (identifier: Q15435-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:237
Mass (Da):27,326
Checksum:i627A59386B5763BB
GO
Isoform 5 (identifier: Q15435-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHSSGIVADLSEQSLKDGEERGEEDPE → M
     274-280: NKLTMLD → VQDSLTY
     281-360: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:221
Mass (Da):25,593
Checksum:i9AB66B080F2F52C0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060MAAER…EEDPE → M in isoform 5. CuratedVSP_055672Add
BLAST
Alternative sequencei18 – 6043Missing in isoform 2 and isoform 4. 1 PublicationVSP_019244Add
BLAST
Alternative sequencei274 – 2807NKLTMLD → VQDSLTY in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_019245
Alternative sequencei281 – 36080Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_019246Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AC005237 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW71243.1.
BC000910 mRNA. Translation: AAH00910.1.
BC012397 mRNA. Translation: AAH12397.1.
BC013001 mRNA. Translation: AAH13001.1.
CCDSiCCDS2546.1. [Q15435-1]
CCDS63190.1. [Q15435-5]
CCDS63192.1. [Q15435-3]
CCDS63193.1. [Q15435-4]
CCDS63194.1. [Q15435-2]
PIRiS68209.
RefSeqiNP_001269338.1. NM_001282409.1. [Q15435-2]
NP_001269339.1. NM_001282410.1. [Q15435-3]
NP_001269340.1. NM_001282411.1. [Q15435-4]
NP_001269341.1. NM_001282412.1.
NP_001269342.1. NM_001282413.1.
NP_001269343.1. NM_001282414.1. [Q15435-5]
NP_002703.1. NM_002712.2. [Q15435-1]
UniGeneiHs.36587.

Genome annotation databases

EnsembliENST00000234038; ENSP00000234038; ENSG00000115685. [Q15435-1]
ENST00000272983; ENSP00000272983; ENSG00000115685. [Q15435-2]
ENST00000401987; ENSP00000385466; ENSG00000115685. [Q15435-4]
ENST00000402734; ENSP00000385012; ENSG00000115685. [Q15435-5]
ENST00000406106; ENSP00000385022; ENSG00000115685. [Q15435-3]
ENST00000407025; ENSP00000385657; ENSG00000115685. [Q15435-1]
GeneIDi5510.
KEGGihsa:5510.
UCSCiuc002was.3. human. [Q15435-3]
uc002wat.1. human. [Q15435-1]
uc002wau.1. human. [Q15435-2]

Polymorphism databases

DMDMi74762145.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AC005237 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW71243.1.
BC000910 mRNA. Translation: AAH00910.1.
BC012397 mRNA. Translation: AAH12397.1.
BC013001 mRNA. Translation: AAH13001.1.
CCDSiCCDS2546.1. [Q15435-1]
CCDS63190.1. [Q15435-5]
CCDS63192.1. [Q15435-3]
CCDS63193.1. [Q15435-4]
CCDS63194.1. [Q15435-2]
PIRiS68209.
RefSeqiNP_001269338.1. NM_001282409.1. [Q15435-2]
NP_001269339.1. NM_001282410.1. [Q15435-3]
NP_001269340.1. NM_001282411.1. [Q15435-4]
NP_001269341.1. NM_001282412.1.
NP_001269342.1. NM_001282413.1.
NP_001269343.1. NM_001282414.1. [Q15435-5]
NP_002703.1. NM_002712.2. [Q15435-1]
UniGeneiHs.36587.

3D structure databases

ProteinModelPortaliQ15435.
SMRiQ15435. Positions 77-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111502. 23 interactions.
DIPiDIP-1005N.
IntActiQ15435. 12 interactions.
MINTiMINT-5004667.
STRINGi9606.ENSP00000234038.

PTM databases

PhosphoSiteiQ15435.

Polymorphism databases

DMDMi74762145.

2D gel databases

REPRODUCTION-2DPAGEIPI00033600.

Proteomic databases

MaxQBiQ15435.
PaxDbiQ15435.
PRIDEiQ15435.

Protocols and materials databases

DNASUi5510.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234038; ENSP00000234038; ENSG00000115685. [Q15435-1]
ENST00000272983; ENSP00000272983; ENSG00000115685. [Q15435-2]
ENST00000401987; ENSP00000385466; ENSG00000115685. [Q15435-4]
ENST00000402734; ENSP00000385012; ENSG00000115685. [Q15435-5]
ENST00000406106; ENSP00000385022; ENSG00000115685. [Q15435-3]
ENST00000407025; ENSP00000385657; ENSG00000115685. [Q15435-1]
GeneIDi5510.
KEGGihsa:5510.
UCSCiuc002was.3. human. [Q15435-3]
uc002wat.1. human. [Q15435-1]
uc002wau.1. human. [Q15435-2]

Organism-specific databases

CTDi5510.
GeneCardsiGC02P242088.
HGNCiHGNC:9295. PPP1R7.
HPAiHPA034500.
HPA034501.
MIMi602877. gene.
neXtProtiNX_Q15435.
PharmGKBiPA33658.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00730000110223.
HOGENOMiHOG000211189.
HOVERGENiHBG082161.
InParanoidiQ15435.
KOiK17550.
OMAiQRICLRQ.
PhylomeDBiQ15435.
TreeFamiTF105538.

Miscellaneous databases

ChiTaRSiPPP1R7. human.
GeneWikiiPPP1R7.
GenomeRNAii5510.
NextBioi21312.
PROiQ15435.
SOURCEiSearch...

Gene expression databases

BgeeiQ15435.
CleanExiHS_PPP1R7.
ExpressionAtlasiQ15435. baseline and differential.
GenevestigatoriQ15435.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
PfamiPF12799. LRR_4. 2 hits.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 12 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "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.
  9. "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.
  10. "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].
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-44 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPP1R7_HUMAN
AccessioniPrimary (citable) accession number: Q15435
Secondary accession number(s): B4DFD4
, B5MCY6, Q9UQE5, Q9UQE6, Q9Y6K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.