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Signal Peptide Database - Mammalia
Entry Details
ID
293
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
P98095 (Created: 1995-11-01 Updated: 2008-12-16)
UniProtKB/Swiss-Prot Entry Name
FBLN2_HUMAN
Protein Name
Fibulin-2
Gene
FBLN2
Organism Scientific
Homo sapiens
Organism Common
Human
Lineage
Eukaryota
Metazoa
Chordata
Craniata
Vertebrata
Euteleostomi
Mammalia
Eutheria
Euarchontoglires
Primates
Haplorrhini
Catarrhini
Hominidae
Homo
Protein Length [aa]
1184
Protein Mass [Da]
126544
Features
Type
Description
Status
Start
End
signal peptide
potential
1
27
chain
Fibulin-2
28
1184
disulfide bond
by similarity
445
472
disulfide bond
by similarity
446
479
disulfide bond
by similarity
459
480
disulfide bond
by similarity
489
518
disulfide bond
by similarity
502
519
disulfide bond
by similarity
521
545
disulfide bond
by similarity
522
552
disulfide bond
by similarity
535
553
disulfide bond
by similarity
608
620
disulfide bond
by similarity
616
629
disulfide bond
by similarity
631
644
disulfide bond
by similarity
683
693
disulfide bond
by similarity
689
702
disulfide bond
by similarity
704
717
disulfide bond
by similarity
723
736
disulfide bond
by similarity
730
745
disulfide bond
by similarity
751
762
disulfide bond
by similarity
768
781
disulfide bond
by similarity
775
790
disulfide bond
by similarity
796
808
disulfide bond
by similarity
814
827
disulfide bond
by similarity
821
836
disulfide bond
by similarity
843
856
disulfide bond
by similarity
862
875
disulfide bond
by similarity
869
884
disulfide bond
by similarity
886
899
disulfide bond
by similarity
905
917
disulfide bond
by similarity
913
926
disulfide bond
by similarity
928
941
disulfide bond
by similarity
947
956
disulfide bond
by similarity
952
965
disulfide bond
by similarity
967
980
disulfide bond
by similarity
986
998
disulfide bond
by similarity
994
1007
disulfide bond
by similarity
1009
1023
disulfide bond
by similarity
1029
1042
disulfide bond
by similarity
1036
1051
disulfide bond
by similarity
1056
1068
domain
Anaphylatoxin-like 1
445
480
domain
Anaphylatoxin-like 2
488
519
domain
Anaphylatoxin-like 3
521
553
domain
EGF-like 1; calcium-binding
604
645
domain
EGF-like 2
679
718
domain
EGF-like 3; calcium-binding
719
763
domain
EGF-like 4; calcium-binding
764
809
domain
EGF-like 5; calcium-binding
810
857
domain
EGF-like 6; calcium-binding
858
900
domain
EGF-like 7; calcium-binding
901
942
domain
EGF-like 8; calcium-binding
943
981
domain
EGF-like 9; calcium-binding
982
1024
domain
EGF-like 10; calcium-binding
1025
1069
region of interest
Subdomain NA (Cys-rich)
28
177
region of interest
N
28
444
region of interest
Subdomain NB (Cys-free)
178
444
region of interest
Domain III
1070
1184
modified residue
Phosphoserine
277
277
glycosylation site
N-linked (GlcNAc...)
potential
180
180
glycosylation site
N-linked (GlcNAc...)
potential
507
507
glycosylation site
N-linked (GlcNAc...)
potential
1035
1035
SP Length
27
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MVLLWEPAGAWLALGLALALGPSVAAA
Sequence
MVLLWEPAGAWLALGLALALGPSVAAA
APRQDCTGVECPPLENCIEEALE
PGACCATCVQQGCACEGYQYYDCLQGGFVRGRVPAGQSYFVDFGSTECSC
PPGGGKISCQFMLCPELPPNCIEAVVVADSCPQCGQVGCVHAGHEYAAGH
TVHLPPCRACHCPDAGGELICYQLPGC
HG
N
FSDAEEGDPERHYEDPYSYD
QEVAEVEAATALGGEVQAGAVQAGAGGPPAALGGGSQPLSTIQAPPWPAV
LPRPTAAAALGPPAPVQAKARRVTED
S
EEEEEEEEEREEMAVTEQLAAGG
HRGLDGLPTTAPAGPSLPIQEERAEAGARAEAGARPEENLILDAQATSRS
TGPEGVTHAPSLGKAALVPTQAVPGSPRDPVKPSPHNILSTSLPDAAWIP
PTREVPRKPQVLPHSHVEEDTDPNSVHSIPRSSPEGSTKDLIET
CCAAGQ
QWAIDNDECLEIPESGTEDNVCRTAQRHCC
VSYLQEK
SCMAGVLGAKEGE
TCGAED
N
DSCGISLYKQCC
D
CCGLGLRVRAEGQSCESNPNLGYPCNHVML
SCC
EGEEPLIVPEVRRPPEPAAAPRRVSEAEMAGREALSLGTEAELPNSL
PGD
DQDECLLLPGELCQHLCINTVGSYHCACFPGFSLQDDGRTCR
PEGHP
PQPEAPQEPALKSEFSQVASNTIPLPLP
QPNTCKDNGPCKQVCSTVGGSA
ICSCFPGYAIMADGVSCE
DINECVTDLHTCSRGEHCVNTLGSFHCYKALT
CEPGYALKDGECE
DVDECAMGTHTCQPGFLCQNTKGSFYCQARQRCMDGF
LQDPEGNCV
DINECTSLSEPCRPGFSCINTVGSYTCQRNPLICARGYHAS
DDGAKCV
DVNECETGVHRCGEGQVCHNLPGSYRCDCKAGFQRDAFGRGCI
DVNECWASPGRLCQHTCENTLGSYRCSCASGFLLAADGKRCE
DVNECEAQ
RCSQECANIYGSYQCYCRQGYQLAEDGHTCT
DIDECAQGAGILCTFRCLN
VPGSYQCACPEQGYTMTANGRSCK
DVDECALGTH
N
CSEAETCHNIQGSFR
CLRFECPPNYVQVSKTKCE
RTTCHDFLECQNSPARITHYQLNFQTGLLVP
AHIFRIGPAPAFTGDTIALNIIKGNEEGYFGTRRLNAYTGVVYLQRAVLE
PRDFALDVEMKLWRQGSVTTFLAKMHIFFTTFAL
Original
MVLLWEPAGAWLALGLALALGPSVAAAAPRQDCTGVECPPLENCIEEALE
PGACCATCVQQGCACEGYQYYDCLQGGFVRGRVPAGQSYFVDFGSTECSC
PPGGGKISCQFMLCPELPPNCIEAVVVADSCPQCGQVGCVHAGHEYAAGH
TVHLPPCRACHCPDAGGELICYQLPGCHGNFSDAEEGDPERHYEDPYSYD
QEVAEVEAATALGGEVQAGAVQAGAGGPPAALGGGSQPLSTIQAPPWPAV
LPRPTAAAALGPPAPVQAKARRVTEDSEEEEEEEEEREEMAVTEQLAAGG
HRGLDGLPTTAPAGPSLPIQEERAEAGARAEAGARPEENLILDAQATSRS
TGPEGVTHAPSLGKAALVPTQAVPGSPRDPVKPSPHNILSTSLPDAAWIP
PTREVPRKPQVLPHSHVEEDTDPNSVHSIPRSSPEGSTKDLIETCCAAGQ
QWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCMAGVLGAKEGE
TCGAEDNDSCGISLYKQCCDCCGLGLRVRAEGQSCESNPNLGYPCNHVML
SCCEGEEPLIVPEVRRPPEPAAAPRRVSEAEMAGREALSLGTEAELPNSL
PGDDQDECLLLPGELCQHLCINTVGSYHCACFPGFSLQDDGRTCRPEGHP
PQPEAPQEPALKSEFSQVASNTIPLPLPQPNTCKDNGPCKQVCSTVGGSA
ICSCFPGYAIMADGVSCEDINECVTDLHTCSRGEHCVNTLGSFHCYKALT
CEPGYALKDGECEDVDECAMGTHTCQPGFLCQNTKGSFYCQARQRCMDGF
LQDPEGNCVDINECTSLSEPCRPGFSCINTVGSYTCQRNPLICARGYHAS
DDGAKCVDVNECETGVHRCGEGQVCHNLPGSYRCDCKAGFQRDAFGRGCI
DVNECWASPGRLCQHTCENTLGSYRCSCASGFLLAADGKRCEDVNECEAQ
RCSQECANIYGSYQCYCRQGYQLAEDGHTCTDIDECAQGAGILCTFRCLN
VPGSYQCACPEQGYTMTANGRSCKDVDECALGTHNCSEAETCHNIQGSFR
CLRFECPPNYVQVSKTKCERTTCHDFLECQNSPARITHYQLNFQTGLLVP
AHIFRIGPAPAFTGDTIALNIIKGNEEGYFGTRRLNAYTGVVYLQRAVLE
PRDFALDVEMKLWRQGSVTTFLAKMHIFFTTFAL
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
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, Dresden, Germany, last update 2010-06-11