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Q4VCS5

- AMOT_HUMAN

UniProt

Q4VCS5 - AMOT_HUMAN

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Protein

Angiomotin

Gene

AMOT

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

Functioni

Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions.2 Publications

GO - Molecular functioni

  1. angiostatin binding Source: UniProtKB
  2. receptor activity Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. blood vessel endothelial cell migration Source: Ensembl
  3. cell-cell junction assembly Source: UniProtKB
  4. cell migration involved in gastrulation Source: Ensembl
  5. cellular protein localization Source: MGI
  6. chemotaxis Source: Ensembl
  7. establishment of cell polarity involved in ameboidal cell migration Source: Ensembl
  8. gastrulation with mouth forming second Source: Ensembl
  9. hippo signaling Source: MGI
  10. in utero embryonic development Source: Ensembl
  11. negative regulation of angiogenesis Source: MGI
  12. negative regulation of GTPase activity Source: Ensembl
  13. negative regulation of vascular permeability Source: UniProtKB
  14. positive regulation of blood vessel endothelial cell migration Source: UniProtKB
  15. positive regulation of cell size Source: UniProtKB
  16. positive regulation of embryonic development Source: Ensembl
  17. positive regulation of stress fiber assembly Source: UniProtKB
  18. regulation of cell migration Source: MGI
  19. regulation of small GTPase mediated signal transduction Source: Ensembl
  20. vasculogenesis Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118607. Signaling by Hippo.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiomotin
Gene namesi
Name:AMOT
Synonyms:KIAA1071
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:17810. AMOT.

Subcellular locationi

Cell junctiontight junction 1 Publication
Note: Localized on the cell surface. May act as a transmembrane protein.

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. endocytic vesicle Source: MGI
  6. external side of plasma membrane Source: MGI
  7. integral component of membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. ruffle Source: MGI
  10. stress fiber Source: UniProtKB
  11. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10841084AngiomotinPRO_0000190668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei714 – 7141PhosphoserineBy similarity

Post-translational modificationi

Polyubiquitinated by NEDD4, NEDD4L and ITCH, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ4VCS5.
PaxDbiQ4VCS5.
PRIDEiQ4VCS5.

PTM databases

PhosphoSiteiQ4VCS5.

Expressioni

Tissue specificityi

Expressed in placenta and skeletal muscle. Found in the endothelial cells of capillaries as well as larger vessels of the placenta.1 Publication

Gene expression databases

BgeeiQ4VCS5.
CleanExiHS_AMOT.
ExpressionAtlasiQ4VCS5. baseline and differential.
GenevestigatoriQ4VCS5.

Interactioni

Subunit structurei

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with MAGI1. Isoform 1 interacts with angiostatin.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP17Q68EM74EBI-3891843,EBI-1642807
NF2P352408EBI-2511319,EBI-1014472
Nf2P466622EBI-2511319,EBI-644586From a different organism.

Protein-protein interaction databases

BioGridi127557. 76 interactions.
IntActiQ4VCS5. 61 interactions.
STRINGi9606.ENSP00000361027.

Structurei

3D structure databases

ProteinModelPortaliQ4VCS5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili429 – 689261Sequence AnalysisAdd
BLAST
Coiled coili721 – 75131Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1081 – 10844PDZ-binding

Domaini

The coiled coil domain interacts directly with the BAR domain of ARHGAP17.1 Publication
The angiostatin binding domain (871-1005) allows the binding to angiostatin.1 Publication

Sequence similaritiesi

Belongs to the angiomotin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG131728.
GeneTreeiENSGT00530000063846.
HOGENOMiHOG000233789.
HOVERGENiHBG066485.
InParanoidiQ4VCS5.
KOiK16819.
OMAiPGKVHQD.
OrthoDBiEOG7M6D6Q.
PhylomeDBiQ4VCS5.
TreeFamiTF333368.

Family and domain databases

InterProiIPR009114. Angiomotin.
IPR024646. Angiomotin_C.
[Graphical view]
PANTHERiPTHR14826. PTHR14826. 1 hit.
PfamiPF12240. Angiomotin_C. 1 hit.
[Graphical view]
PRINTSiPR01807. ANGIOMOTIN.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q4VCS5-1) [UniParc]FASTAAdd to Basket

Also known as: p130

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
MRNSEEQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNGPPFPS
60 70 80 90 100
GSGNPGPQSD VLSPQDHHQQ LVAHAARQEP QGQEIQSENL IMEKQLSPRM
110 120 130 140 150
QNNEELPTYE EAKVQSQYFR GQQHASVGAA FYVTGVTNQK MRTEGRPSVQ
160 170 180 190 200
RLNPGKMHQD EGLRDLKQGH VRSLSERLMQ MSLATSGVKA HPPVTSAPLS
210 220 230 240 250
PPQPNDLYKN PTSSSEFYKA QGPLPNQHSL KGMEHRGPPP EYPFKGMPPQ
260 270 280 290 300
SVVCKPQEPG HFYSEHRLNQ PGRTEGQLMR YQHPPEYGAA RPAQDISLPL
310 320 330 340 350
SARNSQPHSP TSSLTSGGSL PLLQSPPSTR LSPARHPLVP NQGDHSAHLP
360 370 380 390 400
RPQQHFLPNQ AHQGDHYRLS QPGLSQQQQQ QQQQHHHHHH HQQQQQQQPQ
410 420 430 440 450
QQPGEAYSAM PRAQPSSASY QPVPADPFAI VSRAQQMVEI LSDENRNLRQ
460 470 480 490 500
ELEGCYEKVA RLQKVETEIQ RVSEAYENLV KSSSKREALE KAMRNKLEGE
510 520 530 540 550
IRRMHDFNRD LRERLETANK QLAEKEYEGS EDTRKTISQL FAKNKESQRE
560 570 580 590 600
KEKLEAELAT ARSTNEDQRR HIEIRDQALS NAQAKVVKLE EELKKKQVYV
610 620 630 640 650
DKVEKMQQAL VQLQAACEKR EQLEHRLRTR LERELESLRI QQRQGNCQPT
660 670 680 690 700
NVSEYNAAAL MELLREKEER ILALEADMTK WEQKYLEENV MRHFALDAAA
710 720 730 740 750
TVAAQRDTTV ISHSPNTSYD TALEARIQKE EEEILMANKR CLDMEGRIKT
760 770 780 790 800
LHAQIIEKDA MIKVLQQRSR KEPSKTEQLS CMRPAKSLMS ISNAGSGLLS
810 820 830 840 850
HSSTLTGSPI MEEKRDDKSW KGSLGILLGG DYRAEYVPST PSPVPPSTPL
860 870 880 890 900
LSAHSKTGSR DCSTQTERGT ESNKTAAVAP ISVPAPVAAA ATAAAITATA
910 920 930 940 950
ATITTTMVAA APVAVAAAAA PAAAAAPSPA TAAATAAAVS PAAAGQIPAA
960 970 980 990 1000
ASVASAAAVA PSAAAAAAVQ VAPAAPAPVP APALVPVPAP AAAQASAPAQ
1010 1020 1030 1040 1050
TQAPTSAPAV APTPAPTPTP AVAQAEVPAS PATGPGPHRL SIPSLTCNPD
1060 1070 1080
KTDGPVFHSN TLERKTPIQI LGQEPDAEMV EYLI
Length:1,084
Mass (Da):118,085
Last modified:July 5, 2005 - v1
Checksum:iD7E7021E9535A628
GO
Isoform 2 (identifier: Q4VCS5-2) [UniParc]FASTAAdd to Basket

Also known as: p80

The sequence of this isoform differs from the canonical sequence as follows:
     1-409: Missing.

Show »
Length:675
Mass (Da):72,540
Checksum:iEBC28B74427AD481
GO

Sequence cautioni

The sequence AAH94712.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 409409Missing in isoform 2. 2 PublicationsVSP_015709Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286598 mRNA. Translation: AAG01851.1.
AY987378 mRNA. Translation: AAY24451.1.
AB028994 mRNA. Translation: BAA83023.3.
BC094712 mRNA. Translation: AAH94712.1. Sequence problems.
CCDSiCCDS14563.1. [Q4VCS5-2]
CCDS48154.1. [Q4VCS5-1]
RefSeqiNP_001106962.1. NM_001113490.1. [Q4VCS5-1]
NP_573572.1. NM_133265.2. [Q4VCS5-2]
XP_005262144.1. XM_005262087.1. [Q4VCS5-1]
XP_005262145.1. XM_005262088.1. [Q4VCS5-1]
XP_005262146.1. XM_005262089.1. [Q4VCS5-1]
XP_005262147.1. XM_005262090.1. [Q4VCS5-2]
XP_006724686.1. XM_006724623.1. [Q4VCS5-2]
UniGeneiHs.528051.

Genome annotation databases

EnsembliENST00000304758; ENSP00000305557; ENSG00000126016. [Q4VCS5-2]
ENST00000371959; ENSP00000361027; ENSG00000126016. [Q4VCS5-1]
ENST00000524145; ENSP00000429013; ENSG00000126016. [Q4VCS5-1]
GeneIDi154796.
KEGGihsa:154796.
UCSCiuc004epr.3. human. [Q4VCS5-1]

Polymorphism databases

DMDMi74753814.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286598 mRNA. Translation: AAG01851.1 .
AY987378 mRNA. Translation: AAY24451.1 .
AB028994 mRNA. Translation: BAA83023.3 .
BC094712 mRNA. Translation: AAH94712.1 . Sequence problems.
CCDSi CCDS14563.1. [Q4VCS5-2 ]
CCDS48154.1. [Q4VCS5-1 ]
RefSeqi NP_001106962.1. NM_001113490.1. [Q4VCS5-1 ]
NP_573572.1. NM_133265.2. [Q4VCS5-2 ]
XP_005262144.1. XM_005262087.1. [Q4VCS5-1 ]
XP_005262145.1. XM_005262088.1. [Q4VCS5-1 ]
XP_005262146.1. XM_005262089.1. [Q4VCS5-1 ]
XP_005262147.1. XM_005262090.1. [Q4VCS5-2 ]
XP_006724686.1. XM_006724623.1. [Q4VCS5-2 ]
UniGenei Hs.528051.

3D structure databases

ProteinModelPortali Q4VCS5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127557. 76 interactions.
IntActi Q4VCS5. 61 interactions.
STRINGi 9606.ENSP00000361027.

PTM databases

PhosphoSitei Q4VCS5.

Polymorphism databases

DMDMi 74753814.

Proteomic databases

MaxQBi Q4VCS5.
PaxDbi Q4VCS5.
PRIDEi Q4VCS5.

Protocols and materials databases

DNASUi 154796.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304758 ; ENSP00000305557 ; ENSG00000126016 . [Q4VCS5-2 ]
ENST00000371959 ; ENSP00000361027 ; ENSG00000126016 . [Q4VCS5-1 ]
ENST00000524145 ; ENSP00000429013 ; ENSG00000126016 . [Q4VCS5-1 ]
GeneIDi 154796.
KEGGi hsa:154796.
UCSCi uc004epr.3. human. [Q4VCS5-1 ]

Organism-specific databases

CTDi 154796.
GeneCardsi GC0XM112017.
HGNCi HGNC:17810. AMOT.
MIMi 300410. gene.
neXtProti NX_Q4VCS5.
PharmGKBi PA24773.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG131728.
GeneTreei ENSGT00530000063846.
HOGENOMi HOG000233789.
HOVERGENi HBG066485.
InParanoidi Q4VCS5.
KOi K16819.
OMAi PGKVHQD.
OrthoDBi EOG7M6D6Q.
PhylomeDBi Q4VCS5.
TreeFami TF333368.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.

Miscellaneous databases

ChiTaRSi AMOT. human.
GeneWikii AMOT.
GenomeRNAii 154796.
NextBioi 87314.
PROi Q4VCS5.
SOURCEi Search...

Gene expression databases

Bgeei Q4VCS5.
CleanExi HS_AMOT.
ExpressionAtlasi Q4VCS5. baseline and differential.
Genevestigatori Q4VCS5.

Family and domain databases

InterProi IPR009114. Angiomotin.
IPR024646. Angiomotin_C.
[Graphical view ]
PANTHERi PTHR14826. PTHR14826. 1 hit.
Pfami PF12240. Angiomotin_C. 1 hit.
[Graphical view ]
PRINTSi PR01807. ANGIOMOTIN.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Angiomotin. An angiostatin binding protein that regulates endothelial cell migration and tube formation."
    Troyanovsky B., Levchenko T., Maensson G., Matvijenko O., Holmgren L.
    J. Cell Biol. 152:1247-1254(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
    Tissue: Placenta.
  2. "Angiomotin regulates endothelial cell-cell junctions and cell motility."
    Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., Holmgren L.
    J. Biol. Chem. 280:34859-34869(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TOPOLOGY, INTERACTION WITH ANGIOSTATIN AND MAGI1, SUBCELLULAR LOCATION.
  3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 (ISOFORM 1).
    Tissue: Spinal cord.
  6. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
    Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
    Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, FUNCTION, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; MPP5; INADL AND PARD3.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "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].
  9. "The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-dependent degradation."
    Wang C., An J., Zhang P., Xu C., Gao K., Wu D., Wang D., Yu H., Liu J.O., Yu L.
    Biochem. J. 444:279-289(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY NEDD4; NEDD4L AND ITCH.

Entry informationi

Entry nameiAMOT_HUMAN
AccessioniPrimary (citable) accession number: Q4VCS5
Secondary accession number(s): Q504X5, Q9HD27, Q9UPT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 98 of the entry and version 1 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

Miscellaneous

'Motus' means 'motility' in Latin.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3