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Q9BY76 (ANGL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiopoietin-related protein 4
Alternative name(s):
Angiopoietin-like protein 4
Hepatic fibrinogen/angiopoietin-related protein
Short name=HFARP
Gene names
Name:ANGPTL4
Synonyms:ARP4, HFARP, PGAR
ORF Names:PP1158, PSEC0166, UNQ171/PRO197
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.12

Subunit structure

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.

Subcellular location

Secreted. 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. Ref.1

Tissue specificity

Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney. Ref.1 Ref.12

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular lipid metabolic process

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipoprotein lipase activity

Inferred from direct assay PubMed 19542565. Source: BHF-UCL

positive regulation of angiogenesis

Traceable author statement Ref.3. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Non-traceable author statement PubMed 12707035. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.1. Source: MGI

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21397862. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BY76-1)

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.
Isoform 2 (identifier: Q9BY76-2)

The sequence of this isoform differs from the canonical sequence as follows:
     183-221: RLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSD → H
Note: Gene prediction based on EST data.
Isoform 3 (identifier: Q9BY76-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-167: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 406381Angiopoietin-related protein 4
PRO_0000009124

Regions

Domain179 – 401223Fibrinogen C-terminal
Coiled coil100 – 14344 Potential

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond188 ↔ 216 By similarity
Disulfide bond341 ↔ 354 By similarity

Natural variations

Alternative sequence1 – 167167Missing in isoform 3.
VSP_055092
Alternative sequence183 – 22139RLPRD…KMTSD → H in isoform 2.
VSP_047045
Natural variant51P → L. Ref.13
VAR_032642
Natural variant401E → K Associated with lower plasma levels of triglyceride and higher levels of HDL cholesterol. Ref.13
Corresponds to variant rs116843064 [ dbSNP | Ensembl ].
VAR_032643
Natural variant411M → I. Ref.13
Corresponds to variant rs186754194 [ dbSNP | Ensembl ].
VAR_032644
Natural variant671S → R. Ref.13
VAR_032645
Natural variant721R → L. Ref.13
Corresponds to variant rs141831018 [ dbSNP | Ensembl ].
VAR_032646
Natural variant771G → R. Ref.13
VAR_032647
Natural variant1671E → K. Ref.13
Corresponds to variant rs140640857 [ dbSNP | Ensembl ].
VAR_032648
Natural variant1741P → S. Ref.13
VAR_032649
Natural variant1901E → Q. Ref.13
Corresponds to variant rs77938377 [ dbSNP | Ensembl ].
VAR_032650
Natural variant1961E → K. Ref.13
VAR_032651
Natural variant2301R → C. Ref.13
Corresponds to variant rs201026877 [ dbSNP | Ensembl ].
VAR_032652
Natural variant2331G → R. Ref.13
VAR_032653
Natural variant2371F → V. Ref.13
VAR_032654
Natural variant2511P → T. Ref.13
VAR_032655
Natural variant2661T → M. Ref.1 Ref.8 Ref.13
Corresponds to variant rs1044250 [ dbSNP | Ensembl ].
VAR_020428
Natural variant2781R → Q. Ref.13
Corresponds to variant rs35061979 [ dbSNP | Ensembl ].
VAR_032656
Natural variant2911V → M. Ref.13
VAR_032657
Natural variant2931L → M. Ref.13
VAR_032658
Natural variant2961E → V. Ref.13
VAR_032659
Natural variant3071P → S. Ref.13
VAR_032660
Natural variant3081V → M. Ref.13
Corresponds to variant rs139998264 [ dbSNP | Ensembl ].
VAR_032661
Natural variant3361R → C. Ref.13
Corresponds to variant rs140744493 [ dbSNP | Ensembl ].
VAR_032662
Natural variant3381D → E. Ref.13
VAR_032663
Natural variant3491W → C. Ref.13
VAR_032664
Natural variant3611G → R. Ref.13
VAR_032665
Natural variant3611G → S. Ref.13
VAR_032666
Natural variant3711R → Q. Ref.13
VAR_032667
Natural variant3841R → W. Ref.13
VAR_032668

Experimental info

Sequence conflict55 – 7117LREHA…SALER → CANTGAHPQSAERAGA in AAD41088. Ref.5
Sequence conflict601E → G in BAB40692. Ref.4
Sequence conflict1751A → P in AAF62868. Ref.1
Sequence conflict2371F → S in BAG64351. Ref.7
Sequence conflict2511P → S in BAD96209. Ref.8
Sequence conflict2701N → D Ref.7
Sequence conflict2701N → D Ref.8
Sequence conflict2771L → R in BAD96244. Ref.8
Sequence conflict3041L → F in AAF62868. Ref.1
Sequence conflict3631Y → H in BAD96209. Ref.8
Sequence conflict3891P → S in AAF62868. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: 219E56FEB3F602AF

FASTA40645,214
        10         20         30         40         50         60 
MSGAPTAGAA LMLCAATAVL LSAQGGPVQS KSPRFASWDE MNVLAHGLLQ LGQGLREHAE 

        70         80         90        100        110        120 
RTRSQLSALE RRLSACGSAC QGTEGSTDLP LAPESRVDPE VLHSLQTQLK AQNSRIQQLF 

       130        140        150        160        170        180 
HKVAQQQRHL EKQHLRIQHL QSQFGLLDHK HLDHEVAKPA RRKRLPEMAQ PVDPAHNVSR 

       190        200        210        220        230        240 
LHRLPRDCQE LFQVGERQSG LFEIQPQGSP PFLVNCKMTS DGGWTVIQRR HDGSVDFNRP 

       250        260        270        280        290        300 
WEAYKAGFGD PHGEFWLGLE KVHSITGDRN SRLAVQLRDW DGNAELLQFS VHLGGEDTAY 

       310        320        330        340        350        360 
SLQLTAPVAG QLGATTVPPS GLSVPFSTWD QDHDLRRDKN CAKSLSGGWW FGTCSHSNLN 

       370        380        390        400 
GQYFRSIPQQ RQKLKKGIFW KTWRGRYYPL QATTMLIQPM AAEAAS 

« Hide

Isoform 2 [UniParc].

Checksum: 7D61B5306C3AF298
Show »

FASTA36840,917
Isoform 3 [UniParc].

Checksum: FBB362F2DBDB6900
Show »

FASTA23926,853

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12200.1. [Q9BY76-1]
CCDS42493.1. [Q9BY76-2]
RefSeqNP_001034756.1. NM_001039667.2. [Q9BY76-2]
NP_647475.1. NM_139314.2. [Q9BY76-1]
UniGeneHs.9613.

3D structure databases

ProteinModelPortalQ9BY76.
SMRQ9BY76. Positions 48-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119316. 4 interactions.
IntActQ9BY76. 4 interactions.
STRING9606.ENSP00000301455.

PTM databases

PhosphoSiteQ9BY76.

Polymorphism databases

DMDM25008123.

Proteomic databases

PaxDbQ9BY76.
PRIDEQ9BY76.

Protocols and materials databases

DNASU51129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301455; ENSP00000301455; ENSG00000167772. [Q9BY76-1]
ENST00000393962; ENSP00000377534; ENSG00000167772. [Q9BY76-2]
ENST00000541807; ENSP00000439833; ENSG00000167772.
ENST00000593998; ENSP00000472551; ENSG00000167772. [Q9BY76-1]
GeneID51129.
KEGGhsa:51129.
UCSCuc002mjq.1. human. [Q9BY76-1]

Organism-specific databases

CTD51129.
GeneCardsGC19P008429.
HGNCHGNC:16039. ANGPTL4.
HPAHPA007879.
MIM605910. gene.
neXtProtNX_Q9BY76.
PharmGKBPA24797.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281759.
HOVERGENHBG001644.
InParanoidQ9BY76.
KOK08767.
OMAVDFNRPW.
PhylomeDBQ9BY76.
TreeFamTF329953.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9BY76.
BgeeQ9BY76.
CleanExHS_ANGPTL4.
GenevestigatorQ9BY76.

Family and domain databases

Gene3D3.90.215.10. 2 hits.
4.10.530.10. 1 hit.
InterProIPR028793. 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]
PANTHERPTHR19143:SF16. PTHR19143:SF16. 1 hit.
PfamPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiANGPTL4.
GenomeRNAi51129.
NextBio53949.
PROQ9BY76.
SOURCESearch...

Entry information

Entry nameANGL4_HUMAN
AccessionPrimary (citable) accession number: Q9BY76
Secondary accession number(s): A8MY84 expand/collapse secondary AC list , B4E089, D6W670, F5H0I2, Q53HQ6, Q53HU1, Q6UXN0, Q9HBV4, Q9NZU4, Q9Y5B3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM