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Protein

Signal-induced proliferation-associated 1-like protein 1

Gene

SIPA1L1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

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 1
Short name:
SIPA1-like protein 1
Alternative name(s):
High-risk human papilloma viruses E6 oncoproteins targeted protein 1
Short name:
E6-targeted protein 1
Gene namesi
Name:SIPA1L1
Synonyms:E6TP1, KIAA0440
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20284. SIPA1L1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134940118.

Polymorphism and mutation databases

BioMutaiSIPA1L1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18041804Signal-induced proliferation-associated 1-like protein 1PRO_0000056746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei255 – 2551PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei1127 – 11271PhosphoserineBy similarity
Modified residuei1181 – 11811PhosphoserineCombined sources
Modified residuei1255 – 12551PhosphoserineCombined sources
Modified residuei1270 – 12701PhosphoserineCombined sources
Modified residuei1326 – 13261Phosphoserine; by PLK2By similarity
Modified residuei1330 – 13301Phosphothreonine; by PLK2By similarity
Modified residuei1349 – 13491Phosphoserine; by CDK5By similarity
Modified residuei1431 – 14311PhosphoserineCombined sources
Modified residuei1433 – 14331PhosphoserineCombined sources
Modified residuei1549 – 15491PhosphoserineCombined sources
Modified residuei1551 – 15511PhosphothreonineCombined sources
Modified residuei1554 – 15541PhosphoserineCombined sources
Modified residuei1565 – 15651PhosphoserineCombined sources
Modified residuei1568 – 15681PhosphoserineCombined sources
Modified residuei1585 – 15851PhosphoserineCombined sources
Modified residuei1603 – 16031PhosphoserineBy similarity
Modified residuei1645 – 16451PhosphoserineBy similarity
Modified residuei1647 – 16471PhosphoserineBy similarity
Modified residuei1650 – 16501PhosphoserineBy similarity
Modified residuei1708 – 17081PhosphoserineBy similarity
Modified residuei1711 – 17111PhosphoserineBy similarity
Modified residuei1728 – 17281PhosphoserineBy similarity
Modified residuei1729 – 17291PhosphoserineBy similarity
Modified residuei1734 – 17341PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.By similarity
Phosphorylated at Ser-1349 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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43166.
MaxQBiO43166.
PaxDbiO43166.
PRIDEiO43166.

PTM databases

iPTMnetiO43166.
PhosphoSiteiO43166.

Miscellaneous databases

PMAP-CutDBO43166.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiO43166.
CleanExiHS_SIPA1L1.
ExpressionAtlasiO43166. baseline and differential.
GenevisibleiO43166. HS.

Organism-specific databases

HPAiHPA002875.

Interactioni

Subunit structurei

Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton (By similarity). 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. Interacts with HPV E6.By similarity2 Publications

Protein-protein interaction databases

BioGridi117503. 30 interactions.
IntActiO43166. 22 interactions.
MINTiMINT-1177792.
STRINGi9606.ENSP00000450832.

Structurei

3D structure databases

ProteinModelPortaliO43166.
SMRiO43166. Positions 489-819, 952-1027.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini613 – 830218Rap-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini967 – 104579PDZPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1735 – 179561Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi107 – 14337Ser-richAdd
BLAST
Compositional biasi1154 – 11574Poly-Ser
Compositional biasi1291 – 1486196Ser-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

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
GeneTreeiENSGT00760000119182.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO43166.
KOiK17701.
OMAiESELNSY.
OrthoDBiEOG7DVD9F.
PhylomeDBiO43166.
TreeFamiTF318626.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR030770. SIPA1L1.
IPR021818. SIPA1L_C.
[Graphical view]
PANTHERiPTHR15711:SF10. PTHR15711:SF10. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43166-1) [UniParc]FASTAAdd to basket

Also known as: E6TP1 beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSLKRSQTE RPLATDRASV VGTDGTPKVH TDDFYMRRFR SQNGSLGSSV
60 70 80 90 100
MAPVGPPRSE GSHHITSTPG VPKMGVRARI ADWPPRKENI KESSRSSQEI
110 120 130 140 150
ETSSCLDSLS SKSSPVSQGS SVSLNSNDSA MLKSIQNTLK NKTRPSENMD
160 170 180 190 200
SRFLMPEAYP SSPRKALRRI RQRSNSDITI SELDVDSFDE CISPTYKTGP
210 220 230 240 250
SLHREYGSTS SIDKQGTSGE SFFDLLKGYK DDKSDRGPTP 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 LVSGPLSHSA SFSSPMGSTE DLNSKGSLSM
410 420 430 440 450
DQGDDKSNEL VMSCPYFRNE IGGEGERKIS LSKSNSGSFS GCESASFEST
460 470 480 490 500
LSSHCTNAGV AVLEVPKENL VLHLDRVKRY IVEHVDLGAY YYRKFFYQKE
510 520 530 540 550
HWNYFGADEN LGPVAVSIRR EKPDEMKENG SPYNYRIIFR TSELMTLRGS
560 570 580 590 600
VLEDAIPSTA KHSTARGLPL KEVLEHVVPE LNVQCLRLAF NTPKVTEQLM
610 620 630 640 650
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN NESAGPAFEE FLQLLGERVR
660 670 680 690 700
LKGFEKYRAQ LDTKTDSTGT HSLYTTYKDY EIMFHVSTML PYTPNNKQQL
710 720 730 740 750
LRKRHIGNDI VTIVFQEPGA QPFSPKNIRS HFQHVFVIVR VHNPCSDSVC
760 770 780 790 800
YSVAVTRSRD VPSFGPPIPK GVTFPKSNVF RDFLLAKVIN AENAAHKSEK
810 820 830 840 850
FRAMATRTRQ EYLKDLAEKN VTNTPIDPSG KFPFISLASK KKEKSKPYPG
860 870 880 890 900
AELSSMGAIV WAVRAEDYNK AMELDCLLGI SNEFIVLIEQ ETKSVVFNCS
910 920 930 940 950
CRDVIGWTST DTSLKIFYER GECVSVGSFI NIEEIKEIVK RLQFVSKGCE
960 970 980 990 1000
SVEMTLRRNG LGQLGFHVNY EGIVADVEPY GYAWQAGLRQ GSRLVEICKV
1010 1020 1030 1040 1050
AVATLSHEQM IDLLRTSVTV KVVIIPPHDD CTPRRSCSET YRMPVMEYKM
1060 1070 1080 1090 1100
NEGVSYEFKF PFRNNNKWQR NASKGPHSPQ VPSQVQSPMT SRLNAGKGDG
1110 1120 1130 1140 1150
KMPPPERAAN IPRSISSDGR PLERRLSPGS DIYVTVSSMA LARSQCRNSP
1160 1170 1180 1190 1200
SNLSSSSDTG SVGGTYRQKS MPEGFGVSRR SPASIDRQNT QSDIGGSGKS
1210 1220 1230 1240 1250
TPSWQRSEDS IADQMAYSYR GPQDFNSFVL EQHEYTEPTC HLPAVSKVLP
1260 1270 1280 1290 1300
AFRESPSGRL MRQDPVVHLS PNKQGHSDSH YSSHSSSNTL SSNASSAHSD
1310 1320 1330 1340 1350
EKWYDGDRTE SELNSYNYLQ GTSADSGIDT TSYGPSHGST ASLGAATSSP
1360 1370 1380 1390 1400
RSGPGKEKVA PLWHSSSEVI SMADRTLETE SHGLDRKTES SLSLDIHSKS
1410 1420 1430 1440 1450
QAGSTPLTRE NSTFSINDAA SHTSTMSSRH SASPVVFTSA RSSPKEELHP
1460 1470 1480 1490 1500
AAPSQLAPSF SSSSSSSSGP RSFYPRQGAT SKYLIGWKKP EGTINSVGFM
1510 1520 1530 1540 1550
DTRKRHQSDG NEIAHTRLRA STRDLRASPK PTSKSTIEED LKKLIDLESP
1560 1570 1580 1590 1600
TPESQKSFKF HALSSPQSPF PSTPTSRRAL HRTLSDESIY NSQREHFFTS
1610 1620 1630 1640 1650
RASLLDQALP NDVLFSSTYP SLPKSLPLRR PSYTLGMKSL HGEFSASDSS
1660 1670 1680 1690 1700
LTDIQETRRQ PMPDPGLMPL PDTAADLDWS NLVDAAKAYE VQRASFFAAS
1710 1720 1730 1740 1750
DENHRPLSAA SNSDQLEDQA LAQMKPYSSS KDSSPTLASK VDQLEGMLKM
1760 1770 1780 1790 1800
LREDLKKEKE DKAHLQAEVQ HLREDNLRLQ EESQNASDKL KKFTEWVFNT

IDMS
Length:1,804
Mass (Da):200,029
Last modified:October 3, 2006 - v4
Checksum:i91AB6AB4E7F47B2F
GO
Isoform 2 (identifier: O43166-2) [UniParc]FASTAAdd to basket

Also known as: E6TP1 alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1216-1236: Missing.

Show »
Length:1,783
Mass (Da):197,495
Checksum:i8C9FB14DBD867FCC
GO
Isoform 3 (identifier: O43166-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1216-1236: Missing.
     1728-1728: Missing.

Note: No experimental confirmation available.
Show »
Length:1,782
Mass (Da):197,408
Checksum:iDFF4318DCB195EC5
GO

Sequence cautioni

The sequence BAA23712.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1387 – 13871K → R in AK122930 (PubMed:14702039).Curated
Sequence conflicti1722 – 17221A → P in BAA23712 (PubMed:9455477).Curated
Sequence conflicti1730 – 17301Missing in BAA23712 (PubMed:9455477).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561P → T.
Corresponds to variant rs12884638 [ dbSNP | Ensembl ].
VAR_049152
Natural varianti996 – 9961E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_035549

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1216 – 123621Missing in isoform 2 and isoform 3. 2 PublicationsVSP_010917Add
BLAST
Alternative sequencei1728 – 17281Missing in isoform 3. 1 PublicationVSP_054774

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090989 mRNA. Translation: AAD12543.1.
AF090990 mRNA. Translation: AAD12544.1.
AB007900 mRNA. Translation: BAA23712.2. Different initiation.
AK122930 mRNA. No translation available.
AC004974 Genomic DNA. Translation: AAC83179.1.
AC004900 Genomic DNA. No translation available.
AC004968 Genomic DNA. No translation available.
AC005476 Genomic DNA. No translation available.
AC005994 Genomic DNA. No translation available.
AL391735 Genomic DNA. No translation available.
CCDSiCCDS61490.1. [O43166-2]
CCDS61491.1. [O43166-3]
CCDS9807.1. [O43166-1]
RefSeqiNP_001271174.1. NM_001284245.1. [O43166-2]
NP_001271175.1. NM_001284246.1. [O43166-3]
NP_001271176.1. NM_001284247.1.
NP_056371.1. NM_015556.2. [O43166-1]
XP_005267573.1. XM_005267516.3. [O43166-1]
XP_005267576.1. XM_005267519.1. [O43166-3]
XP_006720172.1. XM_006720109.2. [O43166-1]
XP_006720175.1. XM_006720112.1. [O43166-2]
XP_011534932.1. XM_011536630.1. [O43166-1]
XP_011534933.1. XM_011536631.1. [O43166-1]
XP_011534934.1. XM_011536632.1. [O43166-1]
XP_011534935.1. XM_011536633.1. [O43166-1]
XP_011534936.1. XM_011536634.1. [O43166-1]
XP_011534937.1. XM_011536635.1. [O43166-1]
UniGeneiHs.654657.

Genome annotation databases

EnsembliENST00000358550; ENSP00000351352; ENSG00000197555. [O43166-3]
ENST00000381232; ENSP00000370630; ENSG00000197555. [O43166-2]
ENST00000555818; ENSP00000450832; ENSG00000197555. [O43166-1]
GeneIDi26037.
KEGGihsa:26037.
UCSCiuc001xms.5. human. [O43166-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090989 mRNA. Translation: AAD12543.1.
AF090990 mRNA. Translation: AAD12544.1.
AB007900 mRNA. Translation: BAA23712.2. Different initiation.
AK122930 mRNA. No translation available.
AC004974 Genomic DNA. Translation: AAC83179.1.
AC004900 Genomic DNA. No translation available.
AC004968 Genomic DNA. No translation available.
AC005476 Genomic DNA. No translation available.
AC005994 Genomic DNA. No translation available.
AL391735 Genomic DNA. No translation available.
CCDSiCCDS61490.1. [O43166-2]
CCDS61491.1. [O43166-3]
CCDS9807.1. [O43166-1]
RefSeqiNP_001271174.1. NM_001284245.1. [O43166-2]
NP_001271175.1. NM_001284246.1. [O43166-3]
NP_001271176.1. NM_001284247.1.
NP_056371.1. NM_015556.2. [O43166-1]
XP_005267573.1. XM_005267516.3. [O43166-1]
XP_005267576.1. XM_005267519.1. [O43166-3]
XP_006720172.1. XM_006720109.2. [O43166-1]
XP_006720175.1. XM_006720112.1. [O43166-2]
XP_011534932.1. XM_011536630.1. [O43166-1]
XP_011534933.1. XM_011536631.1. [O43166-1]
XP_011534934.1. XM_011536632.1. [O43166-1]
XP_011534935.1. XM_011536633.1. [O43166-1]
XP_011534936.1. XM_011536634.1. [O43166-1]
XP_011534937.1. XM_011536635.1. [O43166-1]
UniGeneiHs.654657.

3D structure databases

ProteinModelPortaliO43166.
SMRiO43166. Positions 489-819, 952-1027.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117503. 30 interactions.
IntActiO43166. 22 interactions.
MINTiMINT-1177792.
STRINGi9606.ENSP00000450832.

PTM databases

iPTMnetiO43166.
PhosphoSiteiO43166.

Polymorphism and mutation databases

BioMutaiSIPA1L1.

Proteomic databases

EPDiO43166.
MaxQBiO43166.
PaxDbiO43166.
PRIDEiO43166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358550; ENSP00000351352; ENSG00000197555. [O43166-3]
ENST00000381232; ENSP00000370630; ENSG00000197555. [O43166-2]
ENST00000555818; ENSP00000450832; ENSG00000197555. [O43166-1]
GeneIDi26037.
KEGGihsa:26037.
UCSCiuc001xms.5. human. [O43166-1]

Organism-specific databases

CTDi26037.
GeneCardsiSIPA1L1.
HGNCiHGNC:20284. SIPA1L1.
HPAiHPA002875.
neXtProtiNX_O43166.
PharmGKBiPA134940118.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3686. Eukaryota.
ENOG410XTIX. LUCA.
GeneTreeiENSGT00760000119182.
HOGENOMiHOG000154319.
HOVERGENiHBG056135.
InParanoidiO43166.
KOiK17701.
OMAiESELNSY.
OrthoDBiEOG7DVD9F.
PhylomeDBiO43166.
TreeFamiTF318626.

Miscellaneous databases

ChiTaRSiSIPA1L1. human.
GeneWikiiSIPA1L1.
GenomeRNAii26037.
PMAP-CutDBO43166.
PROiO43166.

Gene expression databases

BgeeiO43166.
CleanExiHS_SIPA1L1.
ExpressionAtlasiO43166. baseline and differential.
GenevisibleiO43166. HS.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR000331. Rap_GAP_dom.
IPR030770. SIPA1L1.
IPR021818. SIPA1L_C.
[Graphical view]
PANTHERiPTHR15711:SF10. PTHR15711:SF10. 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. "The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation."
    Gao Q., Srinivasan S., Boyer S.N., Wazer D.E., Band V.
    Mol. Cell. Biol. 19:733-744(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH HPV E6.
  2. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: INTERACTION WITH EPHA4.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 SER-162; SER-288; SER-1549 AND SER-1585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255; SER-1270; SER-1433; SER-1549; THR-1551; SER-1554; SER-1565 AND SER-1568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181; SER-1270; SER-1431; SER-1433; SER-1549; SER-1585 AND SER-1734, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-187; SER-193; SER-255; SER-1549; SER-1585 AND SER-1734, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-996.

Entry informationi

Entry nameiSI1L1_HUMAN
AccessioniPrimary (citable) accession number: O43166
Secondary accession number(s): J3KP19
, O95321, Q9UDU4, Q9UNU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 3, 2006
Last modified: June 8, 2016
This is version 143 of the entry and version 4 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 14
    Human chromosome 14: 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. 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.