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Protein

EGF-containing fibulin-like extracellular matrix protein 2

Gene

EFEMP2

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

Functioni

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: ProtInc
  3. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: InterPro
  2. extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EGF-containing fibulin-like extracellular matrix protein 2
Alternative name(s):
Fibulin-4
Short name:
FIBL-4
Protein UPH1
Gene namesi
Name:EFEMP2
Synonyms:FBLN4
ORF Names:UNQ200/PRO226
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3219. EFEMP2.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: ProtInc
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: InterPro
  5. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 1B (ARCL1B)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. ARCL1B features include emphysema, lethal pulmonary artery occlusion, aortic aneurysm, cardiopulmonary insufficiency, birth fractures, arachnodactyly, and fragility of blood vessels.

See also OMIM:614437
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571E → K in ARCL1B. 1 Publication
VAR_027019
Natural varianti267 – 2671C → Y in ARCL1B. 1 Publication
VAR_067069
Natural varianti279 – 2791R → C in ARCL1B. 1 Publication
VAR_067070

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614437. phenotype.
Orphaneti90349. Autosomal recessive cutis laxa type 1.
314718. Lethal arteriopathy syndrome due to fibulin-4 deficiency.
PharmGKBiPA27653.

Polymorphism and mutation databases

BioMutaiEFEMP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 443418EGF-containing fibulin-like extracellular matrix protein 2PRO_0000007575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 121PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 80PROSITE-ProRule annotation1 Publication
Disulfide bondi71 ↔ 109PROSITE-ProRule annotation1 Publication
Disulfide bondi127 ↔ 140PROSITE-ProRule annotation
Disulfide bondi134 ↔ 149PROSITE-ProRule annotation
Disulfide bondi151 ↔ 162PROSITE-ProRule annotation
Disulfide bondi168 ↔ 177PROSITE-ProRule annotation
Disulfide bondi173 ↔ 186PROSITE-ProRule annotation
Disulfide bondi188 ↔ 201PROSITE-ProRule annotation
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi207 ↔ 217PROSITE-ProRule annotation
Disulfide bondi213 ↔ 226PROSITE-ProRule annotation
Disulfide bondi228 ↔ 241PROSITE-ProRule annotation
Disulfide bondi247 ↔ 258PROSITE-ProRule annotation
Disulfide bondi254 ↔ 267PROSITE-ProRule annotation
Disulfide bondi269 ↔ 281PROSITE-ProRule annotation
Disulfide bondi287 ↔ 300PROSITE-ProRule annotation
Disulfide bondi294 ↔ 309PROSITE-ProRule annotation
Disulfide bondi315 ↔ 327PROSITE-ProRule annotation
Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO95967.
PRIDEiO95967.

PTM databases

PhosphoSiteiO95967.

Expressioni

Gene expression databases

BgeeiO95967.
CleanExiHS_EFEMP2.
ExpressionAtlasiO95967. baseline and differential.
GenevestigatoriO95967.

Organism-specific databases

HPAiHPA023270.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ATN1P542593EBI-743414,EBI-945980
C5orf24Q7Z6I83EBI-743414,EBI-9995695
CREB5Q02930-35EBI-743414,EBI-10192698
ELNP155025EBI-743414,EBI-1222108
FAM74A6Q5TZK33EBI-743414,EBI-10247271
FBLN5Q9UBX53EBI-743414,EBI-947897
FBN1P355553EBI-743414,EBI-2505934
HDAC4P565243EBI-743414,EBI-308629
Hoxa1P090223EBI-743414,EBI-3957603From a different organism.
LCE2DQ5TA823EBI-743414,EBI-10246750
LCE3CQ5T5A83EBI-743414,EBI-10245291
LOXP283004EBI-743414,EBI-3893481
MEOX2A4D1273EBI-743414,EBI-10172134
NUFIP2A1L3A73EBI-743414,EBI-10172018
PTGER3Q147X83EBI-743414,EBI-10234038
RBPMSQ930623EBI-743414,EBI-740322
RHOXF2Q9BQY42EBI-743414,EBI-372094
SGTAO437654EBI-743414,EBI-347996
SGTBQ96EQ04EBI-743414,EBI-744081
STK16O757163EBI-743414,EBI-749295
UBQLN1Q9UMX0-23EBI-743414,EBI-10173939

Protein-protein interaction databases

BioGridi119026. 51 interactions.
DIPiDIP-34518N.
IntActiO95967. 56 interactions.
MINTiMINT-1439082.
STRINGi9606.ENSP00000309953.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi68 – 736Combined sources
Beta strandi78 – 825Combined sources
Beta strandi113 – 1164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KL7NMR-A54-123[»]
ProteinModelPortaliO95967.
SMRiO95967. Positions 54-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95967.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 8146EGF-like 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini123 – 16341EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini164 – 20239EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 24240EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 28240EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 32846EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 6 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG254862.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiO95967.
OMAiQECHNLP.
PhylomeDBiO95967.
TreeFamiTF317514.

Family and domain databases

InterProiIPR026823. cEGF.
IPR026824. Efemp2.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PANTHERiPTHR24048:SF2. PTHR24048:SF2. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O95967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPCASCLPG SLLLWALLLL LLGSASPQDS EEPDSYTECT DGYEWDPDSQ
60 70 80 90 100
HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV
110 120 130 140 150
PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT
160 170 180 190 200
CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS
210 220 230 240 250
CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS
260 270 280 290 300
SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC
310 320 330 340 350
VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI
360 370 380 390 400
TSERSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV
410 420 430 440
LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF
Length:443
Mass (Da):49,405
Last modified:March 20, 2007 - v3
Checksum:i9315CFBBAA0FD3A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → T in CAA10791 (PubMed:10601734).Curated
Sequence conflicti44 – 518EWDPDSQH → TQTAN in AAC62108 (Ref. 2) Curated
Sequence conflicti46 – 461D → G in BAF84768 (PubMed:14702039).Curated
Sequence conflicti96 – 961P → L in BAG50843 (PubMed:14702039).Curated
Sequence conflicti103 – 1119AQHPNPCPP → VNTQPLPT in AAC62108 (Ref. 2) Curated
Sequence conflicti294 – 2941C → W in AAC62108 (Ref. 2) Curated
Sequence conflicti354 – 3563RSV → AER in AAC62108 (Ref. 2) Curated
Sequence conflicti355 – 3551S → R in AAF65188 (PubMed:10982184).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571E → K in ARCL1B. 1 Publication
VAR_027019
Natural varianti259 – 2591I → V.7 Publications
Corresponds to variant rs601314 [ dbSNP | Ensembl ].
VAR_027020
Natural varianti267 – 2671C → Y in ARCL1B. 1 Publication
VAR_067069
Natural varianti279 – 2791R → C in ARCL1B. 1 Publication
VAR_067070

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132819 mRNA. Translation: CAA10791.2.
AF093119 mRNA. Translation: AAC62108.1.
AF109121 mRNA. Translation: AAF65188.1.
AK000980 mRNA. Translation: BAG50843.1.
AK292079 mRNA. Translation: BAF84768.1.
AY358899 mRNA. Translation: AAQ89258.1.
AK075453 mRNA. Translation: BAG52143.1.
AP001201 Genomic DNA. No translation available.
BC010456 mRNA. Translation: AAH10456.1.
CCDSiCCDS8116.1.
RefSeqiNP_058634.4. NM_016938.4.
UniGeneiHs.731454.

Genome annotation databases

EnsembliENST00000307998; ENSP00000309953; ENSG00000172638.
ENST00000531972; ENSP00000435295; ENSG00000172638.
GeneIDi30008.
KEGGihsa:30008.
UCSCiuc001ofy.4. human.

Polymorphism and mutation databases

BioMutaiEFEMP2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132819 mRNA. Translation: CAA10791.2.
AF093119 mRNA. Translation: AAC62108.1.
AF109121 mRNA. Translation: AAF65188.1.
AK000980 mRNA. Translation: BAG50843.1.
AK292079 mRNA. Translation: BAF84768.1.
AY358899 mRNA. Translation: AAQ89258.1.
AK075453 mRNA. Translation: BAG52143.1.
AP001201 Genomic DNA. No translation available.
BC010456 mRNA. Translation: AAH10456.1.
CCDSiCCDS8116.1.
RefSeqiNP_058634.4. NM_016938.4.
UniGeneiHs.731454.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KL7NMR-A54-123[»]
ProteinModelPortaliO95967.
SMRiO95967. Positions 54-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119026. 51 interactions.
DIPiDIP-34518N.
IntActiO95967. 56 interactions.
MINTiMINT-1439082.
STRINGi9606.ENSP00000309953.

PTM databases

PhosphoSiteiO95967.

Polymorphism and mutation databases

BioMutaiEFEMP2.

Proteomic databases

PaxDbiO95967.
PRIDEiO95967.

Protocols and materials databases

DNASUi30008.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307998; ENSP00000309953; ENSG00000172638.
ENST00000531972; ENSP00000435295; ENSG00000172638.
GeneIDi30008.
KEGGihsa:30008.
UCSCiuc001ofy.4. human.

Organism-specific databases

CTDi30008.
GeneCardsiGC11M065633.
GeneReviewsiEFEMP2.
HGNCiHGNC:3219. EFEMP2.
HPAiHPA023270.
MIMi604633. gene.
614437. phenotype.
neXtProtiNX_O95967.
Orphaneti90349. Autosomal recessive cutis laxa type 1.
314718. Lethal arteriopathy syndrome due to fibulin-4 deficiency.
PharmGKBiPA27653.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG254862.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiO95967.
OMAiQECHNLP.
PhylomeDBiO95967.
TreeFamiTF317514.

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

EvolutionaryTraceiO95967.
GeneWikiiEFEMP2.
GenomeRNAii30008.
NextBioi52820.
PROiO95967.
SOURCEiSearch...

Gene expression databases

BgeeiO95967.
CleanExiHS_EFEMP2.
ExpressionAtlasiO95967. baseline and differential.
GenevestigatoriO95967.

Family and domain databases

InterProiIPR026823. cEGF.
IPR026824. Efemp2.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PANTHERiPTHR24048:SF2. PTHR24048:SF2. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4."
    Giltay R., Timpl R., Kostka G.
    Matrix Biol. 18:469-480(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-259.
    Tissue: Melanoma.
  2. Zemel R., Shaul Y.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-259.
  3. "Isolation of a paralog of the Doyne honeycomb retinal dystrophy gene from the multiple retinopathy critical region on 11q13."
    Katsanis N., Venable S., Smith J.R., Lupski J.R.
    Hum. Genet. 106:66-72(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-259.
  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], VARIANT VAL-259.
    Tissue: Embryo and Synovium.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-259.
  6. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-259.
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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], VARIANT VAL-259.
    Tissue: Brain.
  9. "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.
  10. "Solution NMR structure of the EGF-like 1 domain of human fibulin-4."
    Northeast structural genomics consortium (NESG)
    Submitted (JUL-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 54-123, DISULFIDE BONDS.
  11. "Fibulin-4: a novel gene for an autosomal recessive cutis laxa syndrome."
    Hucthagowder V., Sausgruber N., Kim K.H., Angle B., Marmorstein L.Y., Urban Z.
    Am. J. Hum. Genet. 78:1075-1080(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1B LYS-57.
  12. "Compound heterozygous mutations in fibulin-4 causing neonatal lethal pulmonary artery occlusion, aortic aneurysm, arachnodactyly, and mild cutis laxa."
    Dasouki M., Markova D., Garola R., Sasaki T., Charbonneau N.L., Sakai L.Y., Chu M.L.
    Am. J. Med. Genet. A 143:2635-2641(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1B CYS-279.
  13. "Lethal cutis laxa with contractural arachnodactyly, overgrowth and soft tissue bleeding due to a novel homozygous fibulin-4 gene mutation."
    Hoyer J., Kraus C., Hammersen G., Geppert J.P., Rauch A.
    Clin. Genet. 76:276-281(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1B TYR-267.

Entry informationi

Entry nameiFBLN4_HUMAN
AccessioniPrimary (citable) accession number: O95967
Secondary accession number(s): A8K7R4
, B3KM31, B3KQT1, O75967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 20, 2007
Last modified: April 29, 2015
This is version 158 of the entry and version 3 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 11
    Human chromosome 11: 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.