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Protein

Signal-induced proliferation-associated 1-like protein 3

Gene

SIPA1L3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217).1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Signal-induced proliferation-associated 1-like protein 3
Short name:
SIPA1-like protein 3
Alternative name(s):
SPA-1-like protein 3
Gene namesi
Name:SIPA1L3
Synonyms:KIAA0545, SPAL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:23801. SIPA1L3.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: UniProtKB
  • apical plasma membrane Source: UniProtKB-SubCell
  • extracellular space Source: UniProtKB
  • stress fiber Source: UniProtKB
  • tricellular tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal translocation involving SIPA1L3 is found in a patient with bilateral severe ocular abnormalities including congenital cataracts, corneal clouding, iridocorneal and lenticular adhesions and microphthalmia. Chromosomal translocation t(2;19)(q37.3;q13.1). In addition to translocation, missense variant has been found in patient with bilateral congenital cataracts (PubMed:26231217).

Organism-specific databases

PharmGKBiPA134866783.

Polymorphism and mutation databases

BioMutaiSIPA1L3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17811781Signal-induced proliferation-associated 1-like protein 3PRO_0000056752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei401 – 4011PhosphoserineCombined sources
Modified residuei1364 – 13641PhosphoserineBy similarity
Modified residuei1387 – 13871PhosphothreonineBy similarity
Modified residuei1448 – 14481N6-acetyllysineCombined sources
Modified residuei1544 – 15441PhosphoserineCombined sources
Modified residuei1547 – 15471PhosphoserineBy similarity
Modified residuei1619 – 16191PhosphoserineBy similarity
Modified residuei1622 – 16221PhosphoserineBy similarity
Modified residuei1677 – 16771PhosphoserineBy similarity
Modified residuei1699 – 16991PhosphothreonineCombined sources
Modified residuei1703 – 17031PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO60292.
MaxQBiO60292.
PaxDbiO60292.
PRIDEiO60292.

PTM databases

iPTMnetiO60292.
PhosphoSiteiO60292.

Expressioni

Gene expression databases

BgeeiO60292.
CleanExiHS_SIPA1L3.
ExpressionAtlasiO60292. baseline and differential.
GenevisibleiO60292. HS.

Organism-specific databases

HPAiHPA042072.
HPA045480.

Interactioni

Protein-protein interaction databases

BioGridi116722. 36 interactions.
IntActiO60292. 32 interactions.
MINTiMINT-2796588.
STRINGi9606.ENSP00000222345.

Structurei

3D structure databases

ProteinModelPortaliO60292.
SMRiO60292. Positions 501-830, 963-1037.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini611 – 828218Rap-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini966 – 104277PDZPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1720 – 177455Sequence analysisAdd
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

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
GeneTreeiENSGT00760000119182.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO60292.
KOiK17703.
OMAiFSDPKKQ.
OrthoDBiEOG7DVD9F.
PhylomeDBiO60292.
TreeFamiTF318626.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR031204. SIPA1L3.
IPR021818. SIPA1L_C.
[Graphical view]
PANTHERiPTHR15711:SF15. PTHR15711:SF15. 4 hits.
PfamiPF02145. Rap_GAP. 1 hit.
PF11881. SPAR_C. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60292-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTYRAIPSD GVDLAASCGA RVGDVLPGPH TGDYAPLGFW AQNGSMSQPL
60 70 80 90 100
GESPATATAT ATATTRPSPT TPAMPKMGVR ARVADWPPKR EALREHSNPS
110 120 130 140 150
PSQDTDGTKA TKMAHSMRSI QNGQPPTSTP ASSGSKAFHR LSRRRSKDVE
160 170 180 190 200
FQDGWPRSPG RAFLPLRHRS SSEITLSECD AEDAGEPRGA RHTGALPLFR
210 220 230 240 250
EYGSTSSIDV QGMPEQSFFD ILNEFRSEQP DARGCQALTE LLRADPGPHL
260 270 280 290 300
MGGGGGAKGD SHNGQPAKDS LLPLQPTKEK EKARKKPARG LGGGDTVDSS
310 320 330 340 350
IFRKLRSSKP EGEAGRSPGE ADEGRSPPEA SRPWVCQKSF AHFDVQSMLF
360 370 380 390 400
DLNEAAANRV SVSQRRNTTT GASAASAASA MASLTASRAH SLGGLDPAFT
410 420 430 440 450
STEDLNCKEN LEQDLGDDNS NDLLLSCPHF RNEIGGECER NVSFSRASVG
460 470 480 490 500
SPSSGEGHLA EPALSAYRTN ASISVLEVPK EQQRTQSRPR QYSIEHVDLG
510 520 530 540 550
ARYYQDYFVG KEHANYFGVD EKLGPVAVSI KREKLEDHKE HGPQYQYRII
560 570 580 590 600
FRTRELITLR GSILEDATPT ATKHGTGRGL PLKDALEYVI PELNIHCLRL
610 620 630 640 650
ALNTPKVTEQ LLKLDEQGLC RKHKVGILYC KAGQSSEEEM YNNEEAGPAF
660 670 680 690 700
EEFLSLIGEK VCLKGFTKYA AQLDVKTDST GTHSLYTMYQ DYEIMFHVST
710 720 730 740 750
LLPYTPNNRQ QLLRKRHIGN DIVTIIFQEP GALPFTPKNI RSHFQHVFII
760 770 780 790 800
VRVHNPCTDN VCYSMAVTRS KDAPPFGPPI PSGTTFRKSD VFRDFLLAKV
810 820 830 840 850
INAENAAHKS DKFHTMATRT RQEYLKDLAE NCVSNTPIDS TGKFNLISLT
860 870 880 890 900
SKKKEKTKAR AGAEQHSAGA IAWRVVAQDY AQGVEIDCIL GISNEFVVLL
910 920 930 940 950
DLRTKEVVFN CYCGDVIGWT PDSSTLKIFY GRGDHIFLQA TEGSVEDIRE
960 970 980 990 1000
IVQRLKVMTS GWETVDMTLR RNGLGQLGFH VKYDGTVAEV EDYGFAWQAG
1010 1020 1030 1040 1050
LRQGSRLVEI CKVAVVTLTH DQMIDLLRTS VTVKVVIIPP FEDGTPRRGW
1060 1070 1080 1090 1100
PETYDMNTSE PKTEQESITP GGRPPYRSNA PWQWSGPASH NSLPASKWAT
1110 1120 1130 1140 1150
PTTPGHAQSL SRPLKQTPIV PFRESQPLHS KRPVSFPETP YTVSPAGADR
1160 1170 1180 1190 1200
VPPYRQPSGS FSTPGSATYV RYKPSPERYT AAPHPLLSLD PHFSHDGTSS
1210 1220 1230 1240 1250
GDSSSGGLTS QESTMERQKP EPLWHVPAQA RLSAIAGSSG NKHPSRQDAA
1260 1270 1280 1290 1300
GKDSPNRHSK GEPQYSSHSS SNTLSSNASS SHSDDRWFDP LDPLEPEQDP
1310 1320 1330 1340 1350
LSKGGSSDSG IDTTLYTSSP SCMSLAKAPR PAKPHKPPGS MGLCGGGREA
1360 1370 1380 1390 1400
AGRSHHADRR REVSPAPAVA GQSKGYRPKL YSSGSSTPTG LAGGSRDPPR
1410 1420 1430 1440 1450
QPSDMGSRVG YPAQVYKTAS AETPRPSQLA QPSPFQLSAS VPKSFFSKQP
1460 1470 1480 1490 1500
VRNKHPTGWK RTEEPPPRPL PFSDPKKQVD TNTKNVFGQP RLRASLRDLR
1510 1520 1530 1540 1550
SPRKNYKSTI EDDLKKLIIM DNLGPEQERD TGQSPQKGLQ RTLSDESLCS
1560 1570 1580 1590 1600
GRREPSFASP AGLEPGLPSD VLFTSTCAFP SSTLPARRQH QHPHPPVGPG
1610 1620 1630 1640 1650
ATPAAGSGFP EKKSTISASE LSLADGRDRP LRRLDPGLMP LPDTAAGLEW
1660 1670 1680 1690 1700
SSLVNAAKAY EVQRAVSLFS LNDPALSPDI PPAHSPVHSH LSLERGPPTP
1710 1720 1730 1740 1750
RTTPTMSEEP PLDLTGKVYQ LEVMLKQLHT DLQKEKQDKV VLQSEVASLR
1760 1770 1780
QNNQRLQEES QAASEQLRKF AEIFCREKKE L
Length:1,781
Mass (Da):194,610
Last modified:March 7, 2006 - v3
Checksum:i6A91F43B5BC3E175
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481D → Y Probable disease-associated mutation found in a patient with bilateral congenital cataracts; lacks of normal basal actin stress fiber formation; absence of SIPA1L3 and F-actin colocalization. 1 Publication
VAR_075045
Natural varianti1371 – 13711G → S.
Corresponds to variant rs2304133 [ dbSNP | Ensembl ].
VAR_025476
Natural varianti1450 – 14501P → A.
Corresponds to variant rs3745945 [ dbSNP | Ensembl ].
VAR_025477

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168880 mRNA. Translation: AAO12531.1.
AB011117 mRNA. Translation: BAA25471.2.
AC011465 Genomic DNA. No translation available.
AC011479 Genomic DNA. No translation available.
CCDSiCCDS33007.1.
RefSeqiNP_055888.1. NM_015073.2.
XP_005258728.1. XM_005258671.3.
XP_011524959.1. XM_011526657.1.
UniGeneiHs.655502.

Genome annotation databases

EnsembliENST00000222345; ENSP00000222345; ENSG00000105738.
GeneIDi23094.
KEGGihsa:23094.
UCSCiuc002ohk.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY168880 mRNA. Translation: AAO12531.1.
AB011117 mRNA. Translation: BAA25471.2.
AC011465 Genomic DNA. No translation available.
AC011479 Genomic DNA. No translation available.
CCDSiCCDS33007.1.
RefSeqiNP_055888.1. NM_015073.2.
XP_005258728.1. XM_005258671.3.
XP_011524959.1. XM_011526657.1.
UniGeneiHs.655502.

3D structure databases

ProteinModelPortaliO60292.
SMRiO60292. Positions 501-830, 963-1037.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116722. 36 interactions.
IntActiO60292. 32 interactions.
MINTiMINT-2796588.
STRINGi9606.ENSP00000222345.

PTM databases

iPTMnetiO60292.
PhosphoSiteiO60292.

Polymorphism and mutation databases

BioMutaiSIPA1L3.

Proteomic databases

EPDiO60292.
MaxQBiO60292.
PaxDbiO60292.
PRIDEiO60292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222345; ENSP00000222345; ENSG00000105738.
GeneIDi23094.
KEGGihsa:23094.
UCSCiuc002ohk.4. human.

Organism-specific databases

CTDi23094.
GeneCardsiSIPA1L3.
HGNCiHGNC:23801. SIPA1L3.
HPAiHPA042072.
HPA045480.
MIMi616655. gene.
neXtProtiNX_O60292.
PharmGKBiPA134866783.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
GeneTreeiENSGT00760000119182.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO60292.
KOiK17703.
OMAiFSDPKKQ.
OrthoDBiEOG7DVD9F.
PhylomeDBiO60292.
TreeFamiTF318626.

Miscellaneous databases

ChiTaRSiSIPA1L3. human.
GenomeRNAii23094.
NextBioi44255.
PROiO60292.
SOURCEiSearch...

Gene expression databases

BgeeiO60292.
CleanExiHS_SIPA1L3.
ExpressionAtlasiO60292. baseline and differential.
GenevisibleiO60292. HS.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR031204. SIPA1L3.
IPR021818. SIPA1L_C.
[Graphical view]
PANTHERiPTHR15711:SF15. PTHR15711:SF15. 4 hits.
PfamiPF02145. Rap_GAP. 1 hit.
PF11881. SPAR_C. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Matsuura K., Kohu K., Akiyama T.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-1781.
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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 THR-1699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT TYR-148, CHARACTERIZATION OF VARIANT TYR-148, CHROMOSOMAL TRANSLOCATION.

Entry informationi

Entry nameiSI1L3_HUMAN
AccessioniPrimary (citable) accession number: O60292
Secondary accession number(s): Q2TV87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 7, 2006
Last modified: April 13, 2016
This is version 126 of the entry and version 3 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.