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O35412

- SI1L1_RAT

UniProt

O35412 - SI1L1_RAT

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Protein

Signal-induced proliferation-associated 1-like protein 1

Gene
Sipa1l1, Spa1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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 – 1621Phosphoserine By similarity
Modified residuei288 – 2881Phosphoserine By similarity
Modified residuei1220 – 12201Phosphoserine By similarity
Modified residuei1273 – 12731Phosphoserine By similarity
Modified residuei1288 – 12881Phosphoserine By similarity
Modified residuei1344 – 13441Phosphoserine; by PLK21 Publication
Modified residuei1348 – 13481Phosphothreonine; by PLK21 Publication
Modified residuei1367 – 13671Phosphoserine; by CDK51 Publication
Modified residuei1449 – 14491Phosphoserine By similarity
Modified residuei1451 – 14511Phosphoserine By similarity
Modified residuei1567 – 15671Phosphoserine By similarity
Modified residuei1569 – 15691Phosphothreonine By similarity
Modified residuei1572 – 15721Phosphoserine By similarity
Modified residuei1583 – 15831Phosphoserine By similarity
Modified residuei1586 – 15861Phosphoserine By similarity
Modified residuei1603 – 16031Phosphoserine By similarity
Modified residuei1752 – 17521Phosphoserine By similarity

Post-translational modificationi

Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.3 Publications
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.4 Publications

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.3 Publications

Protein-protein interaction databases

BioGridi251530. 6 interactions.
STRINGi10116.ENSRNOP00000010626.

Structurei

3D structure databases

ProteinModelPortaliO35412.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini638 – 855218Rap-GAPAdd
BLAST
Domaini992 – 106877PDZAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1753 – 181361 Reviewed predictionAdd
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.
Contains 1 Rap-GAP domain.

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

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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: June 11, 2014
This is version 97 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

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