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O35412

- SI1L1_RAT

UniProt

O35412 - SI1L1_RAT

Protein

Signal-induced proliferation-associated 1-like protein 1

Gene

Sipa1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. GTPase activator activity Source: RGD
    3. protein binding Source: UniProtKB
    4. protein complex binding Source: RGD
    5. protein kinase binding Source: UniProtKB
    6. ubiquitin protein ligase binding Source: RGD

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. activation of Rap GTPase activity Source: UniProtKB
    3. ephrin receptor signaling pathway Source: UniProtKB
    4. regulation of axonogenesis Source: UniProtKB
    5. regulation of dendrite morphogenesis Source: RGD
    6. regulation of dendritic spine morphogenesis Source: UniProtKB
    7. regulation of Rap GTPase activity Source: UniProtKB
    8. regulation of synaptic plasticity Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal-induced proliferation-associated 1-like protein 1
    Short name:
    SIPA1-like protein 1
    Alternative name(s):
    SPA-1-like protein p1294
    Spine-associated Rap GTPase-activating protein
    Short name:
    SPAR
    Gene namesi
    Name:Sipa1l1
    Synonyms:Spa1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi708497. Sipa1l1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapsesynaptosome
    Note: Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB-KW
    3. dendritic spine Source: UniProtKB
    4. neuronal cell body Source: RGD
    5. postsynaptic density Source: UniProtKB
    6. postsynaptic membrane Source: UniProtKB-KW
    7. protein complex Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi743 – 7431R → A: Decreases stimulation of the GTPase activity of RAP2A. 1 Publication
    Mutagenesisi846 – 8472RT → AS: Abolishes stimulation of the GTPase activity of RAP2A.
    Mutagenesisi1344 – 13441S → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1348. 1 Publication
    Mutagenesisi1348 – 13481T → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1344. 1 Publication
    Mutagenesisi1367 – 13671S → A: Abolishes phosphorylation by CDK5 and subsequent phosphorylation by PLK2, leading to prevent ubiquitination and degradation by the proteasome. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18221822Signal-induced proliferation-associated 1-like protein 1PRO_0000056748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei162 – 1621PhosphoserineBy similarity
    Modified residuei288 – 2881PhosphoserineBy similarity
    Modified residuei1220 – 12201PhosphoserineBy similarity
    Modified residuei1273 – 12731PhosphoserineBy similarity
    Modified residuei1288 – 12881PhosphoserineBy similarity
    Modified residuei1344 – 13441Phosphoserine; by PLK21 Publication
    Modified residuei1348 – 13481Phosphothreonine; by PLK21 Publication
    Modified residuei1367 – 13671Phosphoserine; by CDK51 Publication
    Modified residuei1449 – 14491PhosphoserineBy similarity
    Modified residuei1451 – 14511PhosphoserineBy similarity
    Modified residuei1567 – 15671PhosphoserineBy similarity
    Modified residuei1569 – 15691PhosphothreonineBy similarity
    Modified residuei1572 – 15721PhosphoserineBy similarity
    Modified residuei1583 – 15831PhosphoserineBy similarity
    Modified residuei1586 – 15861PhosphoserineBy similarity
    Modified residuei1603 – 16031PhosphoserineBy similarity
    Modified residuei1752 – 17521PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.
    Phosphorylated at Ser-1367 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO35412.
    PRIDEiO35412.

    PTM databases

    PhosphoSiteiO35412.

    Expressioni

    Tissue specificityi

    Detected in brain (at protein level).2 Publications

    Gene expression databases

    GenevestigatoriO35412.

    Interactioni

    Subunit structurei

    Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases By similarity. Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi251530. 6 interactions.
    STRINGi10116.ENSRNOP00000010626.

    Structurei

    3D structure databases

    ProteinModelPortaliO35412.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini638 – 855218Rap-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini992 – 106877PDZPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1753 – 181361Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi93 – 12937Ser-richAdd
    BLAST
    Compositional biasi1153 – 1486334Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG279955.
    HOGENOMiHOG000154319.
    HOVERGENiHBG056135.
    InParanoidiO35412.
    KOiK17701.
    PhylomeDBiO35412.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR021818. DUF3401.
    IPR001478. PDZ.
    IPR000331. Rap_GAP_dom.
    [Graphical view]
    PfamiPF11881. DUF3401. 1 hit.
    PF00595. PDZ. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50106. PDZ. 1 hit.
    PS50085. RAPGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O35412-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSLKRSQTE RPVTADRASV VSTDGTPKVH TDDFYMRRFR SQNGSLGSSV     50
    MAAVGPPRSE GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI 100
    ETSSCLESLS SKGSPVSQGS SVSLNSNDSA MLKSIQNTLK NKTGPAESMD 150
    SRFLMPEAYP SSPRKALRRI RQRSNSDITI SELDVDSFDE CISPTYKSGP 200
    SLHREYGSTS SIDKQGTSGE SFFGLLKGYK DDRADRGPTP TKLSDFLITG 250
    GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR 300
    NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR 350
    HNVIKRRNTT TGASAAAVAS LVSGPLSHST SFSSPMGSTE DFNSKGSLGM 400
    DQGDDKSNEL VMSCPYFRNE IGGEGERKIS LSKSNSGSFS GCESTSFESA 450
    LSSHCTNAGV AVLEVPKESL MLHLDRVRRY TVEHVDLGAY YYRKCFYQKE 500
    HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR TSELMTLRGS 550
    VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM 600
    KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN TPKVTEQFMK LDEQGLNYQQ 650
    KVGIMYCKAG QSTEEEMYNN ESAGPAFEEF LQLLGERVRL KGFEKYRAQL 700
    DTKTDSTGTH SLYTTYKDYE IMFHVSTMLP YTPNNKQQLL RKRHIGNDIV 750
    TIVFQEPGAQ PFSPKNIRSH FQHVFVIVRA HNPCTESVCY SVAVTRSRDV 800
    PSFGPPIPKG VTFPKSNVFR DFLLAKVINA ENAAHKSEKF RAMATRTRQE 850
    YLKDLAEKNV TNTPIDPSGK FPFISLASKK KEKSKPYPGA ELSSMGAIVW 900
    AVRAKDYNKA MEFDCLLGIS NEFIVLIEQE TKSVVFNCSC RDVIGWTSSD 950
    SSLKIFYERG ECISVESFMS SEDIKEIVKR LQFVSKGCES VEMTLRRNGL 1000
    GQLGFHVNYE GIVADVEPYG YAWQAGLKQG SRLVEICKVA VATLSHEQMI 1050
    DLLRTSVTVK VVIIPPHDDC TPRRSCSETY RMPVMEYKMN EGVSYEYKFP 1100
    FRSNNKWQRN AGKGAHSPQV PLQLQSPMIS RVNAGKGDGK MPLPERAANI 1150
    PRSISSDGRP LERRLSPGSD IYVTVSSMAL ARSQCRNSPS NLSSSSETGS 1200
    GGGTYRQKSM PEGFGVSRRS PASIDRQNTQ SDIGGSGKST PSWQRSEDSL 1250
    ADQMEPTCHL PAVSKVLPAF RESPSGRLMR QDPVVHLSPN KQGHSDSHYS 1300
    SHSSSNTLSS NASSAHSDEK WYDGDRTESD LNSYNYLQGT SADSGIDTAS 1350
    YGLSHGSTAS LGASTSSPRS GPGKEKVAPL WHSSSEVLSL ADRTLETEGH 1400
    GMDRKTESSL SLDIHSKSQG GSSPLTRENS TFSINDATSH TSTMSSRHSA 1450
    SPVVFSSARS SPKEELHPTT SSQLAPSFSS SSSSSSGPRT FYPRQGATSK 1500
    YLIGWKKPEG TINSVGFMDT RKRHQSDGNE IAHTRLRAST RDLRASPKPT 1550
    SKSTIEEDLK KLIDLESPTP ESQKNFKFHG LSSPQSPFPS TPTSRRALHR 1600
    TLSDESIYSS QREHFFTSRA SLLDQALPND VFFSSTYPSL PKSLPLRRPS 1650
    YTLGMKSLHG EFFASDSSLT DIQETRRQPI PDPGLMPLPD TASDLDWSNL 1700
    VDAAKAYEVQ RASFFAASDE NHRPLSAASN SDQLEEQALV QMKSYSSSKD 1750
    SSPTLASKVD QLEGMLKMLR EDLKKEKEDK AHLQAEVEHL REDNLRLQEE 1800
    SQNASDKLKK FTEWVFNTID MS 1822
    Length:1,822
    Mass (Da):201,925
    Last modified:January 1, 1998 - v1
    Checksum:i479821CE8820B4FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026504 mRNA. Translation: AAB81526.1.
    PIRiT14106.
    RefSeqiNP_647546.1. NM_139330.1.
    UniGeneiRn.10835.

    Genome annotation databases

    GeneIDi246212.
    KEGGirno:246212.
    UCSCiRGD:708497. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF026504 mRNA. Translation: AAB81526.1 .
    PIRi T14106.
    RefSeqi NP_647546.1. NM_139330.1.
    UniGenei Rn.10835.

    3D structure databases

    ProteinModelPortali O35412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 251530. 6 interactions.
    STRINGi 10116.ENSRNOP00000010626.

    PTM databases

    PhosphoSitei O35412.

    Proteomic databases

    PaxDbi O35412.
    PRIDEi O35412.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 246212.
    KEGGi rno:246212.
    UCSCi RGD:708497. rat.

    Organism-specific databases

    CTDi 26037.
    RGDi 708497. Sipa1l1.

    Phylogenomic databases

    eggNOGi NOG279955.
    HOGENOMi HOG000154319.
    HOVERGENi HBG056135.
    InParanoidi O35412.
    KOi K17701.
    PhylomeDBi O35412.

    Miscellaneous databases

    NextBioi 623491.

    Gene expression databases

    Genevestigatori O35412.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR021818. DUF3401.
    IPR001478. PDZ.
    IPR000331. Rap_GAP_dom.
    [Graphical view ]
    Pfami PF11881. DUF3401. 1 hit.
    PF00595. PDZ. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    PS50085. RAPGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Takeuchi M., Ide N., Hata Y., Takai Y.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP."
      Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M.
      Neuron 31:289-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DLG4, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-743 AND 846-ARG-THR-847, TISSUE SPECIFICITY.
    3. "ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the scaffolding protein ProSAP2/Shank3."
      Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H., Proepper C., Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.
      J. Biol. Chem. 281:13805-13816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LZTS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "The EphA4 receptor regulates neuronal morphology through SPAR-mediated inactivation of Rap GTPases."
      Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.
      J. Neurosci. 27:14205-14215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    5. "Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the SCFbeta-TRCP ubiquitin ligase in hippocampal neurons."
      Ang X.L., Seeburg D.P., Sheng M., Harper J.W.
      J. Biol. Chem. 283:29424-29432(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1344 AND THR-1348, UBIQUITINATION, MUTAGENESIS OF SER-1344 AND THR-1348.
    6. "Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity."
      Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M.
      Neuron 58:571-583(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1367, UBIQUITINATION, MUTAGENESIS OF SER-1367.
    7. "Postsynaptic PDLIM5/Enigma homolog binds SPAR and causes dendritic spine shrinkage."
      Herrick S., Evers D.M., Lee J.Y., Udagawa N., Pak D.T.
      Mol. Cell. Neurosci. 43:188-200(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDLIM5 AND PDLIM7.
    8. "Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory."
      Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.
      Neuron 69:957-973(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, UBIQUITINATION.

    Entry informationi

    Entry nameiSI1L1_RAT
    AccessioniPrimary (citable) accession number: O35412
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3