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Q9UET6

- TRM7_HUMAN

UniProt

Q9UET6 - TRM7_HUMAN

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Protein
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase
Gene
FTSJ1, JM23
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs By similarity.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei55 – 551S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei75 – 751S-adenosyl-L-methionine By similarity
Binding sitei91 – 911S-adenosyl-L-methionine By similarity
Binding sitei116 – 1161S-adenosyl-L-methionine By similarity
Active sitei156 – 1561Proton acceptor By similarity

GO - Molecular functioni

  1. tRNA methyltransferase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase (EC:2.1.1.205)
Alternative name(s):
2'-O-ribose RNA methyltransferase TRM7 homolog
Protein ftsJ homolog 1
Gene namesi
Name:FTSJ1
ORF Names:JM23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:13254. FTSJ1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 44 (MRX44) [MIM:309549]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi309549. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA28417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseUniRule annotation
PRO_0000155575Add
BLAST

Proteomic databases

MaxQBiQ9UET6.
PaxDbiQ9UET6.
PRIDEiQ9UET6.

PTM databases

PhosphoSiteiQ9UET6.

Expressioni

Tissue specificityi

Found in fetal brain, lung, liver and kidney. In the adult brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus.1 Publication

Gene expression databases

ArrayExpressiQ9UET6.
BgeeiQ9UET6.
CleanExiHS_FTSJ1.
GenevestigatoriQ9UET6.

Organism-specific databases

HPAiHPA002718.

Interactioni

Protein-protein interaction databases

BioGridi117291. 4 interactions.
IntActiQ9UET6. 1 interaction.
STRINGi9606.ENSP00000326948.

Structurei

3D structure databases

ProteinModelPortaliQ9UET6.
SMRiQ9UET6. Positions 20-201.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0293.
HOGENOMiHOG000162368.
HOVERGENiHBG017749.
InParanoidiQ9UET6.
KOiK14864.
OMAiIIRHFEG.
PhylomeDBiQ9UET6.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProiIPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UET6-1) [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

MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA    50
APGSWSQVLS QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE 100
IIQHFKGCPA DLVVCDGAPD VTGLHDVDEY MQAQLLLAAL NIATHVLKPG 150
GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA KPRSSRNSSI EAFAVCQGYD 200
PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD LSSYDSDRSY 250
PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV 300
DTFPQPLAAP QCHTLLAPEM EDNEMSCSP 329
Length:329
Mass (Da):36,079
Last modified:December 1, 2000 - v2
Checksum:i9A85D63A4FA80615
GO
Isoform 2 (identifier: Q9UET6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-220: Missing.

Show »
Length:327
Mass (Da):35,867
Checksum:i54417CCDEB515C55
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 2202Missing in isoform 2.
VSP_041419

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF063015 mRNA. Translation: AAC33734.1.
AJ005892 mRNA. Translation: CAA06749.1.
AK315138 mRNA. Translation: BAG37587.1.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50782.1.
BC023584 mRNA. Translation: AAH23584.1.
CCDSiCCDS14294.1. [Q9UET6-1]
CCDS14295.1. [Q9UET6-2]
RefSeqiNP_001269086.1. NM_001282157.1.
NP_036412.1. NM_012280.3. [Q9UET6-1]
NP_803188.1. NM_177439.2. [Q9UET6-2]
XP_005272652.1. XM_005272595.1. [Q9UET6-2]
UniGeneiHs.23170.

Genome annotation databases

EnsembliENST00000019019; ENSP00000019019; ENSG00000068438. [Q9UET6-2]
ENST00000348411; ENSP00000326948; ENSG00000068438. [Q9UET6-1]
ENST00000456787; ENSP00000415457; ENSG00000068438. [Q9UET6-2]
ENST00000594571; ENSP00000471790; ENSG00000269875. [Q9UET6-2]
ENST00000597753; ENSP00000472739; ENSG00000269875. [Q9UET6-1]
ENST00000601551; ENSP00000470732; ENSG00000269875. [Q9UET6-2]
GeneIDi24140.
KEGGihsa:24140.
UCSCiuc004djn.1. human. [Q9UET6-2]
uc004djo.1. human. [Q9UET6-1]

Polymorphism databases

DMDMi12643879.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF063015 mRNA. Translation: AAC33734.1 .
AJ005892 mRNA. Translation: CAA06749.1 .
AK315138 mRNA. Translation: BAG37587.1 .
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50782.1 .
BC023584 mRNA. Translation: AAH23584.1 .
CCDSi CCDS14294.1. [Q9UET6-1 ]
CCDS14295.1. [Q9UET6-2 ]
RefSeqi NP_001269086.1. NM_001282157.1.
NP_036412.1. NM_012280.3. [Q9UET6-1 ]
NP_803188.1. NM_177439.2. [Q9UET6-2 ]
XP_005272652.1. XM_005272595.1. [Q9UET6-2 ]
UniGenei Hs.23170.

3D structure databases

ProteinModelPortali Q9UET6.
SMRi Q9UET6. Positions 20-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117291. 4 interactions.
IntActi Q9UET6. 1 interaction.
STRINGi 9606.ENSP00000326948.

PTM databases

PhosphoSitei Q9UET6.

Polymorphism databases

DMDMi 12643879.

Proteomic databases

MaxQBi Q9UET6.
PaxDbi Q9UET6.
PRIDEi Q9UET6.

Protocols and materials databases

DNASUi 24140.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000019019 ; ENSP00000019019 ; ENSG00000068438 . [Q9UET6-2 ]
ENST00000348411 ; ENSP00000326948 ; ENSG00000068438 . [Q9UET6-1 ]
ENST00000456787 ; ENSP00000415457 ; ENSG00000068438 . [Q9UET6-2 ]
ENST00000594571 ; ENSP00000471790 ; ENSG00000269875 . [Q9UET6-2 ]
ENST00000597753 ; ENSP00000472739 ; ENSG00000269875 . [Q9UET6-1 ]
ENST00000601551 ; ENSP00000470732 ; ENSG00000269875 . [Q9UET6-2 ]
GeneIDi 24140.
KEGGi hsa:24140.
UCSCi uc004djn.1. human. [Q9UET6-2 ]
uc004djo.1. human. [Q9UET6-1 ]

Organism-specific databases

CTDi 24140.
GeneCardsi GC0XP048334.
HGNCi HGNC:13254. FTSJ1.
HPAi HPA002718.
MIMi 300499. gene.
309549. phenotype.
neXtProti NX_Q9UET6.
Orphaneti 777. X-linked non-syndromic intellectual disability.
PharmGKBi PA28417.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0293.
HOGENOMi HOG000162368.
HOVERGENi HBG017749.
InParanoidi Q9UET6.
KOi K14864.
OMAi IIRHFEG.
PhylomeDBi Q9UET6.
TreeFami TF314897.

Miscellaneous databases

ChiTaRSi FTSJ1. human.
GeneWikii FTSJ1.
GenomeRNAii 24140.
NextBioi 46813.
PROi Q9UET6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UET6.
Bgeei Q9UET6.
CleanExi HS_FTSJ1.
Genevestigatori Q9UET6.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProi IPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10920. PTHR10920. 1 hit.
Pfami PF01728. FtsJ. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human and yeast gene involved in cell division."
    Pengue G., Lutfiyya L.L., Mazzarella R.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Transcription map in Xp11.23."
    Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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).
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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: Lymph.
  7. "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation."
    Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V., Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P., Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.
    Am. J. Hum. Genet. 75:305-309(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRX44, TISSUE SPECIFICITY.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRM7_HUMAN
AccessioniPrimary (citable) accession number: Q9UET6
Secondary accession number(s): B2RCJ0, O75670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: September 3, 2014
This is version 126 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 X
    Human chromosome X: 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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