Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15123

- ANGP2_HUMAN

UniProt

O15123 - ANGP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Angiopoietin-2

Gene

ANGPT2

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

Functioni

Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi429 – 4291Calcium
Metal bindingi431 – 4311Calcium
Metal bindingi433 – 4331Calcium; via carbonyl oxygen
Metal bindingi435 – 4351Calcium; via carbonyl oxygen

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. receptor binding Source: ProtInc
  3. receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. blood coagulation Source: Reactome
  3. cellular response to growth factor stimulus Source: Ensembl
  4. germ cell development Source: Ensembl
  5. glomerulus vasculature development Source: UniProtKB
  6. leukocyte migration Source: Reactome
  7. maternal process involved in female pregnancy Source: Ensembl
  8. negative regulation of angiogenesis Source: Ensembl
  9. negative regulation of blood vessel endothelial cell migration Source: UniProtKB
  10. negative regulation of cell-substrate adhesion Source: Ensembl
  11. negative regulation of positive chemotaxis Source: UniProtKB
  12. organ regeneration Source: Ensembl
  13. positive regulation of angiogenesis Source: Ensembl
  14. response to activity Source: Ensembl
  15. response to glucose Source: Ensembl
  16. response to hypoxia Source: Ensembl
  17. response to mechanical stimulus Source: Ensembl
  18. response to organic cyclic compound Source: Ensembl
  19. response to radiation Source: Ensembl
  20. signal transduction Source: ProtInc
  21. Tie signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_12621. Tie2 Signaling.
SignaLinkiO15123.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-2
Short name:
ANG-2
Gene namesi
Name:ANGPT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:485. ANGPT2.

Subcellular locationi

GO - Cellular componenti

  1. cell projection Source: Ensembl
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB
  4. nucleus Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 496478Angiopoietin-2PRO_0000009113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi284 ↔ 313
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi433 ↔ 435
Disulfide bondi437 ↔ 450

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO15123.
PRIDEiO15123.

PTM databases

PhosphoSiteiO15123.

Expressioni

Gene expression databases

BgeeiO15123.
CleanExiHS_ANGPT2.
ExpressionAtlasiO15123. baseline and differential.
GenevestigatoriO15123.

Organism-specific databases

HPAiCAB011437.
CAB017626.

Interactioni

Subunit structurei

Interacts with TEK/TIE2, competing for the same binding site as ANGPT1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TEKQ027634EBI-2912111,EBI-2257090

Protein-protein interaction databases

BioGridi106782. 7 interactions.
DIPiDIP-6048N.
IntActiO15123. 6 interactions.
MINTiMINT-8247351.
STRINGi9606.ENSP00000314897.

Structurei

Secondary structure

1
496
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi281 – 2833Combined sources
Helixi284 – 2896Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi308 – 3147Combined sources
Beta strandi322 – 33110Combined sources
Helixi339 – 3446Combined sources
Beta strandi351 – 3544Combined sources
Helixi357 – 3648Combined sources
Beta strandi369 – 3768Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi382 – 39211Combined sources
Helixi395 – 3973Combined sources
Beta strandi401 – 41010Combined sources
Beta strandi431 – 4355Combined sources
Helixi437 – 4415Combined sources
Beta strandi448 – 4503Combined sources
Beta strandi452 – 4543Combined sources
Helixi475 – 4784Combined sources
Beta strandi485 – 4939Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z3SX-ray2.35A/B281-496[»]
1Z3UX-ray2.25A/B/C/D281-496[»]
2GY7X-ray3.70A281-495[»]
4JZCX-ray1.90A279-496[»]
ProteinModelPortaliO15123.
SMRiO15123. Positions 165-495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15123.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini275 – 495221Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 24883Sequence AnalysisAdd
BLAST

Domaini

The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor.

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG298026.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiO15123.
KOiK05466.
OMAiIKAYCDM.
OrthoDBiEOG7X9G60.
PhylomeDBiO15123.
TreeFamiTF336658.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028844. Ang-2.
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:SF199. PTHR19143:SF199. 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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15123) [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

        10         20         30         40         50
MWQIVFFTLS CDLVLAAAYN NFRKSMDSIG KKQYQVQHGS CSYTFLLPEM
60 70 80 90 100
DNCRSSSSPY VSNAVQRDAP LEYDDSVQRL QVLENIMENN TQWLMKLENY
110 120 130 140 150
IQDNMKKEMV EIQQNAVQNQ TAVMIEIGTN LLNQTAEQTR KLTDVEAQVL
160 170 180 190 200
NQTTRLELQL LEHSLSTNKL EKQILDQTSE INKLQDKNSF LEKKVLAMED
210 220 230 240 250
KHIIQLQSIK EEKDQLQVLV SKQNSIIEEL EKKIVTATVN NSVLQKQQHD
260 270 280 290 300
LMETVNNLLT MMSTSNSAKD PTVAKEEQIS FRDCAEVFKS GHTTNGIYTL
310 320 330 340 350
TFPNSTEEIK AYCDMEAGGG GWTIIQRRED GSVDFQRTWK EYKVGFGNPS
360 370 380 390 400
GEYWLGNEFV SQLTNQQRYV LKIHLKDWEG NEAYSLYEHF YLSSEELNYR
410 420 430 440 450
IHLKGLTGTA GKISSISQPG NDFSTKDGDN DKCICKCSQM LTGGWWFDAC
460 470 480 490
GPSNLNGMYY PQRQNTNKFN GIKWYYWKGS GYSLKATTMM IRPADF
Length:496
Mass (Da):56,919
Last modified:January 1, 1998 - v1
Checksum:i5642A58847A7385C
GO
Isoform 3 (identifier: O15123-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-148: Missing.

Show »
Length:444
Mass (Da):50,958
Checksum:iE512409CE73987A1
GO
Isoform 2 (identifier: O15123-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: Missing.

Note: No experimental confirmation available.

Show »
Length:495
Mass (Da):56,848
Checksum:iEBFAC35ABF1F08F6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti333 – 3331V → I.
Corresponds to variant rs7813215 [ dbSNP | Ensembl ].
VAR_049069

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei97 – 14852Missing in isoform 3. 1 PublicationVSP_001540Add
BLAST
Alternative sequencei268 – 2681Missing in isoform 2. 2 PublicationsVSP_040096

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004327 mRNA. Translation: AAB63190.1.
AB009865 mRNA. Translation: BAA95590.1.
AF187858 mRNA. Translation: AAF76526.1.
AK290070 mRNA. Translation: BAF82759.1.
AC018398 Genomic DNA. No translation available.
CH471153 Genomic DNA. Translation: EAW80474.1.
BC126200 mRNA. Translation: AAI26201.1.
BC126202 mRNA. Translation: AAI26203.1.
BC143902 mRNA. Translation: AAI43903.1.
CCDSiCCDS47761.1. [O15123-2]
CCDS5958.1. [O15123-1]
RefSeqiNP_001112359.1. NM_001118887.1. [O15123-3]
NP_001112360.1. NM_001118888.1. [O15123-2]
NP_001138.1. NM_001147.2. [O15123-1]
UniGeneiHs.583870.

Genome annotation databases

EnsembliENST00000325203; ENSP00000314897; ENSG00000091879. [O15123-1]
ENST00000338312; ENSP00000343517; ENSG00000091879. [O15123-2]
GeneIDi285.
KEGGihsa:285.
UCSCiuc003wqj.4. human. [O15123-1]
uc003wqk.4. human. [O15123-3]
uc010lri.3. human. [O15123-2]

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
AF004327 mRNA. Translation: AAB63190.1 .
AB009865 mRNA. Translation: BAA95590.1 .
AF187858 mRNA. Translation: AAF76526.1 .
AK290070 mRNA. Translation: BAF82759.1 .
AC018398 Genomic DNA. No translation available.
CH471153 Genomic DNA. Translation: EAW80474.1 .
BC126200 mRNA. Translation: AAI26201.1 .
BC126202 mRNA. Translation: AAI26203.1 .
BC143902 mRNA. Translation: AAI43903.1 .
CCDSi CCDS47761.1. [O15123-2 ]
CCDS5958.1. [O15123-1 ]
RefSeqi NP_001112359.1. NM_001118887.1. [O15123-3 ]
NP_001112360.1. NM_001118888.1. [O15123-2 ]
NP_001138.1. NM_001147.2. [O15123-1 ]
UniGenei Hs.583870.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z3S X-ray 2.35 A/B 281-496 [» ]
1Z3U X-ray 2.25 A/B/C/D 281-496 [» ]
2GY7 X-ray 3.70 A 281-495 [» ]
4JZC X-ray 1.90 A 279-496 [» ]
ProteinModelPortali O15123.
SMRi O15123. Positions 165-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106782. 7 interactions.
DIPi DIP-6048N.
IntActi O15123. 6 interactions.
MINTi MINT-8247351.
STRINGi 9606.ENSP00000314897.

PTM databases

PhosphoSitei O15123.

Proteomic databases

PaxDbi O15123.
PRIDEi O15123.

Protocols and materials databases

DNASUi 285.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325203 ; ENSP00000314897 ; ENSG00000091879 . [O15123-1 ]
ENST00000338312 ; ENSP00000343517 ; ENSG00000091879 . [O15123-2 ]
GeneIDi 285.
KEGGi hsa:285.
UCSCi uc003wqj.4. human. [O15123-1 ]
uc003wqk.4. human. [O15123-3 ]
uc010lri.3. human. [O15123-2 ]

Organism-specific databases

CTDi 285.
GeneCardsi GC08M006347.
HGNCi HGNC:485. ANGPT2.
HPAi CAB011437.
CAB017626.
MIMi 601922. gene.
neXtProti NX_O15123.
PharmGKBi PA24792.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298026.
GeneTreei ENSGT00760000118809.
HOGENOMi HOG000037128.
HOVERGENi HBG001644.
InParanoidi O15123.
KOi K05466.
OMAi IKAYCDM.
OrthoDBi EOG7X9G60.
PhylomeDBi O15123.
TreeFami TF336658.

Enzyme and pathway databases

Reactomei REACT_12621. Tie2 Signaling.
SignaLinki O15123.

Miscellaneous databases

EvolutionaryTracei O15123.
GeneWikii ANGPT2.
GenomeRNAii 285.
NextBioi 1151.
PROi O15123.
SOURCEi Search...

Gene expression databases

Bgeei O15123.
CleanExi HS_ANGPT2.
ExpressionAtlasi O15123. baseline and differential.
Genevestigatori O15123.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR028844. Ang-2.
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:SF199. PTHR19143:SF199. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TEK/TIE2, FUNCTION.
    Tissue: Lung.
  2. "Biologic significance of angiopoietin-2 expression in human hepatocellular carcinoma."
    Tanaka S., Mori M., Sakamoto Y., Makuuchi M., Sugimachi K., Wands J.R.
    J. Clin. Invest. 103:341-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Characterization and expression of a novel alternatively spliced human angiopoietin-2."
    Kim I., Kim J.-H., Ryu Y.S., Jung S.H., Nah J.J., Koh G.Y.
    J. Biol. Chem. 275:18550-18556(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Umbilical vein endothelial cell.
  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 1).
    Tissue: Substantia nigra.
  5. "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].
  6. 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] (ISOFORMS 1 AND 2).
    Tissue: Colon.
  8. "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/TIE2.
  9. "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.
  10. "Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human endothelial cells."
    Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., Jurasz P., Stewart D.J.
    Angiogenesis 12:25-33(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Angiopoietin 2 is a partial agonist/antagonist of Tie2 signaling in the endothelium."
    Yuan H.T., Khankin E.V., Karumanchi S.A., Parikh S.M.
    Mol. Cell. Biol. 29:2011-2022(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TEK/TIE2.
  12. "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.
  13. "Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition."
    Barton W.A., Tzvetkova D., Nikolov D.B.
    Structure 13:825-832(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 281-496, DISULFIDE BONDS, CALCIUM-BINDING SITES.
  14. "Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex."
    Barton W.A., Tzvetkova-Robev D., Miranda E.P., Kolev M.V., Rajashankar K.R., Himanen J.P., Nikolov D.B.
    Nat. Struct. Mol. Biol. 13:524-532(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 281-495 IN COMPLEX WITH TEK, DISULFIDE BONDS, CALCIUM-BINDING SITES.

Entry informationi

Entry nameiANGP2_HUMAN
AccessioniPrimary (citable) accession number: O15123
Secondary accession number(s): A0AV38
, A8K205, B7ZLM7, Q9NRR7, Q9P2Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 130 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

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