Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P98095 (FBLN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibulin-2

Short name=FIBL-2
Gene names
Name:FBLN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

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

Developmental stage

Widely expressed during embryonic development. Primarily detected within the neuropithelium, spinal ganglia and peripheral nerves. Ref.5

Post-translational modification

O-glycosylated with core 1 or possibly core 8 glycans. It is unsure if the O-glycosylation is on Thr-347 or Ser-348. Ref.8

Sequence similarities

Belongs to the fibulin family.

Contains 3 anaphylatoxin-like domains.

Contains 10 EGF-like domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P98095-1)

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: P98095-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 11841157Fibulin-2
PRO_0000007568

Regions

Domain445 – 48036Anaphylatoxin-like 1
Domain488 – 51932Anaphylatoxin-like 2
Domain521 – 55333Anaphylatoxin-like 3
Domain604 – 64542EGF-like 1; calcium-binding
Domain679 – 71840EGF-like 2
Domain719 – 76345EGF-like 3; calcium-binding
Domain764 – 80946EGF-like 4; calcium-binding
Domain810 – 85748EGF-like 5; calcium-binding
Domain858 – 90043EGF-like 6; calcium-binding
Domain901 – 94242EGF-like 7; calcium-binding
Domain943 – 98139EGF-like 8; calcium-binding
Domain982 – 102443EGF-like 9; calcium-binding
Domain1025 – 106945EGF-like 10; calcium-binding
Region28 – 444417N
Region28 – 177150Subdomain NA (Cys-rich)
Region178 – 444267Subdomain NB (Cys-free)
Region1070 – 1184115Domain III

Amino acid modifications

Modified residue2771Phosphoserine Ref.6
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation3471O-linked (GalNAc...); or Ser-348 Ref.8
Glycosylation3481O-linked (GalNAc...); or Thr-347 Ref.8
Glycosylation5071N-linked (GlcNAc...) Potential
Glycosylation10351N-linked (GlcNAc...) Ref.7
Disulfide bond445 ↔ 472 By similarity
Disulfide bond446 ↔ 479 By similarity
Disulfide bond459 ↔ 480 By similarity
Disulfide bond489 ↔ 518 By similarity
Disulfide bond502 ↔ 519 By similarity
Disulfide bond521 ↔ 545 By similarity
Disulfide bond522 ↔ 552 By similarity
Disulfide bond535 ↔ 553 By similarity
Disulfide bond608 ↔ 620 By similarity
Disulfide bond616 ↔ 629 By similarity
Disulfide bond631 ↔ 644 By similarity
Disulfide bond683 ↔ 693 By similarity
Disulfide bond689 ↔ 702 By similarity
Disulfide bond704 ↔ 717 By similarity
Disulfide bond723 ↔ 736 By similarity
Disulfide bond730 ↔ 745 By similarity
Disulfide bond751 ↔ 762 By similarity
Disulfide bond768 ↔ 781 By similarity
Disulfide bond775 ↔ 790 By similarity
Disulfide bond796 ↔ 808 By similarity
Disulfide bond814 ↔ 827 By similarity
Disulfide bond821 ↔ 836 By similarity
Disulfide bond843 ↔ 856 By similarity
Disulfide bond862 ↔ 875 By similarity
Disulfide bond869 ↔ 884 By similarity
Disulfide bond886 ↔ 899 By similarity
Disulfide bond905 ↔ 917 By similarity
Disulfide bond913 ↔ 926 By similarity
Disulfide bond928 ↔ 941 By similarity
Disulfide bond947 ↔ 956 By similarity
Disulfide bond952 ↔ 965 By similarity
Disulfide bond967 ↔ 980 By similarity
Disulfide bond986 ↔ 998 By similarity
Disulfide bond994 ↔ 1007 By similarity
Disulfide bond1009 ↔ 1023 By similarity
Disulfide bond1029 ↔ 1042 By similarity
Disulfide bond1036 ↔ 1051 By similarity
Disulfide bond1056 ↔ 1068 By similarity

Natural variations

Alternative sequence7181E → EDQDECLMGAHDCSRRQFCV NTLGSFYCVNHTVLCADGYI LNAHRKCV in isoform 2.
VSP_041404
Natural variant451I → V.
Corresponds to variant rs60850813 [ dbSNP | Ensembl ].
VAR_061159
Natural variant1441H → R.
Corresponds to variant rs28587534 [ dbSNP | Ensembl ].
VAR_061160
Natural variant3611S → G.
Corresponds to variant rs3732666 [ dbSNP | Ensembl ].
VAR_059266
Natural variant3871N → T.
Corresponds to variant rs3796318 [ dbSNP | Ensembl ].
VAR_059267
Natural variant8541T → A. Ref.1
Corresponds to variant rs9843344 [ dbSNP | Ensembl ].
VAR_059268
Natural variant11141G → R.
Corresponds to variant rs1061375 [ dbSNP | Ensembl ].
VAR_055722

Experimental info

Sequence conflict1451K → E in CAA57876. Ref.1
Sequence conflict1451K → E in AAN05436. Ref.2
Sequence conflict6641E → G in BAH14261. Ref.3

Sequences

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

Last modified March 3, 2009. Version 2.
Checksum: D46890D93518B343

FASTA1,184126,573
        10         20         30         40         50         60 
MVLLWEPAGA WLALGLALAL GPSVAAAAPR QDCTGVECPP LENCIEEALE PGACCATCVQ 

        70         80         90        100        110        120 
QGCACEGYQY YDCLQGGFVR GRVPAGQSYF VDFGSTECSC PPGGGKISCQ FMLCPELPPN 

       130        140        150        160        170        180 
CIEAVVVADS CPQCGQVGCV HAGHKYAAGH TVHLPPCRAC HCPDAGGELI CYQLPGCHGN 

       190        200        210        220        230        240 
FSDAEEGDPE RHYEDPYSYD QEVAEVEAAT ALGGEVQAGA VQAGAGGPPA ALGGGSQPLS 

       250        260        270        280        290        300 
TIQAPPWPAV LPRPTAAAAL GPPAPVQAKA RRVTEDSEEE EEEEEEREEM AVTEQLAAGG 

       310        320        330        340        350        360 
HRGLDGLPTT APAGPSLPIQ EERAEAGARA EAGARPEENL ILDAQATSRS TGPEGVTHAP 

       370        380        390        400        410        420 
SLGKAALVPT QAVPGSPRDP VKPSPHNILS TSLPDAAWIP PTREVPRKPQ VLPHSHVEED 

       430        440        450        460        470        480 
TDPNSVHSIP RSSPEGSTKD LIETCCAAGQ QWAIDNDECL EIPESGTEDN VCRTAQRHCC 

       490        500        510        520        530        540 
VSYLQEKSCM AGVLGAKEGE TCGAEDNDSC GISLYKQCCD CCGLGLRVRA EGQSCESNPN 

       550        560        570        580        590        600 
LGYPCNHVML SCCEGEEPLI VPEVRRPPEP AAAPRRVSEA EMAGREALSL GTEAELPNSL 

       610        620        630        640        650        660 
PGDDQDECLL LPGELCQHLC INTVGSYHCA CFPGFSLQDD GRTCRPEGHP PQPEAPQEPA 

       670        680        690        700        710        720 
LKSEFSQVAS NTIPLPLPQP NTCKDNGPCK QVCSTVGGSA ICSCFPGYAI MADGVSCEDI 

       730        740        750        760        770        780 
NECVTDLHTC SRGEHCVNTL GSFHCYKALT CEPGYALKDG ECEDVDECAM GTHTCQPGFL 

       790        800        810        820        830        840 
CQNTKGSFYC QARQRCMDGF LQDPEGNCVD INECTSLSEP CRPGFSCINT VGSYTCQRNP 

       850        860        870        880        890        900 
LICARGYHAS DDGTKCVDVN ECETGVHRCG EGQVCHNLPG SYRCDCKAGF QRDAFGRGCI 

       910        920        930        940        950        960 
DVNECWASPG RLCQHTCENT LGSYRCSCAS GFLLAADGKR CEDVNECEAQ RCSQECANIY 

       970        980        990       1000       1010       1020 
GSYQCYCRQG YQLAEDGHTC TDIDECAQGA GILCTFRCLN VPGSYQCACP EQGYTMTANG 

      1030       1040       1050       1060       1070       1080 
RSCKDVDECA LGTHNCSEAE TCHNIQGSFR CLRFECPPNY VQVSKTKCER TTCHDFLECQ 

      1090       1100       1110       1120       1130       1140 
NSPARITHYQ LNFQTGLLVP AHIFRIGPAP AFTGDTIALN IIKGNEEGYF GTRRLNAYTG 

      1150       1160       1170       1180 
VVYLQRAVLE PRDFALDVEM KLWRQGSVTT FLAKMHIFFT TFAL 

« Hide

Isoform 2 [UniParc].

Checksum: 914C7630E2D9FC4E
Show »

FASTA1,231131,863

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS46761.1. [P98095-2]
CCDS46762.1. [P98095-1]
PIRA55184.
RefSeqNP_001004019.1. NM_001004019.1. [P98095-2]
NP_001158507.1. NM_001165035.1. [P98095-2]
NP_001989.2. NM_001998.2. [P98095-1]
UniGeneHs.198862.

3D structure databases

ProteinModelPortalP98095.
SMRP98095. Positions 604-637, 685-1060.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108493. 15 interactions.
IntActP98095. 5 interactions.
MINTMINT-1518617.
STRING9606.ENSP00000384169.

PTM databases

PhosphoSiteP98095.

Polymorphism databases

DMDM224471827.

Proteomic databases

MaxQBP98095.
PaxDbP98095.
PRIDEP98095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295760; ENSP00000295760; ENSG00000163520. [P98095-1]
ENST00000404922; ENSP00000384169; ENSG00000163520. [P98095-2]
ENST00000492059; ENSP00000420042; ENSG00000163520. [P98095-2]
GeneID2199.
KEGGhsa:2199.
UCSCuc011ava.2. human. [P98095-2]
uc011avb.2. human. [P98095-1]

Organism-specific databases

CTD2199.
GeneCardsGC03P013565.
H-InvDBHIX0003076.
HGNCHGNC:3601. FBLN2.
HPACAB018622.
HPA001934.
MIM135821. gene.
neXtProtNX_P98095.
PharmGKBPA28014.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007079.
HOVERGENHBG051559.
KOK17307.
OMASETKCER.
OrthoDBEOG7P5T0C.
PhylomeDBP98095.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP98095.
BgeeP98095.
CleanExHS_FBLN2.
GenevestigatorP98095.

Family and domain databases

InterProIPR000020. 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]
PfamPF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 5 hits.
[Graphical view]
SMARTSM00104. ANATO. 3 hits.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 9 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 5 hits.
PROSITEPS01177. 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]
ProtoNetSearch...

Other

GeneWikiFBLN2.
GenomeRNAi2199.
NextBio8885.
PROP98095.
SOURCESearch...

Entry information

Entry nameFBLN2_HUMAN
AccessionPrimary (citable) accession number: P98095
Secondary accession number(s): B7Z9C5, Q8IUI0, Q8IUI1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 3, 2009
Last modified: July 9, 2014
This is version 136 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 3

Human chromosome 3: entries, gene names and cross-references to MIM