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Q9UHJ3

- SMBT1_HUMAN

UniProt

Q9UHJ3 - SMBT1_HUMAN

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Protein
Scm-like with four MBT domains protein 1
Gene
SFMBT1, RU1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis.3 Publications

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. chromatin modification Source: UniProtKB-KW
  3. negative regulation of muscle organ development Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. spermatogenesis Source: UniProtKB-KW
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Differentiation, Spermatogenesis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Scm-like with four MBT domains protein 1
Short name:
hSFMBT
Alternative name(s):
Renal ubiquitous protein 1
Gene namesi
Name:SFMBT1
Synonyms:RU1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:20255. SFMBT1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731F → A: Reduced histone-binding. 1 Publication
Mutagenesisi180 – 1801W → A: Abolishes histone-binding. 1 Publication
Mutagenesisi196 – 1961Y → A: Reduced histone-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134898464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866Scm-like with four MBT domains protein 1
PRO_0000071966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei775 – 7751Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UHJ3.
PaxDbiQ9UHJ3.
PRIDEiQ9UHJ3.

PTM databases

PhosphoSiteiQ9UHJ3.

Expressioni

Tissue specificityi

Expressed in all cell lines and normal tissues tested, including the thymus.1 Publication

Gene expression databases

ArrayExpressiQ9UHJ3.
BgeeiQ9UHJ3.
CleanExiHS_SFMBT1.
GenevestigatoriQ9UHJ3.

Organism-specific databases

HPAiHPA036153.

Interactioni

Subunit structurei

Interacts with MYOD1 By similarity. Component of the SLC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and RCOR1/CoREST.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST3H3Q166954EBI-747398,EBI-358900

Protein-protein interaction databases

BioGridi119553. 8 interactions.
IntActiQ9UHJ3. 10 interactions.
MINTiMINT-1448033.
STRINGi9606.ENSP00000350789.

Structurei

3D structure databases

ProteinModelPortaliQ9UHJ3.
SMRiQ9UHJ3. Positions 14-530, 796-857.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 120101MBT 1
Add
BLAST
Repeati128 – 232105MBT 2
Add
BLAST
Repeati242 – 348107MBT 3
Add
BLAST
Repeati356 – 45398MBT 4
Add
BLAST
Domaini796 – 86469SAM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 429Antigenic epitope

Domaini

The MBT repeats mediate binding to histones tails; however, in contrast to other MBT repeats, does not bind specific histone lysine modifications. The MBT repeats lack the conserved Asp and aromatic cage at conserved positions (1 Publication).

Sequence similaritiesi

Contains 4 MBT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG316861.
HOGENOMiHOG000004859.
HOVERGENiHBG085238.
InParanoidiQ9UHJ3.
OMAiKCSENCS.
OrthoDBiEOG780RKN.
PhylomeDBiQ9UHJ3.
TreeFamiTF316498.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamiPF12140. DUF3588. 1 hit.
PF02820. MBT. 4 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 4 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHJ3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNGEQQLDAD AGSGMEEVEL SWEDYLEETG STAVPYGSFK HVDTRLQNGF    50
APGMKLEVAV RTDPETYWVA TVITTCEQLL LLRYDGYGED RRADFWCDIR 100
KADLYPIGWC EQNKKTLEAP EGIRDKVSDW DEFLRQTLIG ACSPPVPLLE 150
GLRNGRNPLD LIAPGSRLEC QAFQDSLSTW IVTVVENIGG RLKLRYEGLE 200
SSDNYEHWLY YLDPFLHHVG WAAQQGYELQ PPSAIRHLKN EAEWQEILAK 250
VKEEEEEPLP SYLFKDKQVI GIHTFSVNMK LEAVDPWSPF GISPATVVKV 300
FDEKYFLVEM DDLRPENHAR RSFVCHADSP GIFPVQWSLK NGLHISPPPG 350
YPSQDFDWAD YLKQCGAEAA PQRCFPPLIS EHEFKENMKL EAVNPILPEE 400
VCVATITAVR GSYLWLQLEG SKKPIPECIV SVESMDIFPL GWCETNGHPL 450
STPRRARVYK QRKIAVVQPE KQVPSSRTVH EGLRNQELNS TESVMINGKY 500
CCPKIYFNHR CFSGPYLNKG RIAELPQCVG PGNCVLVLRE VLTLLINAAY 550
KPSRVLRELQ LDKDSVWHGC GEVLKAKYKG KSYRATVEIV KTADRVTEFC 600
RQTCIKLECC PNLFGPRMVL DKCSENCSVL TKTKYTHYYG KKKNKRIGRP 650
PGGHSNLACA LKKASKRRKR RKNVFVHKKK RSSASVDNTP AGSPQGSGGE 700
DEDDPDEGDD DSLSEGSTSE QQDELQEESE MSEKKSCSSS PTQSEISTSL 750
PPDRQRRKRE LRTFSFSDDE NKPPSPKEIR IEVAERLHLD SNPLKWSVAD 800
VVRFIRSTDC APLARIFLDQ EIDGQALLLL TLPTVQECMD LKLGPAIKLC 850
HHIERIKFAF YEQFAN 866
Length:866
Mass (Da):98,141
Last modified:June 7, 2005 - v2
Checksum:iDCE67BF35C413EB7
GO
Isoform 2 (identifier: Q9UHJ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     778-820: Missing.

Show »
Length:823
Mass (Da):93,166
Checksum:i896FEF37B9FCCECF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei778 – 82043Missing in isoform 2.
VSP_013857Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti642 – 6421K → R in AAF19794. 1 Publication
Sequence conflicti767 – 7671S → F in AAF19794. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF168132 mRNA. Translation: AAF19794.1.
AB189472 mRNA. Translation: BAE43835.1.
AK313965 mRNA. Translation: BAG36680.1.
AC099667 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65272.1.
BC014614 mRNA. Translation: AAH14614.1.
AL080140 mRNA. Translation: CAB45734.1.
CCDSiCCDS2867.1. [Q9UHJ3-1]
PIRiT12525.
RefSeqiNP_057413.2. NM_016329.3. [Q9UHJ3-1]
XP_005265278.1. XM_005265221.1. [Q9UHJ3-1]
XP_006713266.1. XM_006713203.1. [Q9UHJ3-1]
XP_006713267.1. XM_006713204.1. [Q9UHJ3-1]
UniGeneiHs.343679.

Genome annotation databases

EnsembliENST00000296295; ENSP00000296295; ENSG00000163935. [Q9UHJ3-2]
ENST00000358080; ENSP00000350789; ENSG00000163935. [Q9UHJ3-1]
ENST00000394750; ENSP00000378233; ENSG00000163935. [Q9UHJ3-1]
ENST00000394752; ENSP00000378235; ENSG00000163935. [Q9UHJ3-1]
GeneIDi51460.
KEGGihsa:51460.
UCSCiuc003dgh.3. human. [Q9UHJ3-1]
uc010hmr.3. human. [Q9UHJ3-2]

Polymorphism databases

DMDMi67461585.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF168132 mRNA. Translation: AAF19794.1 .
AB189472 mRNA. Translation: BAE43835.1 .
AK313965 mRNA. Translation: BAG36680.1 .
AC099667 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65272.1 .
BC014614 mRNA. Translation: AAH14614.1 .
AL080140 mRNA. Translation: CAB45734.1 .
CCDSi CCDS2867.1. [Q9UHJ3-1 ]
PIRi T12525.
RefSeqi NP_057413.2. NM_016329.3. [Q9UHJ3-1 ]
XP_005265278.1. XM_005265221.1. [Q9UHJ3-1 ]
XP_006713266.1. XM_006713203.1. [Q9UHJ3-1 ]
XP_006713267.1. XM_006713204.1. [Q9UHJ3-1 ]
UniGenei Hs.343679.

3D structure databases

ProteinModelPortali Q9UHJ3.
SMRi Q9UHJ3. Positions 14-530, 796-857.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119553. 8 interactions.
IntActi Q9UHJ3. 10 interactions.
MINTi MINT-1448033.
STRINGi 9606.ENSP00000350789.

Chemistry

ChEMBLi CHEMBL1764944.

PTM databases

PhosphoSitei Q9UHJ3.

Polymorphism databases

DMDMi 67461585.

Proteomic databases

MaxQBi Q9UHJ3.
PaxDbi Q9UHJ3.
PRIDEi Q9UHJ3.

Protocols and materials databases

DNASUi 51460.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296295 ; ENSP00000296295 ; ENSG00000163935 . [Q9UHJ3-2 ]
ENST00000358080 ; ENSP00000350789 ; ENSG00000163935 . [Q9UHJ3-1 ]
ENST00000394750 ; ENSP00000378233 ; ENSG00000163935 . [Q9UHJ3-1 ]
ENST00000394752 ; ENSP00000378235 ; ENSG00000163935 . [Q9UHJ3-1 ]
GeneIDi 51460.
KEGGi hsa:51460.
UCSCi uc003dgh.3. human. [Q9UHJ3-1 ]
uc010hmr.3. human. [Q9UHJ3-2 ]

Organism-specific databases

CTDi 51460.
GeneCardsi GC03M052913.
HGNCi HGNC:20255. SFMBT1.
HPAi HPA036153.
MIMi 607319. gene.
neXtProti NX_Q9UHJ3.
PharmGKBi PA134898464.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316861.
HOGENOMi HOG000004859.
HOVERGENi HBG085238.
InParanoidi Q9UHJ3.
OMAi KCSENCS.
OrthoDBi EOG780RKN.
PhylomeDBi Q9UHJ3.
TreeFami TF316498.

Miscellaneous databases

ChiTaRSi SFMBT1. human.
GenomeRNAii 51460.
NextBioi 55079.
PROi Q9UHJ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UHJ3.
Bgeei Q9UHJ3.
CleanExi HS_SFMBT1.
Genevestigatori Q9UHJ3.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
InterProi IPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view ]
Pfami PF12140. DUF3588. 1 hit.
PF02820. MBT. 4 hits.
PF00536. SAM_1. 1 hit.
[Graphical view ]
SMARTi SM00561. MBT. 4 hits.
SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
PROSITEi PS51079. MBT. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells."
    Morel S., Levy F., Burlet-Schiltz O., Brasseur F., Probst-Kepper M., Peitrequin A.L., Monsarrat B., Van Velthoven R., Cerottini J.C., Boon T., Gairin J.E., Van den Eynde B.J.
    Immunity 12:107-117(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "SFMBT and H-L(3)MBT interact with each other and regulate HOX expression and cell proliferation."
    Usui H., Ichikawa T., Kobayashi K., Kumanishi T.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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 1).
    Tissue: Testis.
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Muscle.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-866 (ISOFORM 2).
    Tissue: Testis.
  8. "Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3."
    Wu S., Trievel R.C., Rice J.C.
    FEBS Lett. 581:3289-3296(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "SFMBT1 functions with LSD1 to regulate expression of canonical histone genes and chromatin-related factors."
    Zhang J., Bonasio R., Strino F., Kluger Y., Holloway J.K., Modzelewski A.J., Cohen P.E., Reinberg D.
    Genes Dev. 27:749-766(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KDM1A AND RCOR1, IDENTIFICATION IN THE SLC COMPLEX, MUTAGENESIS OF PHE-173; TRP-180 AND TYR-196.
  11. "Proteomic and functional analyses reveal the role of chromatin reader SFMBT1 in regulating epigenetic silencing and the myogenic gene program."
    Lin S., Shen H., Li J.L., Tang S., Gu Y., Chen Z., Hu C., Rice J.C., Lu J., Wu L.
    J. Biol. Chem. 288:6238-6247(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN VARIOUS COREPRESSOR COMPLEX.

Entry informationi

Entry nameiSMBT1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHJ3
Secondary accession number(s): Q402F7, Q96C73, Q9Y4Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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