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Q9Y2U8

- MAN1_HUMAN

UniProt

Q9Y2U8 - MAN1_HUMAN

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Protein

Inner nuclear membrane protein Man1

Gene
LEMD3, MAN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi707 – 726201 PublicationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of activin receptor signaling pathway Source: UniProtKB
  2. negative regulation of BMP signaling pathway Source: UniProtKB
  3. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  4. regulation of cell cycle Source: Ensembl
  5. skeletal muscle cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Inner nuclear membrane protein Man1
Alternative name(s):
LEM domain-containing protein 3
Gene namesi
Name:LEMD3
Synonyms:MAN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:28887. LEMD3.

Subcellular locationi

Nucleus inner membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei475 – 49521Helical; Reviewed predictionAdd
BLAST
Transmembranei628 – 64821Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: MGI
  2. integral component of nuclear inner membrane Source: ProtInc
  3. membrane Source: ProtInc
  4. nuclear inner membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Buschke-Ollendorff syndrome (BOS) [MIM:166700]: A disease characterized by osteopoikilosis and disseminated connective-tissue nevi. Osteopoikilosis is a skeletal dysplasia characterized by a symmetric but unequal distribution of multiple hyperostotic areas in different parts of the skeleton. Elastic-type nevi (juvenile elastoma) and collagen-type nevi (dermatofibrosis lenticularis disseminata) have been described in BOS. Skin or bony lesions can be absent in some family members, whereas other relatives may have both.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Melorheostosis (MEL) [MIM:155950]: Rare mesenchymal dysplasia and one of the sclerosing bone disorders. It is caused by a developmental error, with a sclerotomal distribution, frequently involving one limb. It may be asymptomatic, but pain, stiffness with limitation of motion, leg-length discrepancy and limb deformity may occur.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi703 – 7042LI → ED: Impairs binding to SMAD1. Loss of ability to repress transcriptional activation in response to TGF-beta, BMP2 and activin signaling. 1 Publication
Mutagenesisi835 – 8362YV → DD: Impairs binding to SMAD1. 1 Publication

Organism-specific databases

MIMi155950. phenotype.
166700. phenotype.
Orphaneti94063. 12q14 microdeletion syndrome.
1306. Buschke-Ollendorff syndrome.
166119. Isolated osteopoikilosis.
1879. Melorheostosis with osteopoikilosis.
PharmGKBiPA134907442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 911910Inner nuclear membrane protein Man1PRO_0000206149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei141 – 1411Phosphoserine1 Publication
Modified residuei144 – 1441Phosphoserine2 Publications
Modified residuei185 – 1851Phosphoserine1 Publication
Modified residuei187 – 1871Phosphoserine2 Publications
Modified residuei259 – 2591Phosphoserine2 Publications
Modified residuei261 – 2611Phosphoserine3 Publications
Modified residuei280 – 2801Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei365 – 3651Phosphothreonine1 Publication
Modified residuei402 – 4021Phosphoserine2 Publications
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei883 – 8831Phosphothreonine1 Publication
Modified residuei911 – 9111Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2U8.
PaxDbiQ9Y2U8.
PeptideAtlasiQ9Y2U8.
PRIDEiQ9Y2U8.

PTM databases

PhosphoSiteiQ9Y2U8.

Expressioni

Tissue specificityi

Heart, brain, placenta, lung, liver and skeletal muscle.

Gene expression databases

ArrayExpressiQ9Y2U8.
BgeeiQ9Y2U8.
CleanExiHS_LEMD3.
GenevestigatoriQ9Y2U8.

Organism-specific databases

HPAiHPA025078.

Interactioni

Subunit structurei

Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to both phosphorylated and unphosphorylated R-SMADS.2 Publications

Protein-protein interaction databases

BioGridi117127. 9 interactions.
IntActiQ9Y2U8. 7 interactions.
MINTiMINT-1199446.
STRINGi9606.ENSP00000308369.

Structurei

Secondary structure

1
911
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi659 – 6635
Turni664 – 6696
Helixi670 – 68415
Helixi696 – 7016
Helixi709 – 7124
Helixi713 – 72311
Turni724 – 7263
Beta strandi730 – 7378
Beta strandi740 – 7467
Beta strandi751 – 7533
Beta strandi765 – 7684
Beta strandi771 – 7744

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH0NMR-A655-775[»]
ProteinModelPortaliQ9Y2U8.
SMRiQ9Y2U8. Positions 9-49, 653-780, 783-888.

Miscellaneous databases

EvolutionaryTraceiQ9Y2U8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 5045LEMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni699 – 911213Interaction with SMAD1, SMAD2, SMAD3 and SMAD5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 706Poly-Asn
Compositional biasi72 – 8716Ala-richAdd
BLAST
Compositional biasi82 – 876Poly-Ala
Compositional biasi155 – 1584Poly-Gly
Compositional biasi265 – 2684Poly-Asp
Compositional biasi312 – 3154Poly-Gly
Compositional biasi322 – 3254Poly-Ala
Compositional biasi337 – 3404Poly-Ala
Compositional biasi635 – 6406Poly-Leu
Compositional biasi659 – 6624Poly-Glu

Sequence similaritiesi

Contains 1 LEM domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG70255.
HOGENOMiHOG000063699.
HOVERGENiHBG006319.
InParanoidiQ9Y2U8.
OMAiSPIPRYR.
OrthoDBiEOG75J0MP.
PhylomeDBiQ9Y2U8.
TreeFamiTF315385.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR018996. Inner-Nucl-membr_MAN1.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
PF09402. MSC. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y2U8-1 [UniParc]FASTAAdd to Basket

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MAAAAASAPQ QLSDEELFSQ LRRYGLSPGP VTESTRPVYL KKLKKLREEE    50
QQQHRSGGRG NKTRNSNNNN TAAATVAAAG PAAAAAAGMG VRPVSGDLSY 100
LRTPGGLCRI SASGPESLLG GPGGASAAPA AGSKVLLGFS SDESDVEASP 150
RDQAGGGGRK DRASLQYRGL KAPPAPLAAS EVTNSNSAER RKPHSWWGAR 200
RPAGPELQTP PGKDGAVEDE EGEGEDGEER DPETEEPLWA SRTVNGSRLV 250
PYSCRENYSD SEEEDDDDVA SSRQVLKDDS LSRHRPRRTH SKPLPPLTAK 300
SAGGRLETSV QGGGGLAMND RAAAAGSLDR SRNLEEAAAA EQGGGCDQVD 350
SSPVPRYRVN AKKLTPLLPP PLTDMDSTLD SSTGSLLKTN NHIGGGAFSV 400
DSPRIYSNSL PPSAAVAASS SLRINHANHT GSNHTYLKNT YNKPKLSEPE 450
EELLQQFKRE EVSPTGSFSA HYLSMFLLTA ACLFFLILGL TYLGMRGTGV 500
SEDGELSIEN PFGETFGKIQ ESEKTLMMNT LYKLHDRLAQ LAGDHECGSS 550
SQRTLSVQEA AAYLKDLGPE YEGIFNTSLQ WILENGKDVG IRCVGFGPEE 600
ELTNITDVQF LQSTRPLMSF WCRFRRAFVT VTHRLLLLCL GVVMVCVVLR 650
YMKYRWTKEE EETRQMYDMV VKIIDVLRSH NEACQENKDL QPYMPIPHVR 700
DSLIQPHDRK KMKKVWDRAV DFLAANESRV RTETRRIGGA DFLVWRWIQP 750
SASCDKILVI PSKVWQGQAF HLDRRNSPPN SLTPCLKIRN MFDPVMEIGD 800
QWHLAIQEAI LEKCSDNDGI VHIAVDKNSR EGCVYVKCLS PEYAGKAFKA 850
LHGSWFDGKL VTVKYLRLDR YHHRFPQALT SNTPLKPSNK HMNSMSHLRL 900
RTGLTNSQGS S 911
Length:911
Mass (Da):99,997
Last modified:October 1, 2000 - v2
Checksum:i21D1E6BB0D499131
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti260 – 2601D → Y.
Corresponds to variant rs7487311 [ dbSNP | Ensembl ].
VAR_034605

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti508 – 5092IE → K in AAF73293. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF112299 mRNA. Translation: AAD31593.2.
AF263918
, AF180135, AF180136, AF180137, AF180138, AF180139, AF180140, AF180141, AF180142 Genomic DNA. Translation: AAF73293.1.
AL137533 mRNA. Translation: CAB70796.1. Sequence problems.
CCDSiCCDS8972.1.
PIRiT46377.
RefSeqiNP_001161086.1. NM_001167614.1.
NP_055134.2. NM_014319.4.
UniGeneiHs.744150.

Genome annotation databases

EnsembliENST00000308330; ENSP00000308369; ENSG00000174106.
GeneIDi23592.
KEGGihsa:23592.
UCSCiuc001ssl.2. human.

Polymorphism databases

DMDMi13629600.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF112299 mRNA. Translation: AAD31593.2 .
AF263918
, AF180135 , AF180136 , AF180137 , AF180138 , AF180139 , AF180140 , AF180141 , AF180142 Genomic DNA. Translation: AAF73293.1 .
AL137533 mRNA. Translation: CAB70796.1 . Sequence problems.
CCDSi CCDS8972.1.
PIRi T46377.
RefSeqi NP_001161086.1. NM_001167614.1.
NP_055134.2. NM_014319.4.
UniGenei Hs.744150.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CH0 NMR - A 655-775 [» ]
ProteinModelPortali Q9Y2U8.
SMRi Q9Y2U8. Positions 9-49, 653-780, 783-888.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117127. 9 interactions.
IntActi Q9Y2U8. 7 interactions.
MINTi MINT-1199446.
STRINGi 9606.ENSP00000308369.

PTM databases

PhosphoSitei Q9Y2U8.

Polymorphism databases

DMDMi 13629600.

Proteomic databases

MaxQBi Q9Y2U8.
PaxDbi Q9Y2U8.
PeptideAtlasi Q9Y2U8.
PRIDEi Q9Y2U8.

Protocols and materials databases

DNASUi 23592.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308330 ; ENSP00000308369 ; ENSG00000174106 .
GeneIDi 23592.
KEGGi hsa:23592.
UCSCi uc001ssl.2. human.

Organism-specific databases

CTDi 23592.
GeneCardsi GC12P065563.
HGNCi HGNC:28887. LEMD3.
HPAi HPA025078.
MIMi 155950. phenotype.
166700. phenotype.
607844. gene.
neXtProti NX_Q9Y2U8.
Orphaneti 94063. 12q14 microdeletion syndrome.
1306. Buschke-Ollendorff syndrome.
166119. Isolated osteopoikilosis.
1879. Melorheostosis with osteopoikilosis.
PharmGKBi PA134907442.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG70255.
HOGENOMi HOG000063699.
HOVERGENi HBG006319.
InParanoidi Q9Y2U8.
OMAi SPIPRYR.
OrthoDBi EOG75J0MP.
PhylomeDBi Q9Y2U8.
TreeFami TF315385.

Enzyme and pathway databases

Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

EvolutionaryTracei Q9Y2U8.
GenomeRNAii 23592.
NextBioi 46240.
PROi Q9Y2U8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y2U8.
Bgeei Q9Y2U8.
CleanExi HS_LEMD3.
Genevestigatori Q9Y2U8.

Family and domain databases

Gene3Di 1.10.720.40. 1 hit.
3.30.70.330. 1 hit.
InterProi IPR018996. Inner-Nucl-membr_MAN1.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view ]
Pfami PF03020. LEM. 1 hit.
PF09402. MSC. 1 hit.
[Graphical view ]
SMARTi SM00540. LEM. 1 hit.
[Graphical view ]
SUPFAMi SSF63451. SSF63451. 1 hit.
PROSITEi PS50954. LEM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin."
    Lin F., Blake D.L., Callebaut I., Skerjanc I.S., Holmer L., McBurney M.W., Paulin-Levasseur M., Worman H.J.
    J. Biol. Chem. 275:4840-4847(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-911.
    Tissue: Testis.
  3. Cited for: INVOLVEMENT IN BOS AND MEL.
  4. "MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling."
    Lin F., Morrison J.M., Wu W., Worman H.J.
    Hum. Mol. Genet. 14:437-445(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMAD2 AND SMAD3.
  5. "The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines."
    Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.
    J. Biol. Chem. 280:15992-16001(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMAD1; SMAD2; SMAD3 AND SMAD5, MUTAGENESIS OF 703-LEU-ILE-704 AND 835-TYR-VAL-836.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-187; SER-259; SER-261; SER-280; SER-352; THR-365; SER-402; SER-777 AND SER-911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-141; SER-144 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-187 AND THR-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain."
    Caputo S., Couprie J., Duband-Goulet I., Konde E., Lin F., Braud S., Gondry M., Gilquin B., Worman H.J., Zinn-Justin S.
    J. Biol. Chem. 281:18208-18215(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 655-775, DNA-BINDING.

Entry informationi

Entry nameiMAN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2U8
Secondary accession number(s): Q9NT47, Q9NYA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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