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Q15435

- PP1R7_HUMAN

UniProt

Q15435 - PP1R7_HUMAN

Protein

Protein phosphatase 1 regulatory subunit 7

Gene

PPP1R7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. positive regulation of protein dephosphorylation Source: MGI
    2. regulation of catalytic activity Source: GOC

    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: UniProt
    4. nucleus Source: UniProt

    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 – 271Phosphoserine3 Publications
    Modified residuei44 – 441Phosphoserine1 Publication
    Modified residuei47 – 471Phosphoserine1 Publication

    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

    ArrayExpressiQ15435.
    BgeeiQ15435.
    CleanExiHS_PPP1R7.
    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. 17 interactions.
    DIPiDIP-1005N.
    IntActiQ15435. 12 interactions.
    MINTiMINT-5004667.
    STRINGi9606.ENSP00000234038.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15435.
    SMRiQ15435. Positions 57-359.
    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.
    HOGENOMiHOG000211189.
    HOVERGENiHBG082161.
    InParanoidiQ15435.
    KOiK17550.
    OMAiANRIKKI.
    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. Align

    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

    MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD    50
    GEERGEEDPE EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV 100
    KTLCLRQNLI KCIENLEELQ SLRELDLYDN QIKKIENLEA LTELEILDIS 150
    FNLLRNIEGV DKLTRLKKLF LVNNKISKIE NLSNLHQLQM LELGSNRIRA 200
    IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN RLTKIEGLQN 250
    LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE 300
    FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV 350
    RQIDATFVRF 360
    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:
    EMBL
    GenBank
    DDBJ
    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]
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2546.1. [Q15435-1 ]
    CCDS63192.1. [Q15435-3 ]
    CCDS63193.1. [Q15435-4 ]
    CCDS63194.1. [Q15435-2 ]
    PIRi S68209.
    RefSeqi NP_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.
    NP_002703.1. NM_002712.2. [Q15435-1 ]
    UniGenei Hs.36587.

    3D structure databases

    ProteinModelPortali Q15435.
    SMRi Q15435. Positions 57-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111502. 17 interactions.
    DIPi DIP-1005N.
    IntActi Q15435. 12 interactions.
    MINTi MINT-5004667.
    STRINGi 9606.ENSP00000234038.

    PTM databases

    PhosphoSitei Q15435.

    Polymorphism databases

    DMDMi 74762145.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00033600.

    Proteomic databases

    MaxQBi Q15435.
    PaxDbi Q15435.
    PRIDEi Q15435.

    Protocols and materials databases

    DNASUi 5510.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234038 ; 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 ]
    GeneIDi 5510.
    KEGGi hsa:5510.
    UCSCi uc002was.3. human. [Q15435-3 ]
    uc002wat.1. human. [Q15435-1 ]
    uc002wau.1. human. [Q15435-2 ]

    Organism-specific databases

    CTDi 5510.
    GeneCardsi GC02P242088.
    HGNCi HGNC:9295. PPP1R7.
    HPAi HPA034500.
    HPA034501.
    MIMi 602877. gene.
    neXtProti NX_Q15435.
    PharmGKBi PA33658.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000211189.
    HOVERGENi HBG082161.
    InParanoidi Q15435.
    KOi K17550.
    OMAi ANRIKKI.
    PhylomeDBi Q15435.
    TreeFami TF105538.

    Miscellaneous databases

    ChiTaRSi PPP1R7. human.
    GeneWikii PPP1R7.
    GenomeRNAii 5510.
    NextBioi 21312.
    PROi Q15435.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15435.
    Bgeei Q15435.
    CleanExi HS_PPP1R7.
    Genevestigatori Q15435.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view ]
    Pfami PF12799. LRR_4. 2 hits.
    [Graphical view ]
    SMARTi SM00446. LRRcap. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 12 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 132 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