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Protein

Angiopoietin-related protein 4

Gene

ANGPTL4

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

Functioni

Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-related protein 4
Alternative name(s):
Angiopoietin-like protein 4
Hepatic fibrinogen/angiopoietin-related protein
Short name:
HFARP
Gene namesi
Name:ANGPTL4
Synonyms:ARP4, HFARP, PGAR
ORF Names:PP1158, PSEC0166, UNQ171/PRO197
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:16039. ANGPTL4.

Subcellular locationi

  • Secreted 1 Publication
  • Secretedextracellular spaceextracellular matrix By similarity

  • Note: The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (By similarity).By similarity

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: MGI
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

MIMi615881. phenotype.
PharmGKBiPA24797.

Polymorphism and mutation databases

BioMutaiANGPTL4.
DMDMi25008123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 406381Angiopoietin-related protein 4PRO_0000009124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi188 ↔ 216PROSITE-ProRule annotation
Disulfide bondi341 ↔ 354PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9BY76.
PaxDbiQ9BY76.
PRIDEiQ9BY76.

PTM databases

PhosphoSiteiQ9BY76.

Expressioni

Tissue specificityi

Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney.2 Publications

Gene expression databases

BgeeiQ9BY76.
CleanExiHS_ANGPTL4.
ExpressionAtlasiQ9BY76. baseline and differential.
GenevisibleiQ9BY76. HS.

Organism-specific databases

HPAiCAB033770.

Interactioni

Subunit structurei

Homooligomer. The homooligomer undergoes proteolytic processing to release its carboxyl fibrinogen-like domain, which circulates as a monomer. The homooligomer unprocessed form is able to interact with the extracellular matrix (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1P055562EBI-2968146,EBI-703066
ITGB5P180843EBI-2968146,EBI-1223434

Protein-protein interaction databases

BioGridi119316. 4 interactions.
IntActiQ9BY76. 13 interactions.
STRINGi9606.ENSP00000301455.

Structurei

3D structure databases

ProteinModelPortaliQ9BY76.
SMRiQ9BY76. Positions 137-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini179 – 401223Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili100 – 14344Sequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG281759.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ9BY76.
KOiK08767.
OMAiVDFNRPW.
PhylomeDBiQ9BY76.
TreeFamiTF329953.

Family and domain databases

Gene3Di3.90.215.10. 2 hits.
4.10.530.10. 1 hit.
InterProiIPR028793. ANGPTL4.
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:SF16. PTHR19143:SF16. 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. AlignAdd to basket

Isoform 1 (identifier: Q9BY76-1) [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
MSGAPTAGAA LMLCAATAVL LSAQGGPVQS KSPRFASWDE MNVLAHGLLQ
60 70 80 90 100
LGQGLREHAE RTRSQLSALE RRLSACGSAC QGTEGSTDLP LAPESRVDPE
110 120 130 140 150
VLHSLQTQLK AQNSRIQQLF HKVAQQQRHL EKQHLRIQHL QSQFGLLDHK
160 170 180 190 200
HLDHEVAKPA RRKRLPEMAQ PVDPAHNVSR LHRLPRDCQE LFQVGERQSG
210 220 230 240 250
LFEIQPQGSP PFLVNCKMTS DGGWTVIQRR HDGSVDFNRP WEAYKAGFGD
260 270 280 290 300
PHGEFWLGLE KVHSITGDRN SRLAVQLRDW DGNAELLQFS VHLGGEDTAY
310 320 330 340 350
SLQLTAPVAG QLGATTVPPS GLSVPFSTWD QDHDLRRDKN CAKSLSGGWW
360 370 380 390 400
FGTCSHSNLN GQYFRSIPQQ RQKLKKGIFW KTWRGRYYPL QATTMLIQPM

AAEAAS
Length:406
Mass (Da):45,214
Last modified:November 8, 2002 - v2
Checksum:i219E56FEB3F602AF
GO
Isoform 2 (identifier: Q9BY76-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-221: RLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSD → H

Note: Gene prediction based on EST data.
Show »
Length:368
Mass (Da):40,917
Checksum:i7D61B5306C3AF298
GO
Isoform 3 (identifier: Q9BY76-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-167: Missing.

Note: No experimental confirmation available.
Show »
Length:239
Mass (Da):26,853
Checksum:iFBB362F2DBDB6900
GO

Sequence cautioni

The sequence AAQ88642.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 7117LREHA…SALER → CANTGAHPQSAERAGA in AAD41088 (Ref. 5) CuratedAdd
BLAST
Sequence conflicti60 – 601E → G in BAB40692 (PubMed:14583458).Curated
Sequence conflicti175 – 1751A → P in AAF62868 (PubMed:10698685).Curated
Sequence conflicti237 – 2371F → S in BAG64351 (PubMed:14702039).Curated
Sequence conflicti251 – 2511P → S in BAD96209 (Ref. 8) Curated
Sequence conflicti270 – 2701N → D (PubMed:14702039).Curated
Sequence conflicti270 – 2701N → D (Ref. 8) Curated
Sequence conflicti277 – 2771L → R in BAD96244 (Ref. 8) Curated
Sequence conflicti304 – 3041L → F in AAF62868 (PubMed:10698685).Curated
Sequence conflicti363 – 3631Y → H in BAD96209 (Ref. 8) Curated
Sequence conflicti389 – 3891P → S in AAF62868 (PubMed:10698685).Curated

Polymorphismi

Genetic variations in ANGPTL4 are associated with low plasma triglyceride levels and define the plasma triglyceride level quantitative trait locus (TGQTL) [MIMi:615881].1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51P → L.1 Publication
VAR_032642
Natural varianti40 – 401E → K Associated with lower plasma levels of triglyceride and higher levels of HDL cholesterol. 1 Publication
Corresponds to variant rs116843064 [ dbSNP | Ensembl ].
VAR_032643
Natural varianti41 – 411M → I.1 Publication
Corresponds to variant rs186754194 [ dbSNP | Ensembl ].
VAR_032644
Natural varianti67 – 671S → R.1 Publication
VAR_032645
Natural varianti72 – 721R → L.1 Publication
Corresponds to variant rs141831018 [ dbSNP | Ensembl ].
VAR_032646
Natural varianti77 – 771G → R.1 Publication
VAR_032647
Natural varianti167 – 1671E → K.1 Publication
Corresponds to variant rs140640857 [ dbSNP | Ensembl ].
VAR_032648
Natural varianti174 – 1741P → S.1 Publication
VAR_032649
Natural varianti190 – 1901E → Q.1 Publication
Corresponds to variant rs77938377 [ dbSNP | Ensembl ].
VAR_032650
Natural varianti196 – 1961E → K.1 Publication
VAR_032651
Natural varianti230 – 2301R → C.1 Publication
Corresponds to variant rs201026877 [ dbSNP | Ensembl ].
VAR_032652
Natural varianti233 – 2331G → R.1 Publication
VAR_032653
Natural varianti237 – 2371F → V.1 Publication
VAR_032654
Natural varianti251 – 2511P → T.1 Publication
VAR_032655
Natural varianti266 – 2661T → M.3 Publications
Corresponds to variant rs1044250 [ dbSNP | Ensembl ].
VAR_020428
Natural varianti278 – 2781R → Q.1 Publication
Corresponds to variant rs35061979 [ dbSNP | Ensembl ].
VAR_032656
Natural varianti291 – 2911V → M.1 Publication
VAR_032657
Natural varianti293 – 2931L → M.1 Publication
VAR_032658
Natural varianti296 – 2961E → V.1 Publication
VAR_032659
Natural varianti307 – 3071P → S.1 Publication
VAR_032660
Natural varianti308 – 3081V → M.1 Publication
Corresponds to variant rs139998264 [ dbSNP | Ensembl ].
VAR_032661
Natural varianti336 – 3361R → C.1 Publication
Corresponds to variant rs140744493 [ dbSNP | Ensembl ].
VAR_032662
Natural varianti338 – 3381D → E.1 Publication
VAR_032663
Natural varianti349 – 3491W → C.1 Publication
VAR_032664
Natural varianti361 – 3611G → R.1 Publication
VAR_032665
Natural varianti361 – 3611G → S.1 Publication
VAR_032666
Natural varianti371 – 3711R → Q.1 Publication
VAR_032667
Natural varianti384 – 3841R → W.1 Publication
VAR_032668

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 167167Missing in isoform 3. 1 PublicationVSP_055092Add
BLAST
Alternative sequencei183 – 22139RLPRD…KMTSD → H in isoform 2. CuratedVSP_047045Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169312 mRNA. Translation: AAF62868.1.
AF202636 mRNA. Translation: AAG22490.1.
AB056477 mRNA. Translation: BAB40692.1.
AF153606 mRNA. Translation: AAD41088.1.
AY358275 mRNA. Translation: AAQ88642.1. Different initiation.
AK303269 mRNA. Translation: BAG64351.1.
AK222489 mRNA. Translation: BAD96209.1.
AK222524 mRNA. Translation: BAD96244.1.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68930.1.
CH471139 Genomic DNA. Translation: EAW68931.1.
BC023647 mRNA. Translation: AAH23647.1.
CCDSiCCDS12200.1. [Q9BY76-1]
CCDS42493.1. [Q9BY76-2]
RefSeqiNP_001034756.1. NM_001039667.2. [Q9BY76-2]
NP_647475.1. NM_139314.2. [Q9BY76-1]
UniGeneiHs.9613.

Genome annotation databases

EnsembliENST00000301455; ENSP00000301455; ENSG00000167772.
ENST00000393962; ENSP00000377534; ENSG00000167772. [Q9BY76-2]
ENST00000593998; ENSP00000472551; ENSG00000167772.
GeneIDi51129.
KEGGihsa:51129.
UCSCiuc002mjq.1. human. [Q9BY76-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169312 mRNA. Translation: AAF62868.1.
AF202636 mRNA. Translation: AAG22490.1.
AB056477 mRNA. Translation: BAB40692.1.
AF153606 mRNA. Translation: AAD41088.1.
AY358275 mRNA. Translation: AAQ88642.1. Different initiation.
AK303269 mRNA. Translation: BAG64351.1.
AK222489 mRNA. Translation: BAD96209.1.
AK222524 mRNA. Translation: BAD96244.1.
AC136469 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68930.1.
CH471139 Genomic DNA. Translation: EAW68931.1.
BC023647 mRNA. Translation: AAH23647.1.
CCDSiCCDS12200.1. [Q9BY76-1]
CCDS42493.1. [Q9BY76-2]
RefSeqiNP_001034756.1. NM_001039667.2. [Q9BY76-2]
NP_647475.1. NM_139314.2. [Q9BY76-1]
UniGeneiHs.9613.

3D structure databases

ProteinModelPortaliQ9BY76.
SMRiQ9BY76. Positions 137-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119316. 4 interactions.
IntActiQ9BY76. 13 interactions.
STRINGi9606.ENSP00000301455.

PTM databases

PhosphoSiteiQ9BY76.

Polymorphism and mutation databases

BioMutaiANGPTL4.
DMDMi25008123.

Proteomic databases

MaxQBiQ9BY76.
PaxDbiQ9BY76.
PRIDEiQ9BY76.

Protocols and materials databases

DNASUi51129.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301455; ENSP00000301455; ENSG00000167772.
ENST00000393962; ENSP00000377534; ENSG00000167772. [Q9BY76-2]
ENST00000593998; ENSP00000472551; ENSG00000167772.
GeneIDi51129.
KEGGihsa:51129.
UCSCiuc002mjq.1. human. [Q9BY76-1]

Organism-specific databases

CTDi51129.
GeneCardsiGC19P008429.
HGNCiHGNC:16039. ANGPTL4.
HPAiCAB033770.
MIMi605910. gene.
615881. phenotype.
neXtProtiNX_Q9BY76.
PharmGKBiPA24797.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG281759.
GeneTreeiENSGT00770000120463.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ9BY76.
KOiK08767.
OMAiVDFNRPW.
PhylomeDBiQ9BY76.
TreeFamiTF329953.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSiANGPTL4. human.
GeneWikiiANGPTL4.
GenomeRNAii51129.
NextBioi35476680.
PROiQ9BY76.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BY76.
CleanExiHS_ANGPTL4.
ExpressionAtlasiQ9BY76. baseline and differential.
GenevisibleiQ9BY76. HS.

Family and domain databases

Gene3Di3.90.215.10. 2 hits.
4.10.530.10. 1 hit.
InterProiIPR028793. ANGPTL4.
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:SF16. PTHR19143:SF16. 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. "Hepatic expression, synthesis and secretion of a novel fibrinogen/angiopoietin-related protein that prevents endothelial-cell apoptosis."
    Kim I., Kim H.-G., Kim H., Kim H.-H., Park S.K., Uhm C.-S., Lee Z.H., Koh G.Y.
    Biochem. J. 346:603-610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANT MET-266.
  2. "Peroxisome proliferator-activated receptor gamma target gene encoding a novel angiopoietin-related protein associated with adipose differentiation."
    Yoon J.C., Chickering T.W., Rosen E.D., Dussault B., Qin Y., Soukas A., Friedman J.M., Holmes W.E., Spiegelman B.M.
    Mol. Cell. Biol. 20:5343-5349(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION.
    Tissue: Aortic endothelium.
  3. "Cloning of a novel gene, ANGPTL4 and the functional study in angiogenesis."
    Zhu H., Li J., Qin W., Yang Y., He X., Wan D., Gu J.
    Zhonghua Yi Xue Za Zhi 82:94-99(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "Inhibition of angiogenesis and vascular leakiness by angiopoietin-related protein 4."
    Ito Y., Oike Y., Yasunaga K., Hamada K., Miyata K., Matsumoto S., Sugano S., Tanihara H., Masuho Y., Suda T.
    Cancer Res. 63:6651-6657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Placenta.
  5. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hair follicle dermal papilla.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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 3).
    Tissue: Thymus.
  8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-266.
    Tissue: Adipose tissue.
  9. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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).
    Tissue: Pancreas.
  12. "Expression and function of hepatocellular carcinoma-related gene pp1158."
    Zhu H., Li J., Wan D., Yang Y., Qin W., Ge C., Yao M., Gu J.
    Zhonghua Zhong Liu Za Zhi 24:123-125(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  13. "Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL."
    Romeo S., Pennacchio L.A., Fu Y., Boerwinkle E., Tybjaerg-Hansen A., Hobbs H.H., Cohen J.C.
    Nat. Genet. 39:513-516(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH TGQTL, VARIANTS LEU-5; LYS-40; ILE-41; ARG-67; LEU-72; ARG-77; LYS-167; SER-174; GLN-190; LYS-196; CYS-230; ARG-233; VAL-237; THR-251; MET-266; GLN-278; MET-291; MET-293; VAL-296; SER-307; MET-308; CYS-336; GLU-338; CYS-349; SER-361; ARG-361; GLN-371 AND TRP-384.

Entry informationi

Entry nameiANGL4_HUMAN
AccessioniPrimary (citable) accession number: Q9BY76
Secondary accession number(s): A8MY84
, B4E089, D6W670, F5H0I2, Q53HQ6, Q53HU1, Q6UXN0, Q9HBV4, Q9NZU4, Q9Y5B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: July 22, 2015
This is version 133 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. 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.