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Q5VSL9

- STRP1_HUMAN

UniProt

Q5VSL9 - STRP1_HUMAN

Protein

Striatin-interacting protein 1

Gene

STRIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cortical actin cytoskeleton organization Source: UniProtKB
    2. regulation of cell morphogenesis Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Striatin-interacting protein 1
    Alternative name(s):
    Protein FAM40A
    Gene namesi
    Name:STRIP1
    Synonyms:FAM40A, KIAA1761
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25916. STRIP1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Enriched on the plasma membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134939426.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 837837Striatin-interacting protein 1PRO_0000187017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei335 – 3351Phosphoserine8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5VSL9.
    PaxDbiQ5VSL9.
    PRIDEiQ5VSL9.

    PTM databases

    PhosphoSiteiQ5VSL9.

    Expressioni

    Gene expression databases

    BgeeiQ5VSL9.
    CleanExiHS_FAM40A.
    GenevestigatoriQ5VSL9.

    Organism-specific databases

    HPAiHPA060302.

    Interactioni

    Subunit structurei

    Component of striatin-interacting phosphatase and kinase (STRIPAK) complex By similarity. Interacts with CTTNBP2NL.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTTNBP2NLQ9P2B44EBI-1773588,EBI-1774273
    MST4Q9P2892EBI-1773588,EBI-618239
    TRAF3IP3Q9Y2282EBI-1773588,EBI-765817

    Protein-protein interaction databases

    BioGridi124497. 36 interactions.
    IntActiQ5VSL9. 27 interactions.
    STRINGi9606.ENSP00000358810.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VSL9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 3634Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the STRIP family.Curated

    Phylogenomic databases

    eggNOGiNOG247682.
    HOVERGENiHBG081506.
    InParanoidiQ5VSL9.
    OMAiLIMNNKQ.
    OrthoDBiEOG7W1536.
    PhylomeDBiQ5VSL9.
    TreeFamiTF314205.

    Family and domain databases

    InterProiIPR021819. DUF3402.
    IPR012486. N1221.
    [Graphical view]
    PfamiPF11882. DUF3402. 1 hit.
    PF07923. N1221. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5VSL9-1) [UniParc]FASTAAdd to Basket

    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

    MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE    50
    FNRNQRKDSE GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC 100
    FEEDFRIHVT DKKWTELDTN QHRTHAMRLL DGLEVTAREK RLKVARAILY 150
    VAQGTFGECS SEAEVQSWMR YNIFLLLEVG TFNALVELLN MEIDNSAACS 200
    SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE WRTMRQTFRA 250
    ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG 300
    FEELQSMKAE KRSILGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR 350
    GRREHKALIK QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER 400
    DEVMPPPLQH PQTDRLTCPK GLPWAPKVRE KDIEMFLESS RSKFIGYTLG 450
    SDTNTVVGLP RPIHESIKTL KQHKYTSIAE VQAQMEEEYL RSPLSGGEEE 500
    VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD SINILADVLP 550
    EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM 600
    AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE 650
    SLEAGDSNQF CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR 700
    ALKVKQAMMQ LYVLKLLKVQ TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD 750
    WAYGNDLDAR PWDFQAEECA LRANIERFNA RRYDRAHSNP DFLPVDNCLQ 800
    SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ 837
    Length:837
    Mass (Da):95,576
    Last modified:December 7, 2004 - v1
    Checksum:i5F9BA1D4C7DE6925
    GO
    Isoform 2 (identifier: Q5VSL9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:742
    Mass (Da):85,451
    Checksum:iA4C208A05F910919
    GO
    Isoform 3 (identifier: Q5VSL9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-264: Missing.
         596-596: Q → QVPTGLSLLS...FFFFFSCWLQ
         630-630: S → R
         631-837: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:440
    Mass (Da):49,699
    Checksum:iB1ADA0F87A30303E
    GO
    Isoform 4 (identifier: Q5VSL9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         194-212: DNSAACSSAVRKPAISLAD → EHCCVRPAVSALAGGQAQD
         213-837: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:212
    Mass (Da):23,540
    Checksum:i636A065B51CB3595
    GO

    Sequence cautioni

    The sequence AAH32644.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti397 – 3971P → L in BAC86034. (PubMed:14702039)Curated
    Sequence conflicti744 – 7441R → Q in BAB55265. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 264264Missing in isoform 3. 1 PublicationVSP_014856Add
    BLAST
    Alternative sequencei1 – 9595Missing in isoform 2. 1 PublicationVSP_014857Add
    BLAST
    Alternative sequencei194 – 21219DNSAA…ISLAD → EHCCVRPAVSALAGGQAQD in isoform 4. 1 PublicationVSP_014858Add
    BLAST
    Alternative sequencei213 – 837625Missing in isoform 4. 1 PublicationVSP_014859Add
    BLAST
    Alternative sequencei596 – 5961Q → QVPTGLSLLSCGLGPRALLL LQPTRTGALAFDPLELCMNV LRHGPSAKAFHPWRKEGKVP RAAPFFFFFFSCWLQ in isoform 3. 1 PublicationVSP_014860
    Alternative sequencei630 – 6301S → R in isoform 3. 1 PublicationVSP_014861
    Alternative sequencei631 – 837207Missing in isoform 3. 1 PublicationVSP_014862Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051548 mRNA. Translation: BAB21852.2.
    AK027649 mRNA. Translation: BAB55265.1.
    AK125054 mRNA. Translation: BAC86034.1.
    AL834196 mRNA. Translation: CAH56368.1.
    AL772411, AL160006 Genomic DNA. Translation: CAH70967.1.
    AL772411, AL160006 Genomic DNA. Translation: CAH70968.1.
    AL160006, AL772411 Genomic DNA. Translation: CAI22715.1.
    AL160006, AL772411 Genomic DNA. Translation: CAI22716.1.
    BC032644 mRNA. Translation: AAH32644.1. Different initiation.
    BC094786 mRNA. Translation: AAH94786.1.
    BC119814 mRNA. Translation: AAI19815.1.
    BC121793 mRNA. Translation: AAI21794.1.
    CCDSiCCDS30798.1. [Q5VSL9-1]
    CCDS59197.1. [Q5VSL9-2]
    RefSeqiNP_001257697.1. NM_001270768.1. [Q5VSL9-2]
    NP_149079.2. NM_033088.3. [Q5VSL9-1]
    UniGeneiHs.584996.

    Genome annotation databases

    EnsembliENST00000369795; ENSP00000358810; ENSG00000143093. [Q5VSL9-1]
    ENST00000369796; ENSP00000358811; ENSG00000143093. [Q5VSL9-2]
    ENST00000485775; ENSP00000476025; ENSG00000143093. [Q5VSL9-4]
    GeneIDi85369.
    KEGGihsa:85369.
    UCSCiuc001dyz.1. human. [Q5VSL9-1]

    Polymorphism databases

    DMDMi71648671.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051548 mRNA. Translation: BAB21852.2 .
    AK027649 mRNA. Translation: BAB55265.1 .
    AK125054 mRNA. Translation: BAC86034.1 .
    AL834196 mRNA. Translation: CAH56368.1 .
    AL772411 , AL160006 Genomic DNA. Translation: CAH70967.1 .
    AL772411 , AL160006 Genomic DNA. Translation: CAH70968.1 .
    AL160006 , AL772411 Genomic DNA. Translation: CAI22715.1 .
    AL160006 , AL772411 Genomic DNA. Translation: CAI22716.1 .
    BC032644 mRNA. Translation: AAH32644.1 . Different initiation.
    BC094786 mRNA. Translation: AAH94786.1 .
    BC119814 mRNA. Translation: AAI19815.1 .
    BC121793 mRNA. Translation: AAI21794.1 .
    CCDSi CCDS30798.1. [Q5VSL9-1 ]
    CCDS59197.1. [Q5VSL9-2 ]
    RefSeqi NP_001257697.1. NM_001270768.1. [Q5VSL9-2 ]
    NP_149079.2. NM_033088.3. [Q5VSL9-1 ]
    UniGenei Hs.584996.

    3D structure databases

    ProteinModelPortali Q5VSL9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124497. 36 interactions.
    IntActi Q5VSL9. 27 interactions.
    STRINGi 9606.ENSP00000358810.

    PTM databases

    PhosphoSitei Q5VSL9.

    Polymorphism databases

    DMDMi 71648671.

    Proteomic databases

    MaxQBi Q5VSL9.
    PaxDbi Q5VSL9.
    PRIDEi Q5VSL9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369795 ; ENSP00000358810 ; ENSG00000143093 . [Q5VSL9-1 ]
    ENST00000369796 ; ENSP00000358811 ; ENSG00000143093 . [Q5VSL9-2 ]
    ENST00000485775 ; ENSP00000476025 ; ENSG00000143093 . [Q5VSL9-4 ]
    GeneIDi 85369.
    KEGGi hsa:85369.
    UCSCi uc001dyz.1. human. [Q5VSL9-1 ]

    Organism-specific databases

    CTDi 85369.
    GeneCardsi GC01P110577.
    H-InvDB HIX0199796.
    HGNCi HGNC:25916. STRIP1.
    HPAi HPA060302.
    neXtProti NX_Q5VSL9.
    PharmGKBi PA134939426.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247682.
    HOVERGENi HBG081506.
    InParanoidi Q5VSL9.
    OMAi LIMNNKQ.
    OrthoDBi EOG7W1536.
    PhylomeDBi Q5VSL9.
    TreeFami TF314205.

    Miscellaneous databases

    GeneWikii FAM40A.
    GenomeRNAii 85369.
    NextBioi 75905.
    PROi Q5VSL9.

    Gene expression databases

    Bgeei Q5VSL9.
    CleanExi HS_FAM40A.
    Genevestigatori Q5VSL9.

    Family and domain databases

    InterProi IPR021819. DUF3402.
    IPR012486. N1221.
    [Graphical view ]
    Pfami PF11882. DUF3402. 1 hit.
    PF07923. N1221. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Ohara O., Nagase T., Kikuno R.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Thalamus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Amygdala.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Placenta and Uterus.
    7. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    9. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
      Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
      Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTTNBP2NL.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
      Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
      BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. 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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTRP1_HUMAN
    AccessioniPrimary (citable) accession number: Q5VSL9
    Secondary accession number(s): Q0V925
    , Q5VSL8, Q658K2, Q6ZV31, Q8N598, Q96SN2, Q9C0A2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2005
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 90 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3