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P98095

- FBLN2_HUMAN

UniProt

P98095 - FBLN2_HUMAN

Protein

Fibulin-2

Gene

FBLN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (03 Mar 2009)
      Previous versions | rss
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    Functioni

    Its binding to fibronectin and some other ligands is calcium dependent.

    GO - Molecular functioni

    1. calcium ion binding Source: ProtInc
    2. extracellular matrix binding Source: Ensembl
    3. extracellular matrix structural constituent Source: ProtInc

    GO - Biological processi

    1. extracellular matrix organization Source: Reactome
    2. positive regulation of cell-substrate adhesion Source: Ensembl

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_150331. Molecules associated with elastic fibres.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibulin-2
    Short name:
    FIBL-2
    Gene namesi
    Name:FBLN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3601. FBLN2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 11841157Fibulin-2PRO_0000007568Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei277 – 2771Phosphoserine1 Publication
    Glycosylationi347 – 3471O-linked (GalNAc...); or Ser-3481 Publication
    Glycosylationi348 – 3481O-linked (GalNAc...); or Thr-3471 Publication
    Disulfide bondi445 ↔ 472By similarity
    Disulfide bondi446 ↔ 479By similarity
    Disulfide bondi459 ↔ 480By similarity
    Disulfide bondi489 ↔ 518By similarity
    Disulfide bondi502 ↔ 519By similarity
    Glycosylationi507 – 5071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi521 ↔ 545By similarity
    Disulfide bondi522 ↔ 552By similarity
    Disulfide bondi535 ↔ 553By similarity
    Disulfide bondi608 ↔ 620By similarity
    Disulfide bondi616 ↔ 629By similarity
    Disulfide bondi631 ↔ 644By similarity
    Disulfide bondi683 ↔ 693By similarity
    Disulfide bondi689 ↔ 702By similarity
    Disulfide bondi704 ↔ 717By similarity
    Disulfide bondi723 ↔ 736By similarity
    Disulfide bondi730 ↔ 745By similarity
    Disulfide bondi751 ↔ 762By similarity
    Disulfide bondi768 ↔ 781By similarity
    Disulfide bondi775 ↔ 790By similarity
    Disulfide bondi796 ↔ 808By similarity
    Disulfide bondi814 ↔ 827By similarity
    Disulfide bondi821 ↔ 836By similarity
    Disulfide bondi843 ↔ 856By similarity
    Disulfide bondi862 ↔ 875By similarity
    Disulfide bondi869 ↔ 884By similarity
    Disulfide bondi886 ↔ 899By similarity
    Disulfide bondi905 ↔ 917By similarity
    Disulfide bondi913 ↔ 926By similarity
    Disulfide bondi928 ↔ 941By similarity
    Disulfide bondi947 ↔ 956By similarity
    Disulfide bondi952 ↔ 965By similarity
    Disulfide bondi967 ↔ 980By similarity
    Disulfide bondi986 ↔ 998By similarity
    Disulfide bondi994 ↔ 1007By similarity
    Disulfide bondi1009 ↔ 1023By similarity
    Disulfide bondi1029 ↔ 1042By similarity
    Glycosylationi1035 – 10351N-linked (GlcNAc...)1 Publication
    Disulfide bondi1036 ↔ 1051By similarity
    Disulfide bondi1056 ↔ 1068By similarity

    Post-translational modificationi

    O-glycosylated with core 1 or possibly core 8 glycans. It is unsure if the O-glycosylation is on Thr-347 or Ser-348.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP98095.
    PaxDbiP98095.
    PRIDEiP98095.

    PTM databases

    PhosphoSiteiP98095.

    Expressioni

    Tissue specificityi

    Component of both basement membranes and other connective tissues. Expressed in heart, placenta and ovary.

    Developmental stagei

    Widely expressed during embryonic development. Primarily detected within the neuropithelium, spinal ganglia and peripheral nerves.1 Publication

    Gene expression databases

    ArrayExpressiP98095.
    BgeeiP98095.
    CleanExiHS_FBLN2.
    GenevestigatoriP98095.

    Organism-specific databases

    HPAiCAB018622.
    HPA001934.

    Interactioni

    Subunit structurei

    Homotrimer; disulfide-linked. Interacts with LAMA2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108493. 15 interactions.
    IntActiP98095. 5 interactions.
    MINTiMINT-1518617.
    STRINGi9606.ENSP00000384169.

    Structurei

    3D structure databases

    ProteinModelPortaliP98095.
    SMRiP98095. Positions 604-637, 685-1060.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini445 – 48036Anaphylatoxin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 51932Anaphylatoxin-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini521 – 55333Anaphylatoxin-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini604 – 64542EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini679 – 71840EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini719 – 76345EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini764 – 80946EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini810 – 85748EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini858 – 90043EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini901 – 94242EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini943 – 98139EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini982 – 102443EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1025 – 106945EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni28 – 444417NAdd
    BLAST
    Regioni28 – 177150Subdomain NA (Cys-rich)Add
    BLAST
    Regioni178 – 444267Subdomain NB (Cys-free)Add
    BLAST
    Regioni1070 – 1184115Domain IIIAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fibulin family.Curated
    Contains 3 anaphylatoxin-like domains.PROSITE-ProRule annotation
    Contains 10 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000007079.
    HOVERGENiHBG051559.
    KOiK17307.
    OMAiSETKCER.
    OrthoDBiEOG7P5T0C.
    PhylomeDBiP98095.
    TreeFamiTF317514.

    Family and domain databases

    InterProiIPR000020. Anaphylatoxin/fibulin.
    IPR026823. cEGF.
    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]
    PfamiPF01821. ANATO. 2 hits.
    PF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 5 hits.
    [Graphical view]
    SMARTiSM00104. ANATO. 3 hits.
    SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 9 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 5 hits.
    PROSITEiPS01177. ANAPHYLATOXIN_1. 3 hits.
    PS01178. ANAPHYLATOXIN_2. 3 hits.
    PS00010. ASX_HYDROXYL. 5 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 9 hits.
    [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. Align

    Isoform 1 (identifier: P98095-1) [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

    MVLLWEPAGA WLALGLALAL GPSVAAAAPR QDCTGVECPP LENCIEEALE     50
    PGACCATCVQ QGCACEGYQY YDCLQGGFVR GRVPAGQSYF VDFGSTECSC 100
    PPGGGKISCQ FMLCPELPPN CIEAVVVADS CPQCGQVGCV HAGHKYAAGH 150
    TVHLPPCRAC HCPDAGGELI CYQLPGCHGN FSDAEEGDPE RHYEDPYSYD 200
    QEVAEVEAAT ALGGEVQAGA VQAGAGGPPA ALGGGSQPLS TIQAPPWPAV 250
    LPRPTAAAAL GPPAPVQAKA RRVTEDSEEE EEEEEEREEM AVTEQLAAGG 300
    HRGLDGLPTT APAGPSLPIQ EERAEAGARA EAGARPEENL ILDAQATSRS 350
    TGPEGVTHAP SLGKAALVPT QAVPGSPRDP VKPSPHNILS TSLPDAAWIP 400
    PTREVPRKPQ VLPHSHVEED TDPNSVHSIP RSSPEGSTKD LIETCCAAGQ 450
    QWAIDNDECL EIPESGTEDN VCRTAQRHCC VSYLQEKSCM AGVLGAKEGE 500
    TCGAEDNDSC GISLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML 550
    SCCEGEEPLI VPEVRRPPEP AAAPRRVSEA EMAGREALSL GTEAELPNSL 600
    PGDDQDECLL LPGELCQHLC INTVGSYHCA CFPGFSLQDD GRTCRPEGHP 650
    PQPEAPQEPA LKSEFSQVAS NTIPLPLPQP NTCKDNGPCK QVCSTVGGSA 700
    ICSCFPGYAI MADGVSCEDI NECVTDLHTC SRGEHCVNTL GSFHCYKALT 750
    CEPGYALKDG ECEDVDECAM GTHTCQPGFL CQNTKGSFYC QARQRCMDGF 800
    LQDPEGNCVD INECTSLSEP CRPGFSCINT VGSYTCQRNP LICARGYHAS 850
    DDGTKCVDVN ECETGVHRCG EGQVCHNLPG SYRCDCKAGF QRDAFGRGCI 900
    DVNECWASPG RLCQHTCENT LGSYRCSCAS GFLLAADGKR CEDVNECEAQ 950
    RCSQECANIY GSYQCYCRQG YQLAEDGHTC TDIDECAQGA GILCTFRCLN 1000
    VPGSYQCACP EQGYTMTANG RSCKDVDECA LGTHNCSEAE TCHNIQGSFR 1050
    CLRFECPPNY VQVSKTKCER TTCHDFLECQ NSPARITHYQ LNFQTGLLVP 1100
    AHIFRIGPAP AFTGDTIALN IIKGNEEGYF GTRRLNAYTG VVYLQRAVLE 1150
    PRDFALDVEM KLWRQGSVTT FLAKMHIFFT TFAL 1184
    Length:1,184
    Mass (Da):126,573
    Last modified:March 3, 2009 - v2
    Checksum:iD46890D93518B343
    GO
    Isoform 2 (identifier: P98095-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         718-718: E → EDQDECLMGAHDCSRRQFCVNTLGSFYCVNHTVLCADGYILNAHRKCV

    Show »
    Length:1,231
    Mass (Da):131,863
    Checksum:i914C7630E2D9FC4E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451K → E in CAA57876. (PubMed:7806230)Curated
    Sequence conflicti145 – 1451K → E in AAN05436. 1 PublicationCurated
    Sequence conflicti664 – 6641E → G in BAH14261. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451I → V.
    Corresponds to variant rs60850813 [ dbSNP | Ensembl ].
    VAR_061159
    Natural varianti144 – 1441H → R.
    Corresponds to variant rs28587534 [ dbSNP | Ensembl ].
    VAR_061160
    Natural varianti361 – 3611S → G.
    Corresponds to variant rs3732666 [ dbSNP | Ensembl ].
    VAR_059266
    Natural varianti387 – 3871N → T.
    Corresponds to variant rs3796318 [ dbSNP | Ensembl ].
    VAR_059267
    Natural varianti854 – 8541T → A.1 Publication
    Corresponds to variant rs9843344 [ dbSNP | Ensembl ].
    VAR_059268
    Natural varianti1114 – 11141G → R.
    Corresponds to variant rs1061375 [ dbSNP | Ensembl ].
    VAR_055722

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei718 – 7181E → EDQDECLMGAHDCSRRQFCV NTLGSFYCVNHTVLCADGYI LNAHRKCV in isoform 2. 2 PublicationsVSP_041404

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82494 mRNA. Translation: CAA57876.1.
    AY130458, AY130456, AY130457 Genomic DNA. Translation: AAN05435.1.
    AY130459 mRNA. Translation: AAN05436.1.
    AK304827 mRNA. Translation: BAH14261.1.
    AC090509 Genomic DNA. No translation available.
    CCDSiCCDS46761.1. [P98095-2]
    CCDS46762.1. [P98095-1]
    PIRiA55184.
    RefSeqiNP_001004019.1. NM_001004019.1. [P98095-2]
    NP_001158507.1. NM_001165035.1. [P98095-2]
    NP_001989.2. NM_001998.2. [P98095-1]
    UniGeneiHs.198862.

    Genome annotation databases

    EnsembliENST00000295760; ENSP00000295760; ENSG00000163520. [P98095-1]
    ENST00000404922; ENSP00000384169; ENSG00000163520. [P98095-2]
    ENST00000492059; ENSP00000420042; ENSG00000163520. [P98095-2]
    GeneIDi2199.
    KEGGihsa:2199.
    UCSCiuc011ava.2. human. [P98095-2]
    uc011avb.2. human. [P98095-1]

    Polymorphism databases

    DMDMi224471827.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82494 mRNA. Translation: CAA57876.1 .
    AY130458 , AY130456 , AY130457 Genomic DNA. Translation: AAN05435.1 .
    AY130459 mRNA. Translation: AAN05436.1 .
    AK304827 mRNA. Translation: BAH14261.1 .
    AC090509 Genomic DNA. No translation available.
    CCDSi CCDS46761.1. [P98095-2 ]
    CCDS46762.1. [P98095-1 ]
    PIRi A55184.
    RefSeqi NP_001004019.1. NM_001004019.1. [P98095-2 ]
    NP_001158507.1. NM_001165035.1. [P98095-2 ]
    NP_001989.2. NM_001998.2. [P98095-1 ]
    UniGenei Hs.198862.

    3D structure databases

    ProteinModelPortali P98095.
    SMRi P98095. Positions 604-637, 685-1060.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108493. 15 interactions.
    IntActi P98095. 5 interactions.
    MINTi MINT-1518617.
    STRINGi 9606.ENSP00000384169.

    PTM databases

    PhosphoSitei P98095.

    Polymorphism databases

    DMDMi 224471827.

    Proteomic databases

    MaxQBi P98095.
    PaxDbi P98095.
    PRIDEi P98095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295760 ; ENSP00000295760 ; ENSG00000163520 . [P98095-1 ]
    ENST00000404922 ; ENSP00000384169 ; ENSG00000163520 . [P98095-2 ]
    ENST00000492059 ; ENSP00000420042 ; ENSG00000163520 . [P98095-2 ]
    GeneIDi 2199.
    KEGGi hsa:2199.
    UCSCi uc011ava.2. human. [P98095-2 ]
    uc011avb.2. human. [P98095-1 ]

    Organism-specific databases

    CTDi 2199.
    GeneCardsi GC03P013565.
    H-InvDB HIX0003076.
    HGNCi HGNC:3601. FBLN2.
    HPAi CAB018622.
    HPA001934.
    MIMi 135821. gene.
    neXtProti NX_P98095.
    PharmGKBi PA28014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000007079.
    HOVERGENi HBG051559.
    KOi K17307.
    OMAi SETKCER.
    OrthoDBi EOG7P5T0C.
    PhylomeDBi P98095.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    GeneWikii FBLN2.
    GenomeRNAii 2199.
    NextBioi 8885.
    PROi P98095.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98095.
    Bgeei P98095.
    CleanExi HS_FBLN2.
    Genevestigatori P98095.

    Family and domain databases

    InterProi IPR000020. Anaphylatoxin/fibulin.
    IPR026823. cEGF.
    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 ]
    Pfami PF01821. ANATO. 2 hits.
    PF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 5 hits.
    [Graphical view ]
    SMARTi SM00104. ANATO. 3 hits.
    SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 9 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 5 hits.
    PROSITEi PS01177. ANAPHYLATOXIN_1. 3 hits.
    PS01178. ANAPHYLATOXIN_2. 3 hits.
    PS00010. ASX_HYDROXYL. 5 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression, and mapping of the gene on human and mouse chromosomes."
      Zhang R.-Z., Pan T.-C., Zhang Z.-Y., Mattei M.-G., Timpl R., Chu M.-L.
      Genomics 22:425-430(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-854.
      Tissue: Fibroblast.
    2. "Identification of a novel alternatively spliced isoform of human fibulin-2 gene abundantly expressed in heart and genetic evaluation in patients with ARVD."
      Li D., Marian A.J., Roberts R.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "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 2).
      Tissue: Uterus.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo."
      Miosge N., Gotz W., Sasaki T., Chu M.-L., Timpl R., Herken R.
      Histochem. J. 28:109-116(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    6. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1035.
      Tissue: Liver.
    8. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-347 AND SER-348, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiFBLN2_HUMAN
    AccessioniPrimary (citable) accession number: P98095
    Secondary accession number(s): B7Z9C5, Q8IUI0, Q8IUI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 138 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 3
      Human chromosome 3: 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