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Protein

Inner nuclear membrane protein Man1

Gene

LEMD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 72620Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. blood vessel endothelial cell migration involved in intussusceptive angiogenesis Source: Ensembl
  2. negative regulation of activin receptor signaling pathway Source: UniProtKB
  3. negative regulation of BMP signaling pathway Source: UniProtKB
  4. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  5. nucleus organization Source: Ensembl
  6. regulation of cell cycle Source: Ensembl
  7. regulation of extracellular matrix organization Source: Ensembl
  8. 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_263908. 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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:28887. LEMD3.

Subcellular locationi

Nucleus inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei475 – 49521HelicalSequence AnalysisAdd
BLAST
Transmembranei628 – 64821HelicalSequence AnalysisAdd
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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:166700
Melorheostosis (MEL)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare 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.

See also OMIM:155950

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 – 2591Phosphoserine3 Publications
Modified residuei261 – 2611Phosphoserine4 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

BgeeiQ9Y2U8.
CleanExiHS_LEMD3.
ExpressionAtlasiQ9Y2U8. baseline and differential.
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. 23 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 – 6635Combined sources
Turni664 – 6696Combined sources
Helixi670 – 68415Combined sources
Helixi696 – 7016Combined sources
Helixi709 – 7124Combined sources
Helixi713 – 72311Combined sources
Turni724 – 7263Combined sources
Beta strandi730 – 7378Combined sources
Beta strandi740 – 7467Combined sources
Beta strandi751 – 7533Combined sources
Beta strandi765 – 7684Combined sources
Beta strandi771 – 7744Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Y2U8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 5045LEMPROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG70255.
GeneTreeiENSGT00530000063791.
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

« Hide

        10         20         30         40         50
MAAAAASAPQ QLSDEELFSQ LRRYGLSPGP VTESTRPVYL KKLKKLREEE
60 70 80 90 100
QQQHRSGGRG NKTRNSNNNN TAAATVAAAG PAAAAAAGMG VRPVSGDLSY
110 120 130 140 150
LRTPGGLCRI SASGPESLLG GPGGASAAPA AGSKVLLGFS SDESDVEASP
160 170 180 190 200
RDQAGGGGRK DRASLQYRGL KAPPAPLAAS EVTNSNSAER RKPHSWWGAR
210 220 230 240 250
RPAGPELQTP PGKDGAVEDE EGEGEDGEER DPETEEPLWA SRTVNGSRLV
260 270 280 290 300
PYSCRENYSD SEEEDDDDVA SSRQVLKDDS LSRHRPRRTH SKPLPPLTAK
310 320 330 340 350
SAGGRLETSV QGGGGLAMND RAAAAGSLDR SRNLEEAAAA EQGGGCDQVD
360 370 380 390 400
SSPVPRYRVN AKKLTPLLPP PLTDMDSTLD SSTGSLLKTN NHIGGGAFSV
410 420 430 440 450
DSPRIYSNSL PPSAAVAASS SLRINHANHT GSNHTYLKNT YNKPKLSEPE
460 470 480 490 500
EELLQQFKRE EVSPTGSFSA HYLSMFLLTA ACLFFLILGL TYLGMRGTGV
510 520 530 540 550
SEDGELSIEN PFGETFGKIQ ESEKTLMMNT LYKLHDRLAQ LAGDHECGSS
560 570 580 590 600
SQRTLSVQEA AAYLKDLGPE YEGIFNTSLQ WILENGKDVG IRCVGFGPEE
610 620 630 640 650
ELTNITDVQF LQSTRPLMSF WCRFRRAFVT VTHRLLLLCL GVVMVCVVLR
660 670 680 690 700
YMKYRWTKEE EETRQMYDMV VKIIDVLRSH NEACQENKDL QPYMPIPHVR
710 720 730 740 750
DSLIQPHDRK KMKKVWDRAV DFLAANESRV RTETRRIGGA DFLVWRWIQP
760 770 780 790 800
SASCDKILVI PSKVWQGQAF HLDRRNSPPN SLTPCLKIRN MFDPVMEIGD
810 820 830 840 850
QWHLAIQEAI LEKCSDNDGI VHIAVDKNSR EGCVYVKCLS PEYAGKAFKA
860 870 880 890 900
LHGSWFDGKL VTVKYLRLDR YHHRFPQALT SNTPLKPSNK HMNSMSHLRL
910
RTGLTNSQGS S
Length:911
Mass (Da):99,997
Last modified:September 30, 2000 - v2
Checksum:i21D1E6BB0D499131
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti508 – 5092IE → K in AAF73293 (PubMed:10671519).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117127. 23 interactions.
IntActiQ9Y2U8. 7 interactions.
MINTiMINT-1199446.
STRINGi9606.ENSP00000308369.

PTM databases

PhosphoSiteiQ9Y2U8.

Polymorphism databases

DMDMi13629600.

Proteomic databases

MaxQBiQ9Y2U8.
PaxDbiQ9Y2U8.
PeptideAtlasiQ9Y2U8.
PRIDEiQ9Y2U8.

Protocols and materials databases

DNASUi23592.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23592.
GeneCardsiGC12P065563.
HGNCiHGNC:28887. LEMD3.
HPAiHPA025078.
MIMi155950. phenotype.
166700. phenotype.
607844. gene.
neXtProtiNX_Q9Y2U8.
Orphaneti94063. 12q14 microdeletion syndrome.
1306. Buschke-Ollendorff syndrome.
166119. Isolated osteopoikilosis.
1879. Melorheostosis with osteopoikilosis.
PharmGKBiPA134907442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG70255.
GeneTreeiENSGT00530000063791.
HOGENOMiHOG000063699.
HOVERGENiHBG006319.
InParanoidiQ9Y2U8.
OMAiSPIPRYR.
OrthoDBiEOG75J0MP.
PhylomeDBiQ9Y2U8.
TreeFamiTF315385.

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_263908. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

ChiTaRSiLEMD3. human.
EvolutionaryTraceiQ9Y2U8.
GenomeRNAii23592.
NextBioi46240.
PROiQ9Y2U8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2U8.
CleanExiHS_LEMD3.
ExpressionAtlasiQ9Y2U8. baseline and differential.
GenevestigatoriQ9Y2U8.

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]
ProtoNetiSearch...

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(1999) [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(2004) [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(2004) [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(2005) [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(2007) [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(2008) [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(2009) [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(2010) [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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(2005) [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 26, 2001
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.