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Protein

Angiomotin-like protein 2

Gene

Amotl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC (By similarity).By similarity

GO - Molecular functioni

  • identical protein binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-2028269. Signaling by Hippo.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiomotin-like protein 2
Gene namesi
Name:Amotl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1929286. Amotl2.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • bicellular tight junction Source: MGI
  • cytoplasmic vesicle Source: MGI
  • recycling endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001906731 – 772Angiomotin-like protein 2Add BLAST772

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei107Phosphotyrosine; by FGFR1By similarity1
Modified residuei752PhosphoserineCombined sources1
Modified residuei755PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Tyr-107 is necessary for efficient binding to SRC and synergistically functioning with SRC to activate the downstream MAPK pathway.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8K371.
PaxDbiQ8K371.
PRIDEiQ8K371.

PTM databases

iPTMnetiQ8K371.
PhosphoSitePlusiQ8K371.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032531.
CleanExiMM_AMOTL2.
ExpressionAtlasiQ8K371. baseline and differential.
GenevisibleiQ8K371. MM.

Interactioni

Subunit structurei

Interacts with SRC.By similarity

GO - Molecular functioni

  • identical protein binding Source: MGI

Protein-protein interaction databases

BioGridi207908. 7 interactors.
IntActiQ8K371. 1 interactor.
STRINGi10090.ENSMUSP00000035121.

Structurei

3D structure databases

ProteinModelPortaliQ8K371.
SMRiQ8K371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili305 – 578Sequence analysisAdd BLAST274

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi769 – 772PDZ-binding4

Sequence similaritiesi

Belongs to the angiomotin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEF3. Eukaryota.
ENOG410ZEXZ. LUCA.
GeneTreeiENSGT00530000063846.
HOGENOMiHOG000233789.
HOVERGENiHBG066485.
InParanoidiQ8K371.
PhylomeDBiQ8K371.
TreeFamiTF333368.

Family and domain databases

InterProiIPR009114. Angiomotin.
IPR024646. Angiomotin_C.
[Graphical view]
PfamiPF12240. Angiomotin_C. 1 hit.
[Graphical view]
PRINTSiPR01807. ANGIOMOTIN.

Sequencei

Sequence statusi: Complete.

Q8K371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLEDSSGT VLHRLIQEQL RYGNLTETRT LLAIQQQALR GGAGAGGTGS
60 70 80 90 100
PQASLEIGAP EDSQVLQQAT RQEPQGQEHQ GGETHLAENR LYRLCPQPSK
110 120 130 140 150
GEELPTYEEA KAHSQYYAAQ QAGSRPHVGD RDPRGGVSGG GRRQDEALRE
160 170 180 190 200
LRHGHVRSLS ERLLQLSLER NGARVPSHMS SSHSFPQLAR SQQGPQPRGP
210 220 230 240 250
PAEGPEPRGP PPQYPHAVMA QETAAVTDPR YRPRSSPHFQ HAEVRILQAQ
260 270 280 290 300
VPPVFLQQQQ YQYLPQPQEH SPPLHPAALG HGPPSSFGPP AVEGPPSAQA
310 320 330 340 350
TLGSAHLAQM ETVLRENARL QRDNERLQRE LESTSEKAGR IEKLENEIQR
360 370 380 390 400
LSEAHESLMR TSSKREALEK TMRNKMDGEM RRLQDFNRDL RERLESANRH
410 420 430 440 450
LASKTQEAQA GSQDMVAKLL AQSYEQQQEQ EKLEREMALL RGAIEDQRRH
460 470 480 490 500
AELLEQALGN AQSRAARAEE ELRKKQAYVE KVERLQQALG QLQAACEKRE
510 520 530 540 550
QLELRLRTRL EQELKALRAQ QRQTGTLAGG GGSHGGSAEL SALRLSEQLR
560 570 580 590 600
EKEEQILALE ADMTKWEQKY LEERAMRQFA MDAAATAAAQ RDTTLIRHSP
610 620 630 640 650
QPSPSSSFNE GLLPGNHRHQ EMESRLKVLH AQILEKDAVI KVLQQRSRKD
660 670 680 690 700
PGKATQGTLR PAKSVPSIFA AAVGTQGWQG LVSSERQTDA RPAGDRVPAE
710 720 730 740 750
EPPATAPLPA HTKHGSRDGS TQTDGPADNT SACLASEPDG LLGCNSSQRT
760 770
PSLDSIAATR VQDLSDMVEI LI
Length:772
Mass (Da):85,278
Last modified:October 1, 2002 - v1
Checksum:i9979F5F4D2A54989
GO

Sequence cautioni

The sequence BAC30740 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC36853 differs from that shown. Reason: Frameshift at position 171.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti163 – 165LLQ → ILK in BAC36853 (PubMed:16141072).Curated3
Sequence conflicti187 – 197QLARSQQGPQP → EPPGFLGDRST in AAD56362 (PubMed:12406577).CuratedAdd BLAST11
Sequence conflicti257Q → H in AAD56362 (PubMed:12406577).Curated1
Sequence conflicti389D → N in BAC36853 (PubMed:16141072).Curated1
Sequence conflicti450H → N in BAC36853 (PubMed:16141072).Curated1
Sequence conflicti481K → R in AAD56362 (PubMed:12406577).Curated1
Sequence conflicti481K → R in AAD56363 (PubMed:12406577).Curated1
Sequence conflicti643L → P in AAD56362 (PubMed:12406577).Curated1
Sequence conflicti643L → P in AAD56363 (PubMed:12406577).Curated1
Sequence conflicti660R → W in AAD56362 (PubMed:12406577).Curated1
Sequence conflicti660R → W in AAD56363 (PubMed:12406577).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040912 mRNA. Translation: BAC30740.1. Different initiation.
AK077535 mRNA. Translation: BAC36853.1. Frameshift.
AK141348 mRNA. Translation: BAE24658.1.
AK164279 mRNA. Translation: BAE37715.1.
CT573150 Genomic DNA. Translation: CAX15827.1.
CH466560 Genomic DNA. Translation: EDL21058.1.
BC027824 mRNA. Translation: AAH27824.1.
AF175967 mRNA. Translation: AAD56362.2.
AF175968 mRNA. Translation: AAD56363.1.
CCDSiCCDS40745.1.
RefSeqiNP_062738.2. NM_019764.2.
XP_006511834.2. XM_006511771.3.
XP_006511836.1. XM_006511773.2.
UniGeneiMm.21145.

Genome annotation databases

EnsembliENSMUST00000035121; ENSMUSP00000035121; ENSMUSG00000032531.
GeneIDi56332.
KEGGimmu:56332.
UCSCiuc009rfx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040912 mRNA. Translation: BAC30740.1. Different initiation.
AK077535 mRNA. Translation: BAC36853.1. Frameshift.
AK141348 mRNA. Translation: BAE24658.1.
AK164279 mRNA. Translation: BAE37715.1.
CT573150 Genomic DNA. Translation: CAX15827.1.
CH466560 Genomic DNA. Translation: EDL21058.1.
BC027824 mRNA. Translation: AAH27824.1.
AF175967 mRNA. Translation: AAD56362.2.
AF175968 mRNA. Translation: AAD56363.1.
CCDSiCCDS40745.1.
RefSeqiNP_062738.2. NM_019764.2.
XP_006511834.2. XM_006511771.3.
XP_006511836.1. XM_006511773.2.
UniGeneiMm.21145.

3D structure databases

ProteinModelPortaliQ8K371.
SMRiQ8K371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207908. 7 interactors.
IntActiQ8K371. 1 interactor.
STRINGi10090.ENSMUSP00000035121.

PTM databases

iPTMnetiQ8K371.
PhosphoSitePlusiQ8K371.

Proteomic databases

MaxQBiQ8K371.
PaxDbiQ8K371.
PRIDEiQ8K371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035121; ENSMUSP00000035121; ENSMUSG00000032531.
GeneIDi56332.
KEGGimmu:56332.
UCSCiuc009rfx.1. mouse.

Organism-specific databases

CTDi51421.
MGIiMGI:1929286. Amotl2.

Phylogenomic databases

eggNOGiENOG410IEF3. Eukaryota.
ENOG410ZEXZ. LUCA.
GeneTreeiENSGT00530000063846.
HOGENOMiHOG000233789.
HOVERGENiHBG066485.
InParanoidiQ8K371.
PhylomeDBiQ8K371.
TreeFamiTF333368.

Enzyme and pathway databases

ReactomeiR-MMU-2028269. Signaling by Hippo.

Miscellaneous databases

PROiQ8K371.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032531.
CleanExiMM_AMOTL2.
ExpressionAtlasiQ8K371. baseline and differential.
GenevisibleiQ8K371. MM.

Family and domain databases

InterProiIPR009114. Angiomotin.
IPR024646. Angiomotin_C.
[Graphical view]
PfamiPF12240. Angiomotin_C. 1 hit.
[Graphical view]
PRINTSiPR01807. ANGIOMOTIN.
ProtoNetiSearch...

Entry informationi

Entry nameiAMOL2_MOUSE
AccessioniPrimary (citable) accession number: Q8K371
Secondary accession number(s): B8JK80
, Q3TPM1, Q7TPE4, Q8BP84, Q8BS08, Q9QUS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: October 1, 2002
Last modified: November 2, 2016
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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.