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Protein

Angiopoietin-2

Gene

Angpt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • blood vessel morphogenesis Source: MGI
  • blood vessel remodeling Source: DFLAT
  • cellular response to growth factor stimulus Source: Ensembl
  • endoderm development Source: MGI
  • germ cell development Source: Ensembl
  • glomerulus vasculature development Source: Ensembl
  • hemopoiesis Source: DFLAT
  • maternal process involved in female pregnancy Source: Ensembl
  • negative regulation of angiogenesis Source: MGI
  • negative regulation of blood vessel endothelial cell migration Source: MGI
  • negative regulation of cell-substrate adhesion Source: MGI
  • negative regulation of positive chemotaxis Source: MGI
  • organ regeneration Source: Ensembl
  • positive regulation of angiogenesis Source: Ensembl
  • regulation of angiogenesis Source: DFLAT
  • response to activity Source: Ensembl
  • response to glucose Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to mechanical stimulus Source: Ensembl
  • response to organic cyclic compound Source: Ensembl
  • response to radiation Source: Ensembl
  • Tie signaling pathway Source: DFLAT
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_341964. Tie2 Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-2
Short name:
ANG-2
Gene namesi
Name:Angpt2
Synonyms:Agpt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1202890. Angpt2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 496478Angiopoietin-2PRO_0000009114Add
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 ↔ 313PROSITE-ProRule annotation
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi433 ↔ 435PROSITE-ProRule annotation
Disulfide bondi437 ↔ 450PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO35608.

PTM databases

PhosphoSiteiO35608.

Expressioni

Tissue specificityi

Expressed only at sites of vascular remodeling.

Gene expression databases

BgeeiO35608.
CleanExiMM_ANGPT2.
ExpressionAtlasiO35608. baseline and differential.
GenevisibleiO35608. MM.

Interactioni

Subunit structurei

Interacts with TEK/TIE2, competing for the same binding site as ANGPT1.By similarity

Protein-protein interaction databases

DIPiDIP-6049N.
IntActiO35608. 1 interaction.
STRINGi10090.ENSMUSP00000033846.

Structurei

3D structure databases

ProteinModelPortaliO35608.
SMRiO35608. Positions 148-495.
ModBaseiSearch...
MobiDBiSearch...

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 coili159 – 25698Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG298026.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiO35608.
KOiK05466.
OMAiTWKEYKV.
OrthoDBiEOG7X9G60.
PhylomeDBiO35608.
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]

Sequencei

Sequence statusi: Complete.

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

O35608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWQIIFLTFG WDLVLASAYS NFRKSVDSTG RRQYQVQNGP CSYTFLLPET
60 70 80 90 100
DSCRSSSSPY MSNAVQRDAP LDYDDSVQRL QVLENILENN TQWLMKLENY
110 120 130 140 150
IQDNMKKEMV EIQQNVVQNQ TAVMIEIGTS LLNQTAAQTR KLTDVEAQVL
160 170 180 190 200
NQTTRLELQL LQHSISTNKL EKQILDQTSE INKLQNKNSF LEQKVLDMEG
210 220 230 240 250
KHSEQLQSMK EQKDELQVLV SKQSSVIDEL EKKLVTATVN NSLLQKQQHD
260 270 280 290 300
LMETVNSLLT MMSSPNSKSS VAIRKEEQTT FRDCAEIFKS GLTTSGIYTL
310 320 330 340 350
TFPNSTEEIK AYCDMDVGGG GWTVIQHRED GSVDFQRTWK EYKEGFGSPL
360 370 380 390 400
GEYWLGNEFV SQLTGQHRYV LKIQLKDWEG NEAHSLYDHF YLAGEESNYR
410 420 430 440 450
IHLTGLTGTA GKISSISQPG SDFSTKDSDN DKCICKCSQM LSGGWWFDAC
460 470 480 490
GPSNLNGQYY PQKQNTNKFN GIKWYYWKGS GYSLKATTMM IRPADF
Length:496
Mass (Da):56,576
Last modified:April 26, 2004 - v2
Checksum:iE7563B498A0EF331
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481S → N in AAB63189 (PubMed:9204896).Curated
Sequence conflicti411 – 4111G → A in AAB63189 (PubMed:9204896).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004326 mRNA. Translation: AAB63189.1.
AK019860 mRNA. Translation: BAB31887.1.
AK048622 mRNA. Translation: BAC33396.1.
AK156132 mRNA. Translation: BAE33599.1.
BC027216 mRNA. Translation: AAH27216.1.
CCDSiCCDS22125.1.
RefSeqiNP_031452.2. NM_007426.4.
UniGeneiMm.439874.

Genome annotation databases

EnsembliENSMUST00000033846; ENSMUSP00000033846; ENSMUSG00000031465.
GeneIDi11601.
KEGGimmu:11601.
UCSCiuc009kzu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004326 mRNA. Translation: AAB63189.1.
AK019860 mRNA. Translation: BAB31887.1.
AK048622 mRNA. Translation: BAC33396.1.
AK156132 mRNA. Translation: BAE33599.1.
BC027216 mRNA. Translation: AAH27216.1.
CCDSiCCDS22125.1.
RefSeqiNP_031452.2. NM_007426.4.
UniGeneiMm.439874.

3D structure databases

ProteinModelPortaliO35608.
SMRiO35608. Positions 148-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6049N.
IntActiO35608. 1 interaction.
STRINGi10090.ENSMUSP00000033846.

PTM databases

PhosphoSiteiO35608.

Proteomic databases

PRIDEiO35608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033846; ENSMUSP00000033846; ENSMUSG00000031465.
GeneIDi11601.
KEGGimmu:11601.
UCSCiuc009kzu.2. mouse.

Organism-specific databases

CTDi285.
MGIiMGI:1202890. Angpt2.

Phylogenomic databases

eggNOGiNOG298026.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiO35608.
KOiK05466.
OMAiTWKEYKV.
OrthoDBiEOG7X9G60.
PhylomeDBiO35608.
TreeFamiTF336658.

Enzyme and pathway databases

ReactomeiREACT_341964. Tie2 Signaling.

Miscellaneous databases

NextBioi279120.
PROiO35608.
SOURCEiSearch...

Gene expression databases

BgeeiO35608.
CleanExiMM_ANGPT2.
ExpressionAtlasiO35608. baseline and differential.
GenevisibleiO35608. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head, Ovary, Spleen and Uterus.
  3. "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].

Entry informationi

Entry nameiANGP2_MOUSE
AccessioniPrimary (citable) accession number: O35608
Secondary accession number(s): Q3U1A1, Q9D2D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 26, 2004
Last modified: July 22, 2015
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

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

External Data

Dasty 3

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 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.