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Protein

Signal-induced proliferation-associated 1-like protein 1

Gene

Sipa1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • actin filament binding Source: UniProtKB
  • GTPase activator activity Source: RGD
  • protein complex binding Source: RGD
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of GTPase activity Source: UniProtKB
  • ephrin receptor signaling pathway Source: UniProtKB
  • regulation of axonogenesis Source: UniProtKB
  • regulation of dendrite morphogenesis Source: RGD
  • regulation of dendritic spine morphogenesis Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: InterPro
  • regulation of synaptic plasticity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708497. Sipa1l1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • dendritic spine Source: UniProtKB
  • neuronal cell body Source: RGD
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-KW
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi743R → A: Decreases stimulation of the GTPase activity of RAP2A. 1 Publication1
Mutagenesisi846 – 847RT → AS: Abolishes stimulation of the GTPase activity of RAP2A. 1 Publication2
Mutagenesisi1344S → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1348. 1 Publication1
Mutagenesisi1348T → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1344. 1 Publication1
Mutagenesisi1367S → A: Abolishes phosphorylation by CDK5 and subsequent phosphorylation by PLK2, leading to prevent ubiquitination and degradation by the proteasome. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000567481 – 1822Signal-induced proliferation-associated 1-like protein 1Add BLAST1822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei162PhosphoserineBy similarity1
Modified residuei187PhosphoserineBy similarity1
Modified residuei193PhosphoserineBy similarity1
Modified residuei208PhosphoserineBy similarity1
Modified residuei255PhosphoserineBy similarity1
Modified residuei288PhosphoserineBy similarity1
Modified residuei1117PhosphoserineBy similarity1
Modified residuei1126PhosphoserineBy similarity1
Modified residuei1155PhosphoserineBy similarity1
Modified residuei1166PhosphoserineBy similarity1
Modified residuei1188PhosphoserineBy similarity1
Modified residuei1209PhosphoserineBy similarity1
Modified residuei1220PhosphoserineBy similarity1
Modified residuei1273PhosphoserineBy similarity1
Modified residuei1288PhosphoserineCombined sources1
Modified residuei1344Phosphoserine; by PLK21 Publication1
Modified residuei1348Phosphothreonine; by PLK21 Publication1
Modified residuei1367Phosphoserine; by CDK51 Publication1
Modified residuei1384PhosphoserineBy similarity1
Modified residuei1408PhosphoserineBy similarity1
Modified residuei1409PhosphoserineBy similarity1
Modified residuei1430PhosphoserineBy similarity1
Modified residuei1449PhosphoserineCombined sources1
Modified residuei1451PhosphoserineCombined sources1
Modified residuei1546PhosphoserineBy similarity1
Modified residuei1567PhosphoserineCombined sources1
Modified residuei1569PhosphothreonineBy similarity1
Modified residuei1572PhosphoserineBy similarity1
Modified residuei1583PhosphoserineBy similarity1
Modified residuei1586PhosphoserineBy similarity1
Modified residuei1603PhosphoserineCombined sources1
Modified residuei1606PhosphoserineBy similarity1
Modified residuei1619Asymmetric dimethylarginineBy similarity1
Modified residuei1621PhosphoserineBy similarity1
Modified residuei1665PhosphoserineBy similarity1
Modified residuei1668PhosphoserineBy similarity1
Modified residuei1726PhosphoserineBy similarity1
Modified residuei1729PhosphoserineBy similarity1
Modified residuei1746PhosphoserineBy similarity1
Modified residuei1747PhosphoserineBy similarity1
Modified residuei1752PhosphoserineCombined sources1

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

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO35412.
PRIDEiO35412.

PTM databases

iPTMnetiO35412.
PhosphoSitePlusiO35412.

Expressioni

Tissue specificityi

Detected in brain (at protein level).2 Publications

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

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: RGD

Protein-protein interaction databases

BioGridi251530. 7 interactors.
STRINGi10116.ENSRNOP00000054996.

Structurei

3D structure databases

ProteinModelPortaliO35412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini638 – 855Rap-GAPPROSITE-ProRule annotationAdd BLAST218
Domaini992 – 1068PDZPROSITE-ProRule annotationAdd BLAST77

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1753 – 1813Sequence analysisAdd BLAST61

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi93 – 129Ser-richAdd BLAST37
Compositional biasi1153 – 1486Ser-richAdd BLAST334

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO35412.
KOiK17701.
PhylomeDBiO35412.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR021818. SIPA1L_C.
[Graphical view]
PfamiPF02145. Rap_GAP. 1 hit.
PF11881. SPAR_C. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 2 hits.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35412-1 [UniParc]FASTAAdd to basket

« Hide

        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.
PIRiT14106.
RefSeqiNP_647546.1. NM_139330.1.
UniGeneiRn.10835.

3D structure databases

ProteinModelPortaliO35412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251530. 7 interactors.
STRINGi10116.ENSRNOP00000054996.

PTM databases

iPTMnetiO35412.
PhosphoSitePlusiO35412.

Proteomic databases

PaxDbiO35412.
PRIDEiO35412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26037.
RGDi708497. Sipa1l1.

Phylogenomic databases

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO35412.
KOiK17701.
PhylomeDBiO35412.

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

PROiO35412.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR021818. SIPA1L_C.
[Graphical view]
PfamiPF02145. Rap_GAP. 1 hit.
PF11881. SPAR_C. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 2 hits.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.