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Q9NPD8 (UBE2T_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 T

EC=6.3.2.19
Alternative name(s):
Cell proliferation-inducing gene 50 protein
Ubiquitin carrier protein T
Ubiquitin-protein ligase T
Gene names
Name:UBE2T
ORF Names:HSPC150, PIG50
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with FANCL and BRCA1. Ref.9 Ref.10 Ref.11 Ref.13 Ref.17

Subcellular location

Nucleus. Note: Accumulates to chromatin. Ref.10 Ref.13

Induction

Down-regulated following hypoxia. Up-regulated in breast cancers. Ref.18

Post-translational modification

Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91 and Lys-182 are unclear: according to a report, monoubiquitination inactivates E2 enzyme activity (Ref.9). In contrast, according to another report, autoubiquitination does not affect E2 enzyme activity (Ref.11).

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein K27-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein K29-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein K6-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.9Ref.11. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay Ref.9Ref.10Ref.11. Source: UniProtKB

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.10. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay Ref.10. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.9Ref.10Ref.11. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.9Ref.10Ref.11Ref.15. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Ubiquitin-conjugating enzyme E2 T
PRO_0000082509

Sites

Active site861Glycyl thioester intermediate

Amino acid modifications

Cross-link91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.11
Cross-link182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Experimental info

Mutagenesis631F → A: Decreased binding to FANCL. Ref.17
Mutagenesis861C → A: Loss of E2 enzyme activity. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Mutagenesis911K → R: Decreased monoubiquitination. Ref.11
Mutagenesis182 – 19110Missing: Decreased monoubiquitination. Ref.11

Secondary structure

........................ 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NPD8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6C02D774A7FA928A

FASTA19722,521
        10         20         30         40         50         60 
MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV FKLEVIIPER 

        70         80         90        100        110        120 
YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP SLNIATVLTS IQLLMSEPNP 

       130        140        150        160        170        180 
DDPLMADISS EFKYNKPAFL KNARQWTEKH ARQKQKADEE EMLDNLPEAG DSRVHNSTQK 

       190 
RKASQLVGIE KKFHPDV 

« Hide

References

« Hide 'large scale' references
[1]"Ubiquitin-conjugating enzyme isolog."
Okaze H., Hayashi A., Kozuma S., Saito T.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[4]"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. expand/collapse author list , 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].
Tissue: Carcinoma.
[5]"Identification of a human cell proliferation inducing gene."
Kim J.W.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Lung.
[9]"UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation."
Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M., D'Andrea A.D., Dutta A.
Mol. Cell 23:589-596(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91, MUTAGENESIS OF CYS-86.
[10]"UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited independently to chromatin: a basis for the regulation of FANCD2 monoubiquitination."
Alpi A., Langevin F., Mosedale G., Machida Y.J., Dutta A., Patel K.J.
Mol. Cell. Biol. 27:8421-8430(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCL, MUTAGENESIS OF CYS-86.
[11]"Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91 AND LYS-182, MUTAGENESIS OF CYS-86; LYS-91 AND 182-LYS--LYS-191.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating enzyme E2T overexpression in human breast cancer cells."
Ueki T., Park J.H., Nishidate T., Kijima K., Hirata K., Nakamura Y., Katagiri T.
Cancer Res. 69:8752-8760(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-86, INTERACTION WITH BRCA1.
[14]"FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL."
Longerich S., San Filippo J., Liu D., Sung P.
J. Biol. Chem. 284:23182-23186(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-86.
[15]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structural analysis of human FANCL, the E3 ligase in the Fanconi anemia pathway."
Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.
J. Biol. Chem. 286:32628-32637(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FANCL, MUTAGENESIS OF PHE-63.
[18]"Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to chemotherapy through regulation of UBE2T."
Ramaekers C.H., van den Beucken T., Meng A., Kassam S., Thoms J., Bristow R.G., Wouters B.G.
Radiother. Oncol. 101:190-197(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[19]"Ubiquitin-conjugating enzyme HSPC150."
Walker J.R., Avvakumov G.V., Newman E.M., Mackenzie F., Kozieradzki I., Sundstrom M., Arrowsmith C., Edwards A., Bochkarev A., Dhe-Paganon S.
Submitted (FEB-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032931 mRNA. Translation: BAA93711.1.
AF160215 mRNA. Translation: AAF67016.1.
AF161499 mRNA. Translation: AAF29114.1.
AK000504 mRNA. Translation: BAA91211.1.
AY542309 mRNA. Translation: AAT08178.1.
AL356953 Genomic DNA. Translation: CAI15933.1.
CH471067 Genomic DNA. Translation: EAW91411.1.
BC004152 mRNA. Translation: AAH04152.1.
BC019284 mRNA. Translation: AAH19284.1.
RefSeqNP_054895.1. NM_014176.3.
UniGeneHs.5199.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YH2X-ray2.00A1-167[»]
4CCGX-ray2.40A/B1-197[»]
ProteinModelPortalQ9NPD8.
SMRQ9NPD8. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118858. 18 interactions.
IntActQ9NPD8. 10 interactions.
STRING9606.ENSP00000356243.

PTM databases

PhosphoSiteQ9NPD8.

Polymorphism databases

DMDM73622065.

Proteomic databases

PaxDbQ9NPD8.
PRIDEQ9NPD8.

Protocols and materials databases

DNASU29089.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367274; ENSP00000356243; ENSG00000077152.
GeneID29089.
KEGGhsa:29089.
UCSCuc001gxx.4. human.

Organism-specific databases

CTD29089.
GeneCardsGC01M202300.
HGNCHGNC:25009. UBE2T.
HPAHPA002831.
MIM610538. gene.
neXtProtNX_Q9NPD8.
PharmGKBPA142670655.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidQ9NPD8.
KOK13960.
OMAELHMLAT.
OrthoDBEOG7BP84K.
PhylomeDBQ9NPD8.
TreeFamTF354203.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SignaLinkQ9NPD8.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9NPD8.
CleanExHS_UBE2T.
GenevestigatorQ9NPD8.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2T. human.
EvolutionaryTraceQ9NPD8.
GenomeRNAi29089.
NextBio52094.
PROQ9NPD8.
SOURCESearch...

Entry information

Entry nameUBE2T_HUMAN
AccessionPrimary (citable) accession number: Q9NPD8
Secondary accession number(s): Q2TU36
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM