Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P97927

- LAMA4_MOUSE

UniProt

P97927 - LAMA4_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Laminin subunit alpha-4

Gene

Lama4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

GO - Biological processi

  1. blood vessel development Source: MGI
  2. brown fat cell differentiation Source: MGI
  3. cell adhesion Source: UniProtKB-KW
  4. regulation of cell adhesion Source: InterPro
  5. regulation of cell migration Source: InterPro
  6. regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-4
Alternative name(s):
Laminin-14 subunit alpha
Laminin-8 subunit alpha
Laminin-9 subunit alpha
Gene namesi
Name:Lama4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:109321. Lama4.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: MGI
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: Ensembl
  5. laminin-1 complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 18161792Laminin subunit alpha-4PRO_0000017061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 91By similarity
Disulfide bondi84 ↔ 98By similarity
Disulfide bondi101 ↔ 110By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi113 ↔ 129By similarity
Disulfide bondi132 ↔ 146By similarity
Disulfide bondi134 ↔ 155By similarity
Disulfide bondi157 ↔ 166By similarity
Disulfide bondi169 ↔ 184By similarity
Disulfide bondi187 ↔ 202By similarity
Disulfide bondi189 ↔ 209By similarity
Disulfide bondi212 ↔ 221By similarity
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi224 ↔ 238By similarity
Disulfide bondi266 – 266InterchainCurated
Disulfide bondi269 – 269InterchainCurated
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi639 – 6391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi735 – 7351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi754 – 7541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi803 – 8031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1000 ↔ 1030By similarity
Glycosylationi1088 – 10881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1196 ↔ 1222By similarity
Glycosylationi1283 – 12831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1361 – 13611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1365 ↔ 1397By similarity
Disulfide bondi1610 ↔ 1633By similarity
Disulfide bondi1785 ↔ 1813By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP97927.
PaxDbiP97927.
PRIDEiP97927.

PTM databases

PhosphoSiteiP97927.

Expressioni

Tissue specificityi

Strongly expressed in peripheral nerves, cardiac muscle, fat, dermis, lung stroma, aortic endothelium, endocardium and endothelium of blood vessels in skin and brain.

Gene expression databases

BgeeiP97927.
CleanExiMM_LAMA4.
ExpressionAtlasiP97927. baseline and differential.
GenevestigatoriP97927.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423).

Protein-protein interaction databases

IntActiP97927. 1 interaction.
MINTiMINT-4100077.

Structurei

3D structure databases

ProteinModelPortaliP97927.
SMRiP97927. Positions 9-300, 829-1373, 1450-1815.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 13150Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 18655Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 24054Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini241 – 25515Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini826 – 1030205Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1042 – 1222181Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini1229 – 1397169Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1462 – 1633172Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini1640 – 1813174Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 825570Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili431 – 52393Sequence AnalysisAdd
BLAST
Coiled coili556 – 60449Sequence AnalysisAdd
BLAST
Coiled coili655 – 71763Sequence AnalysisAdd
BLAST
Coiled coili770 – 79930Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi717 – 7193Cell attachment siteSequence Analysis

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain G is globular.

Sequence similaritiesi

Contains 4 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG247347.
GeneTreeiENSGT00760000119121.
HOGENOMiHOG000113278.
HOVERGENiHBG052299.
InParanoidiP97927.
KOiK06241.
OMAiPKPVDHR.
OrthoDBiEOG7VX8V2.
PhylomeDBiP97927.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
[Graphical view]
PfamiPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 6 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P97927-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGWSTAWCSV LALWLLWCAV CSNAASGDGN AFPFDIEGSA VVGRQDPSET
60 70 80 90 100
SDSGVTLGRL PPAAERCDAG FFRTLSGECA PCDCNGNSHE CLDGSGFCLH
110 120 130 140 150
CQRNTTGEHC EKCLDGYIGD SIRGTPRFCQ PCPCPLPHLA NFAESCYRKN
160 170 180 190 200
GAVRCICKEN YVGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE
210 220 230 240 250
DCDEITGQCR NCLRNTTGFK CERCAPGYYG DARTAKNCAV CNCGGGPCDS
260 270 280 290 300
VTGECLEEGF EVPTGCDKCV WDLTDDLRLA ALSIEESKSG LLSVSSGAAA
310 320 330 340 350
HRHVTDMNST IHLLRTRLSE RENQYTLRKI QINNSENTLR SLLPDVEGLH
360 370 380 390 400
EKGSQASRKG MLVEKESMDT IDQATHLVEQ AHNMRDKIQE INSKMLYYGE
410 420 430 440 450
NQELGPEEIA EKLVLAQKML EEIRSRQPFL THRELVDEEA DEAQELLSQA
460 470 480 490 500
ENWQRLHNDT RSLFPVVLEQ LDDYNAKLSD LQESINQALD HVRDAEDMNR
510 520 530 540 550
AITFKQRDHE KQHERVKEQM EVVGASLSMS ADSLTIPQLT LEELDEIIKN
560 570 580 590 600
ASGIYAEIDG AKNELQGKLS NLSNLSHDLV QEATDHAYNL QQEADELSRN
610 620 630 640 650
LHSSDMNGLV QKALDASNVY ENIANYVSEA NETAELALNI TDRIYDAVSG
660 670 680 690 700
IDTQIIYHKD ESDNLLNQAR ELQAKADSSN DEAVADTSRR VGGALWRKGA
710 720 730 740 750
LRDRLNDAVK QLQAAERGDA HQRLGQSKLF IEEANKTTAA VQQVTTPMAN
760 770 780 790 800
NLSNWSQNLQ TFDSSAYNTA VDSARDAVRN LTEVVPQLLD QLRTVEQKRP
810 820 830 840 850
ASNISASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH PKVSVDDLKA
860 870 880 890 900
FTSISLYMKP PPKPAEPTGA WVADQFVLYL GSKNAKKEYM GLAIKNDNLV
910 920 930 940 950
YVYNLGMKDV EILLDSKPVS SWPAYFSIVK IERVGKHGKV FLTVPSLSST
960 970 980 990 1000
AEEKFIKKGE FAGDDSLLDL TPEDTVFYVG GVPANFKLPA SLNLPSYSGC
1010 1020 1030 1040 1050
LELATLNNDV ISLYNFKHIY NMDPSKSVPC ARDKLAFTQS RAASYFFDGS
1060 1070 1080 1090 1100
SYAVVRDITR RGKFGQVTRF DIEIRTPADN GLVLLMVNGS MFFSLEMRNG
1110 1120 1130 1140 1150
YLHVFYDFGF SNGPVHLEDT LKKAQINDAK YHEISIIYHN DKKMILVVDR
1160 1170 1180 1190 1200
RHVKSTDNEK KKIPFTDIYI GGAPQEVLQS RTLRAHLPLD INFRGCMKGF
1210 1220 1230 1240 1250
QFQKKDFNLL EQTETLGVGY GCPEDSLISR RAYFNGQSFI ASIQKISFFD
1260 1270 1280 1290 1300
GFEGGFNFRT LQPNGLLFYY TSGSDVFSIS LDNGTVVMDV KGIKVMSTDK
1310 1320 1330 1340 1350
QYHDGLPHFV VTSISDTRYE LVVDKSRLRG KNPTKGKAEQ TQTTEKKFYF
1360 1370 1380 1390 1400
GGSPISPQYA NFTGCISNAY FTRLDRDVEV EDFQRYSEKV HTSLYECPIE
1410 1420 1430 1440 1450
SSPLFLLHKK GKNSSKPKTN KQGEKSKDAP SWDPIGLKFL EQKAPRDSHC
1460 1470 1480 1490 1500
HLSSSPRAIE HAYQYGGTAN SRQEFEHEQG DFGEKSQFAI RLKTRSSHGM
1510 1520 1530 1540 1550
IFYVSDQEEN DFMTLFLAHG RLVFMFNVGH KKLKIRSQEK YNDGLWHDVI
1560 1570 1580 1590 1600
FIREKSSGRL VIDGLRVLEE RLPPSGAAWK IKGPIYLGGV APGRAVKNVQ
1610 1620 1630 1640 1650
ITSVYSFSGC LGNLQLNGAS ITSASQTFSV TPCFEGPMET GTYFSTEGGY
1660 1670 1680 1690 1700
VVLDESFNIG LKFEIAFEVR PRSSSGTLVH GHSVNGEYLN VHMRNGQVIV
1710 1720 1730 1740 1750
KVNNGVRDFS TSVTPKQNLC DGRWHRITVI RDSNVVQLDV DSEVNHVVGP
1760 1770 1780 1790 1800
LNPKPVDHRE PVFVGGVPES LLTPRLAPSK PFTGCIRHFV IDSRPVSFSK
1810
AALVSGAVSI NSCPTA
Length:1,816
Mass (Da):201,819
Last modified:December 13, 2001 - v2
Checksum:iB49C45F3A45999D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81C → S in AAC52982. (PubMed:9049981)Curated
Sequence conflicti18 – 181C → Y(PubMed:9049981)Curated
Sequence conflicti248 – 2481C → R in AAC24725. (PubMed:9346933)Curated
Sequence conflicti297 – 2971G → A in AAC24725. (PubMed:9346933)Curated
Sequence conflicti431 – 4333THR → HPS in AAC52982. (PubMed:9049981)Curated
Sequence conflicti679 – 6791S → C in AAC24725. (PubMed:9346933)Curated
Sequence conflicti703 – 7031D → G in AAC52982. (PubMed:9049981)Curated
Sequence conflicti706 – 7061N → H in AAC52982. (PubMed:9049981)Curated
Sequence conflicti728 – 7281K → R(PubMed:9049981)Curated
Sequence conflicti730 – 7301F → I(PubMed:9049981)Curated
Sequence conflicti779 – 7791R → G AA sequence (PubMed:9219532)Curated
Sequence conflicti810 – 8101R → S in AAC24725. (PubMed:9346933)Curated
Sequence conflicti865 – 8673AEP → QT in AAC52982. (PubMed:9049981)Curated
Sequence conflicti936 – 9361K → E in AAC24725. (PubMed:9346933)Curated
Sequence conflicti970 – 9701L → V in AAC24725. (PubMed:9346933)Curated
Sequence conflicti1132 – 11321H → R in AAC52982. (PubMed:9049981)Curated
Sequence conflicti1200 – 12001F → I in AAC52982. (PubMed:9049981)Curated
Sequence conflicti1382 – 13821D → A in AAC52982. (PubMed:9049981)Curated
Sequence conflicti1413 – 14142NS → EF in CAA70970. (PubMed:9219532)Curated
Sequence conflicti1489 – 14891A → S in AAC52982. (PubMed:9049981)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58950 mRNA. Translation: AAB41840.1.
Y09827 mRNA. Translation: CAA70970.1.
U59865 mRNA. Translation: AAC24725.1.
BC115942 mRNA. Translation: AAI15943.1.
U88352 mRNA. Translation: AAC53178.1.
U69176 mRNA. Translation: AAC52982.1.
CCDSiCCDS35882.1.
RefSeqiNP_034811.2. NM_010681.4.
UniGeneiMm.258065.

Genome annotation databases

EnsembliENSMUST00000019992; ENSMUSP00000019992; ENSMUSG00000019846.
GeneIDi16775.
KEGGimmu:16775.
UCSCiuc007evq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58950 mRNA. Translation: AAB41840.1 .
Y09827 mRNA. Translation: CAA70970.1 .
U59865 mRNA. Translation: AAC24725.1 .
BC115942 mRNA. Translation: AAI15943.1 .
U88352 mRNA. Translation: AAC53178.1 .
U69176 mRNA. Translation: AAC52982.1 .
CCDSi CCDS35882.1.
RefSeqi NP_034811.2. NM_010681.4.
UniGenei Mm.258065.

3D structure databases

ProteinModelPortali P97927.
SMRi P97927. Positions 9-300, 829-1373, 1450-1815.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97927. 1 interaction.
MINTi MINT-4100077.

PTM databases

PhosphoSitei P97927.

Proteomic databases

MaxQBi P97927.
PaxDbi P97927.
PRIDEi P97927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019992 ; ENSMUSP00000019992 ; ENSMUSG00000019846 .
GeneIDi 16775.
KEGGi mmu:16775.
UCSCi uc007evq.2. mouse.

Organism-specific databases

CTDi 3910.
MGIi MGI:109321. Lama4.

Phylogenomic databases

eggNOGi NOG247347.
GeneTreei ENSGT00760000119121.
HOGENOMi HOG000113278.
HOVERGENi HBG052299.
InParanoidi P97927.
KOi K06241.
OMAi PKPVDHR.
OrthoDBi EOG7VX8V2.
PhylomeDBi P97927.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMA4. mouse.
NextBioi 290616.
PROi P97927.
SOURCEi Search...

Gene expression databases

Bgeei P97927.
CleanExi MM_LAMA4.
ExpressionAtlasi P97927. baseline and differential.
Genevestigatori P97927.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 6 hits.
PROSITEi PS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
    Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
    Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 462-469; 478-483; 776-782 AND 940-945.
    Strain: BALB/c.
    Tissue: Endothelial cell.
  2. "The complete cDNA coding sequence and tissue-specific expression of the mouse laminin alpha 4 chain."
    Liu J., Mayne R.
    Matrix Biol. 15:433-437(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. "Primary structure, developmental expression, and immunolocalization of the murine laminin alpha4 chain."
    Iivanainen A., Kortesmaa J., Sahlberg C., Morita T., Bergmann U., Thesleff I., Tryggvason K.
    J. Biol. Chem. 272:27862-27868(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  4. "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].
  5. "The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform."
    Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R.
    J. Cell Biol. 137:685-701(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 836-1106.
    Strain: ICR.
    Tissue: Placenta.
  6. "Distribution of the ten known laminin chains in the pathways and targets of developing sensory axons."
    Lentz S.I., Miner J.H., Sanes J.R., Snider W.D.
    J. Comp. Neurol. 378:547-561(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1467-1691.
    Tissue: Placenta.

Entry informationi

Entry nameiLAMA4_MOUSE
AccessioniPrimary (citable) accession number: P97927
Secondary accession number(s): O88785, P70409, Q14BF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: October 29, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3