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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

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 complex binding Source: RGD
  4. protein kinase binding Source: UniProtKB
  5. 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.

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. 1 Publication
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

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        10         20         30         40         50
MTSLKRSQTE RPVTADRASV VSTDGTPKVH TDDFYMRRFR SQNGSLGSSV
60 70 80 90 100
MAAVGPPRSE GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI
110 120 130 140 150
ETSSCLESLS SKGSPVSQGS SVSLNSNDSA MLKSIQNTLK NKTGPAESMD
160 170 180 190 200
SRFLMPEAYP SSPRKALRRI RQRSNSDITI SELDVDSFDE CISPTYKSGP
210 220 230 240 250
SLHREYGSTS SIDKQGTSGE SFFGLLKGYK DDRADRGPTP TKLSDFLITG
260 270 280 290 300
GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR
310 320 330 340 350
NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR
360 370 380 390 400
HNVIKRRNTT TGASAAAVAS LVSGPLSHST SFSSPMGSTE DFNSKGSLGM
410 420 430 440 450
DQGDDKSNEL VMSCPYFRNE IGGEGERKIS LSKSNSGSFS GCESTSFESA
460 470 480 490 500
LSSHCTNAGV AVLEVPKESL MLHLDRVRRY TVEHVDLGAY YYRKCFYQKE
510 520 530 540 550
HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR TSELMTLRGS
560 570 580 590 600
VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM
610 620 630 640 650
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN TPKVTEQFMK LDEQGLNYQQ
660 670 680 690 700
KVGIMYCKAG QSTEEEMYNN ESAGPAFEEF LQLLGERVRL KGFEKYRAQL
710 720 730 740 750
DTKTDSTGTH SLYTTYKDYE IMFHVSTMLP YTPNNKQQLL RKRHIGNDIV
760 770 780 790 800
TIVFQEPGAQ PFSPKNIRSH FQHVFVIVRA HNPCTESVCY SVAVTRSRDV
810 820 830 840 850
PSFGPPIPKG VTFPKSNVFR DFLLAKVINA ENAAHKSEKF RAMATRTRQE
860 870 880 890 900
YLKDLAEKNV TNTPIDPSGK FPFISLASKK KEKSKPYPGA ELSSMGAIVW
910 920 930 940 950
AVRAKDYNKA MEFDCLLGIS NEFIVLIEQE TKSVVFNCSC RDVIGWTSSD
960 970 980 990 1000
SSLKIFYERG ECISVESFMS SEDIKEIVKR LQFVSKGCES VEMTLRRNGL
1010 1020 1030 1040 1050
GQLGFHVNYE GIVADVEPYG YAWQAGLKQG SRLVEICKVA VATLSHEQMI
1060 1070 1080 1090 1100
DLLRTSVTVK VVIIPPHDDC TPRRSCSETY RMPVMEYKMN EGVSYEYKFP
1110 1120 1130 1140 1150
FRSNNKWQRN AGKGAHSPQV PLQLQSPMIS RVNAGKGDGK MPLPERAANI
1160 1170 1180 1190 1200
PRSISSDGRP LERRLSPGSD IYVTVSSMAL ARSQCRNSPS NLSSSSETGS
1210 1220 1230 1240 1250
GGGTYRQKSM PEGFGVSRRS PASIDRQNTQ SDIGGSGKST PSWQRSEDSL
1260 1270 1280 1290 1300
ADQMEPTCHL PAVSKVLPAF RESPSGRLMR QDPVVHLSPN KQGHSDSHYS
1310 1320 1330 1340 1350
SHSSSNTLSS NASSAHSDEK WYDGDRTESD LNSYNYLQGT SADSGIDTAS
1360 1370 1380 1390 1400
YGLSHGSTAS LGASTSSPRS GPGKEKVAPL WHSSSEVLSL ADRTLETEGH
1410 1420 1430 1440 1450
GMDRKTESSL SLDIHSKSQG GSSPLTRENS TFSINDATSH TSTMSSRHSA
1460 1470 1480 1490 1500
SPVVFSSARS SPKEELHPTT SSQLAPSFSS SSSSSSGPRT FYPRQGATSK
1510 1520 1530 1540 1550
YLIGWKKPEG TINSVGFMDT RKRHQSDGNE IAHTRLRAST RDLRASPKPT
1560 1570 1580 1590 1600
SKSTIEEDLK KLIDLESPTP ESQKNFKFHG LSSPQSPFPS TPTSRRALHR
1610 1620 1630 1640 1650
TLSDESIYSS QREHFFTSRA SLLDQALPND VFFSSTYPSL PKSLPLRRPS
1660 1670 1680 1690 1700
YTLGMKSLHG EFFASDSSLT DIQETRRQPI PDPGLMPLPD TASDLDWSNL
1710 1720 1730 1740 1750
VDAAKAYEVQ RASFFAASDE NHRPLSAASN SDQLEEQALV QMKSYSSSKD
1760 1770 1780 1790 1800
SSPTLASKVD QLEGMLKMLR EDLKKEKEDK AHLQAEVEHL REDNLRLQEE
1810 1820
SQNASDKLKK FTEWVFNTID MS
Length:1,822
Mass (Da):201,925
Last modified:January 1, 1998 - v1
Checksum:i479821CE8820B4FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 99 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