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Q15389

- ANGP1_HUMAN

UniProt

Q15389 - ANGP1_HUMAN

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Protein
Angiopoietin-1
Gene
ANGPT1, KIAA0003
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme.4 Publications

GO - Molecular functioni

  1. receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  1. Tie signaling pathway Source: UniProtKB
  2. activation of transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cell differentiation Source: UniProtKB-KW
  5. cell-substrate adhesion Source: Ensembl
  6. glomerulus vasculature development Source: UniProtKB
  7. hemopoiesis Source: Ensembl
  8. heparin biosynthetic process Source: UniProtKB
  9. in utero embryonic development Source: Ensembl
  10. leukocyte migration Source: Reactome
  11. negative regulation of apoptotic process Source: UniProtKB
  12. negative regulation of cell adhesion Source: UniProtKB
  13. negative regulation of endothelial cell apoptotic process Source: UniProtKB
  14. negative regulation of neuron apoptotic process Source: Ensembl
  15. negative regulation of vascular permeability Source: UniProtKB
  16. positive chemotaxis Source: UniProtKB
  17. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  18. positive regulation of blood vessel endothelial cell migration Source: UniProtKB
  19. positive regulation of cell adhesion Source: Ensembl
  20. positive regulation of endothelial cell migration Source: UniProtKB
  21. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  22. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  23. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  24. positive regulation of protein kinase B signaling Source: UniProtKB
  25. positive regulation of protein ubiquitination Source: UniProtKB
  26. positive regulation of receptor internalization Source: UniProtKB
  27. protein localization to cell surface Source: UniProtKB
  28. regulation of satellite cell proliferation Source: UniProtKB
  29. sprouting angiogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiREACT_12621. Tie2 Signaling.
SignaLinkiQ15389.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-1
Short name:
ANG-1
Gene namesi
Name:ANGPT1
Synonyms:KIAA0003
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:484. ANGPT1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane raft Source: UniProtKB
  5. microvillus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24791.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Chaini16 – 498483Angiopoietin-1
PRO_0000009110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi122 – 1221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi154 – 1541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi243 – 2431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi286 ↔ 315 By similarity
Glycosylationi295 – 2951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi439 ↔ 452 By similarity

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ15389.
PRIDEiQ15389.

PTM databases

PhosphoSiteiQ15389.

Expressioni

Gene expression databases

ArrayExpressiQ15389.
BgeeiQ15389.
CleanExiHS_ANGPT1.
GenevestigatoriQ15389.

Organism-specific databases

HPAiCAB017815.
HPA018793.
HPA018816.

Interactioni

Subunit structurei

Homooligomer. Interacts with TEK/TIE2.3 Publications

Protein-protein interaction databases

BioGridi106781. 2 interactions.
DIPiDIP-6046N.
IntActiQ15389. 1 interaction.
STRINGi9606.ENSP00000297450.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi286 – 2916
Beta strandi298 – 3025
Beta strandi311 – 3166
Helixi319 – 3213
Beta strandi324 – 33310
Helixi341 – 3466
Beta strandi353 – 3564
Helixi359 – 3668
Beta strandi371 – 3788
Beta strandi384 – 39411
Helixi397 – 3993
Beta strandi403 – 41210
Beta strandi433 – 4375
Helixi439 – 4435
Beta strandi450 – 4523
Beta strandi454 – 4563
Turni463 – 4675
Beta strandi473 – 4764
Turni477 – 4793
Beta strandi487 – 4959

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EPUX-ray2.10A/B282-497[»]
4JYOX-ray2.50X280-498[»]
4K0VX-ray4.51B280-498[»]
ProteinModelPortaliQ15389.
SMRiQ15389. Positions 172-497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 497221Fibrinogen C-terminal
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili81 – 11939 Reviewed prediction
Add
BLAST
Coiled coili153 – 261109 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG310490.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiQ15389.
KOiK05465.
OMAiTSQRQYS.
OrthoDBiEOG7X9G60.
PhylomeDBiQ15389.
TreeFamiTF336658.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028843. Ang-1.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PANTHERiPTHR19143:SF156. PTHR19143:SF156. 1 hit.
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15389-1) [UniParc]FASTAAdd to Basket

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

MTVFLSFAFL AAILTHIGCS NQRRSPENSG RRYNRIQHGQ CAYTFILPEH    50
DGNCRESTTD QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL 100
ENYIVENMKS EMAQIQQNAV QNHTATMLEI GTSLLSQTAE QTRKLTDVET 150
QVLNQTSRLE IQLLENSLST YKLEKQLLQQ TNEILKIHEK NSLLEHKILE 200
MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELEKQLNRA TTNNSVLQKQ 250
QLELMDTVHN LVNLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY 300
TIYINNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN 350
PSGEYWLGNE FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN 400
YRLYLKGHTG TAGKQSSLIL HGADFSTKDA DNDNCMCKCA LMLTGGWWFD 450
ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK GPSYSLRSTT MMIRPLDF 498
Length:498
Mass (Da):57,513
Last modified:January 1, 1998 - v2
Checksum:i5D5FA63AEF6BE920
GO
Isoform 2 (identifier: Q15389-2) [UniParc]FASTAAdd to Basket

Also known as: Gly-269 del

The sequence of this isoform differs from the canonical sequence as follows:
     269-269: Missing.

Show »
Length:497
Mass (Da):57,456
Checksum:i3055148F097AC6AF
GO

Sequence cautioni

The sequence BAA02793.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471L → P.
Corresponds to variant rs73701083 [ dbSNP | Ensembl ].
VAR_069165

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei269 – 2691Missing in isoform 2.
VSP_046324

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83508 mRNA. Translation: AAB50557.1.
AB084454 mRNA. Translation: BAB91325.1.
AY121504 mRNA. Translation: AAM81745.1.
AY124380 mRNA. Translation: AAM92271.1.
D13628 mRNA. Translation: BAA02793.2. Different initiation.
BX648814 mRNA. Translation: CAI45984.1.
AC091010 Genomic DNA. No translation available.
AP000428 Genomic DNA. No translation available.
AP003480 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91909.1.
BC152411 mRNA. Translation: AAI52412.1.
BC152419 mRNA. Translation: AAI52420.1.
CCDSiCCDS56551.1. [Q15389-2]
CCDS6306.1. [Q15389-1]
RefSeqiNP_001137.2. NM_001146.3. [Q15389-1]
NP_001186788.1. NM_001199859.1. [Q15389-2]
UniGeneiHs.369675.

Genome annotation databases

EnsembliENST00000297450; ENSP00000297450; ENSG00000154188. [Q15389-2]
ENST00000517746; ENSP00000428340; ENSG00000154188. [Q15389-1]
GeneIDi284.
KEGGihsa:284.
UCSCiuc003ymn.3. human. [Q15389-1]

Polymorphism databases

DMDMi12229574.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Angiopoietin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83508 mRNA. Translation: AAB50557.1 .
AB084454 mRNA. Translation: BAB91325.1 .
AY121504 mRNA. Translation: AAM81745.1 .
AY124380 mRNA. Translation: AAM92271.1 .
D13628 mRNA. Translation: BAA02793.2 . Different initiation.
BX648814 mRNA. Translation: CAI45984.1 .
AC091010 Genomic DNA. No translation available.
AP000428 Genomic DNA. No translation available.
AP003480 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91909.1 .
BC152411 mRNA. Translation: AAI52412.1 .
BC152419 mRNA. Translation: AAI52420.1 .
CCDSi CCDS56551.1. [Q15389-2 ]
CCDS6306.1. [Q15389-1 ]
RefSeqi NP_001137.2. NM_001146.3. [Q15389-1 ]
NP_001186788.1. NM_001199859.1. [Q15389-2 ]
UniGenei Hs.369675.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EPU X-ray 2.10 A/B 282-497 [» ]
4JYO X-ray 2.50 X 280-498 [» ]
4K0V X-ray 4.51 B 280-498 [» ]
ProteinModelPortali Q15389.
SMRi Q15389. Positions 172-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106781. 2 interactions.
DIPi DIP-6046N.
IntActi Q15389. 1 interaction.
STRINGi 9606.ENSP00000297450.

PTM databases

PhosphoSitei Q15389.

Polymorphism databases

DMDMi 12229574.

Proteomic databases

PaxDbi Q15389.
PRIDEi Q15389.

Protocols and materials databases

DNASUi 284.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297450 ; ENSP00000297450 ; ENSG00000154188 . [Q15389-2 ]
ENST00000517746 ; ENSP00000428340 ; ENSG00000154188 . [Q15389-1 ]
GeneIDi 284.
KEGGi hsa:284.
UCSCi uc003ymn.3. human. [Q15389-1 ]

Organism-specific databases

CTDi 284.
GeneCardsi GC08M108330.
HGNCi HGNC:484. ANGPT1.
HPAi CAB017815.
HPA018793.
HPA018816.
MIMi 601667. gene.
neXtProti NX_Q15389.
PharmGKBi PA24791.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310490.
HOGENOMi HOG000037128.
HOVERGENi HBG001644.
InParanoidi Q15389.
KOi K05465.
OMAi TSQRQYS.
OrthoDBi EOG7X9G60.
PhylomeDBi Q15389.
TreeFami TF336658.

Enzyme and pathway databases

Reactomei REACT_12621. Tie2 Signaling.
SignaLinki Q15389.

Miscellaneous databases

ChiTaRSi ANGPT1. human.
GeneWikii Angiopoietin_1.
GenomeRNAii 284.
NextBioi 1147.
PROi Q15389.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15389.
Bgeei Q15389.
CleanExi HS_ANGPT1.
Genevestigatori Q15389.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR028843. Ang-1.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view ]
PANTHERi PTHR19143:SF156. PTHR19143:SF156. 1 hit.
Pfami PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning."
    Davis S., Aldrich T.H., Jones P.F., Acheson A., Compton D.L., Jain V., Ryan T.E., Bruno J., Radziejewski C., Maisonpierre P.C., Yancopoulos G.D.
    Cell 87:1161-1169(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal lung.
  2. "Human angiopoietin-1 mRNA variant form."
    Nakatsukasa M., Komai K., Shiozawa S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Human angiopoietin-1 mRNA variant forms."
    Shan Z.X., Yu X.Y., Lin Q.Y., Fu Y.H., Tan H.H., Zheng M., Lin S.G.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Small intestine.
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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.
  10. Cited for: FUNCTION, INTERACTION WITH TEK.
  11. "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the epidermal growth factor-like repeats."
    Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U., Martiny-Baron G., Marme D., Augustin H.G.
    J. Biol. Chem. 278:1721-1727(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEK.
  12. "Biological characterization of angiopoietin-3 and angiopoietin-4."
    Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y., Kim J.H., Oh J.L., Lee G.M., Koh G.Y.
    FASEB J. 18:1200-1208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION AND ACTIVATION OF AKT1, INTERACTION WITH TEK/TIE2.
  13. "Differential function of Tie2 at cell-cell contacts and cell-substratum contacts regulated by angiopoietin-1."
    Fukuhara S., Sako K., Minami T., Noda K., Kim H.Z., Kodama T., Shibuya M., Takakura N., Koh G.Y., Mochizuki N.
    Nat. Cell Biol. 10:513-526(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION AND CELL SPREADING.
  14. "Angiopoietins assemble distinct Tie2 signalling complexes in endothelial cell-cell and cell-matrix contacts."
    Saharinen P., Eklund L., Miettinen J., Wirkkala R., Anisimov A., Winderlich M., Nottebaum A., Vestweber D., Deutsch U., Koh G.Y., Olsen B.R., Alitalo K.
    Nat. Cell Biol. 10:527-537(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION.
  15. "Control of vascular morphogenesis and homeostasis through the angiopoietin-Tie system."
    Augustin H.G., Koh G.Y., Thurston G., Alitalo K.
    Nat. Rev. Mol. Cell Biol. 10:165-177(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Angiopoietin-1/Tie2 receptor signaling in vascular quiescence and angiogenesis."
    Fukuhara S., Sako K., Noda K., Zhang J., Minami M., Mochizuki N.
    Histol. Histopathol. 25:387-396(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Targeting the ANGPT-TIE2 pathway in malignancy."
    Huang H., Bhat A., Woodnutt G., Lappe R.
    Nat. Rev. Cancer 10:575-585(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiANGP1_HUMAN
AccessioniPrimary (citable) accession number: Q15389
Secondary accession number(s): Q5HYA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 132 of the entry and version 2 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

It may have a potential therapeutic utility since it can be used for specifically targeting tumor vasculature or for promoting angiogenic processes in certain organs such as an ischemic heart.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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