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Protein

Angiopoietin-1

Gene

ANGPT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

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 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:484. ANGPT1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • membrane raft Source: UniProtKB
  • microvillus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24791.

Polymorphism and mutation databases

BioMutaiANGPT1.
DMDMi12229574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 498483Angiopoietin-1PRO_0000009110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi286 ↔ 315PROSITE-ProRule annotation
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi439 ↔ 452PROSITE-ProRule annotation

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ15389.
PRIDEiQ15389.

PTM databases

PhosphoSiteiQ15389.

Expressioni

Gene expression databases

BgeeiQ15389.
CleanExiHS_ANGPT1.
ExpressionAtlasiQ15389. baseline and differential.
GenevisibleiQ15389. HS.

Organism-specific databases

HPAiCAB017815.
HPA018793.
HPA018816.

Interactioni

Subunit structurei

Homooligomer. Interacts with TEK/TIE2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK8IP2Q133873EBI-10692491,EBI-722813

Protein-protein interaction databases

BioGridi106781. 2 interactions.
DIPiDIP-6046N.
IntActiQ15389. 2 interactions.
STRINGi9606.ENSP00000428340.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi286 – 2916Combined sources
Beta strandi298 – 3025Combined sources
Beta strandi311 – 3166Combined sources
Helixi319 – 3213Combined sources
Beta strandi324 – 33310Combined sources
Helixi341 – 3466Combined sources
Beta strandi353 – 3564Combined sources
Helixi359 – 3668Combined sources
Beta strandi371 – 3788Combined sources
Beta strandi384 – 39411Combined sources
Helixi397 – 3993Combined sources
Beta strandi403 – 41210Combined sources
Beta strandi433 – 4375Combined sources
Helixi439 – 4435Combined sources
Beta strandi450 – 4523Combined sources
Beta strandi454 – 4563Combined sources
Turni463 – 4675Combined sources
Beta strandi473 – 4764Combined sources
Turni477 – 4793Combined sources
Beta strandi487 – 4959Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 497221Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili81 – 11939Sequence AnalysisAdd
BLAST
Coiled coili153 – 261109Sequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG310490.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiQ15389.
KOiK05465.
OMAiTQWLQKI.
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. AlignAdd to basket

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

        10         20         30         40         50
MTVFLSFAFL AAILTHIGCS NQRRSPENSG RRYNRIQHGQ CAYTFILPEH
60 70 80 90 100
DGNCRESTTD QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL
110 120 130 140 150
ENYIVENMKS EMAQIQQNAV QNHTATMLEI GTSLLSQTAE QTRKLTDVET
160 170 180 190 200
QVLNQTSRLE IQLLENSLST YKLEKQLLQQ TNEILKIHEK NSLLEHKILE
210 220 230 240 250
MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELEKQLNRA TTNNSVLQKQ
260 270 280 290 300
QLELMDTVHN LVNLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY
310 320 330 340 350
TIYINNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN
360 370 380 390 400
PSGEYWLGNE FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN
410 420 430 440 450
YRLYLKGHTG TAGKQSSLIL HGADFSTKDA DNDNCMCKCA LMLTGGWWFD
460 470 480 490
ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK GPSYSLRSTT MMIRPLDF
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. Curated

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. 3 PublicationsVSP_046324

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Angiopoietin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106781. 2 interactions.
DIPiDIP-6046N.
IntActiQ15389. 2 interactions.
STRINGi9606.ENSP00000428340.

Chemistry

ChEMBLiCHEMBL3217395.

PTM databases

PhosphoSiteiQ15389.

Polymorphism and mutation databases

BioMutaiANGPT1.
DMDMi12229574.

Proteomic databases

PaxDbiQ15389.
PRIDEiQ15389.

Protocols and materials databases

DNASUi284.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi284.
GeneCardsiGC08M108330.
HGNCiHGNC:484. ANGPT1.
HPAiCAB017815.
HPA018793.
HPA018816.
MIMi601667. gene.
neXtProtiNX_Q15389.
PharmGKBiPA24791.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310490.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037128.
HOVERGENiHBG001644.
InParanoidiQ15389.
KOiK05465.
OMAiTQWLQKI.
OrthoDBiEOG7X9G60.
PhylomeDBiQ15389.
TreeFamiTF336658.

Enzyme and pathway databases

ReactomeiREACT_12621. Tie2 Signaling.
SignaLinkiQ15389.

Miscellaneous databases

ChiTaRSiANGPT1. human.
GeneWikiiAngiopoietin_1.
GenomeRNAii284.
NextBioi1147.
PROiQ15389.
SOURCEiSearch...

Gene expression databases

BgeeiQ15389.
CleanExiHS_ANGPT1.
ExpressionAtlasiQ15389. baseline and differential.
GenevisibleiQ15389. HS.

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]
ProtoNetiSearch...

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.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 141 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

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.