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O95967

- FBLN4_HUMAN

UniProt

O95967 - FBLN4_HUMAN

Protein

EGF-containing fibulin-like extracellular matrix protein 2

Gene

EFEMP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

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

    GO - Biological processi

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

    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: 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: UniProt
    4. membrane Source: InterPro

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Cutis laxa, autosomal recessive, 1B (ARCL1B) [MIM:614437]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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 ↔ 1211 PublicationPROSITE-ProRule annotation
    Disulfide bondi65 ↔ 801 PublicationPROSITE-ProRule annotation
    Disulfide bondi71 ↔ 1091 PublicationPROSITE-ProRule annotation
    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

    ArrayExpressiO95967.
    BgeeiO95967.
    CleanExiHS_EFEMP2.
    GenevestigatoriO95967.

    Organism-specific databases

    HPAiHPA023270.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATN1P542593EBI-743414,EBI-945980
    ELNP155025EBI-743414,EBI-1222108
    FBLN5Q9UBX53EBI-743414,EBI-947897
    FBN1P355553EBI-743414,EBI-2505934
    Hoxa1P090223EBI-743414,EBI-3957603From a different organism.
    LOXP283004EBI-743414,EBI-3893481
    RHOXF2Q9BQY42EBI-743414,EBI-372094

    Protein-protein interaction databases

    BioGridi119026. 38 interactions.
    DIPiDIP-34518N.
    IntActiO95967. 44 interactions.
    MINTiMINT-1439082.
    STRINGi9606.ENSP00000309953.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    IPR001491. Thrombomodulin.
    [Graphical view]
    PANTHERiPTHR24048:SF2. PTHR24048:SF2. 1 hit.
    PfamiPF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 3 hits.
    [Graphical view]
    PRINTSiPR00907. THRMBOMODULN.
    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

    MLPCASCLPG SLLLWALLLL LLGSASPQDS EEPDSYTECT DGYEWDPDSQ    50
    HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV 100
    PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT 150
    CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS 200
    CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS 250
    SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC 300
    VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI 350
    TSERSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV 400
    LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF 443
    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. 1 PublicationCurated
    Sequence conflicti46 – 461D → G in BAF84768. (PubMed:14702039)Curated
    Sequence conflicti96 – 961P → L in BAG50843. (PubMed:14702039)Curated
    Sequence conflicti103 – 1119AQHPNPCPP → VNTQPLPT in AAC62108. 1 PublicationCurated
    Sequence conflicti294 – 2941C → W in AAC62108. 1 PublicationCurated
    Sequence conflicti354 – 3563RSV → AER in AAC62108. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8116.1.
    RefSeqi NP_058634.4. NM_016938.4.
    UniGenei Hs.731454.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KL7 NMR - A 54-123 [» ]
    ProteinModelPortali O95967.
    SMRi O95967. Positions 54-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119026. 38 interactions.
    DIPi DIP-34518N.
    IntActi O95967. 44 interactions.
    MINTi MINT-1439082.
    STRINGi 9606.ENSP00000309953.

    PTM databases

    PhosphoSitei O95967.

    Proteomic databases

    PaxDbi O95967.
    PRIDEi O95967.

    Protocols and materials databases

    DNASUi 30008.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307998 ; ENSP00000309953 ; ENSG00000172638 .
    ENST00000531972 ; ENSP00000435295 ; ENSG00000172638 .
    GeneIDi 30008.
    KEGGi hsa:30008.
    UCSCi uc001ofy.4. human.

    Organism-specific databases

    CTDi 30008.
    GeneCardsi GC11M065633.
    GeneReviewsi EFEMP2.
    HGNCi HGNC:3219. EFEMP2.
    HPAi HPA023270.
    MIMi 604633. gene.
    614437. phenotype.
    neXtProti NX_O95967.
    Orphaneti 90349. Autosomal recessive cutis laxa type 1.
    314718. Lethal arteriopathy syndrome due to Fibulin-4 deficiency.
    PharmGKBi PA27653.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254862.
    HOGENOMi HOG000234337.
    HOVERGENi HBG051560.
    InParanoidi O95967.
    OMAi QECHNLP.
    PhylomeDBi O95967.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    EvolutionaryTracei O95967.
    GeneWikii EFEMP2.
    GenomeRNAii 30008.
    NextBioi 52820.
    PROi O95967.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95967.
    Bgeei O95967.
    CleanExi HS_EFEMP2.
    Genevestigatori O95967.

    Family and domain databases

    InterProi IPR026823. 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.
    IPR001491. Thrombomodulin.
    [Graphical view ]
    PANTHERi PTHR24048:SF2. PTHR24048:SF2. 1 hit.
    Pfami PF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 3 hits.
    [Graphical view ]
    PRINTSi PR00907. THRMBOMODULN.
    SMARTi SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 2 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    10. "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.
    11. "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.
    12. "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: October 1, 2014
    This is version 151 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