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P26368 (U2AF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor U2AF 65 kDa subunit
Alternative name(s):
U2 auxiliary factor 65 kDa subunit
Short name=hU2AF(65)
Short name=hU2AF65
U2 snRNP auxiliary factor large subunit
Gene names
Name:U2AF2
Synonyms:U2AF65
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. Ref.9 Ref.13 Ref.16

Subunit structure

Interacts with U2AF1L4 By similarity. Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. Interacts with ZRSR2/U2AF1-RS2. Ref.5 Ref.6 Ref.7 Ref.8 Ref.19

Subcellular location

Nucleus.

Post-translational modification

Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   PTMAcetylation
Hydroxylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator PubMed 9731529. Source: HGNC

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.9. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnuclear speck

Inferred from direct assay PubMed 21984414. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.16. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26368-1)

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.
Isoform 2 (identifier: P26368-2)

The sequence of this isoform differs from the canonical sequence as follows:
     345-348: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 475474Splicing factor U2AF 65 kDa subunit
PRO_0000081988

Regions

Domain149 – 23183RRM 1
Domain259 – 33779RRM 2
Domain385 – 46682RRM 3
Compositional bias27 – 6236Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue21N-acetylserine Ref.4 Ref.12 Ref.17 Ref.21 Ref.22
Modified residue21Phosphoserine Ref.10 Ref.17 Ref.20
Modified residue1515-hydroxylysine; by JMJD6 Ref.16
Modified residue701N6-acetyllysine Ref.15
Modified residue791Phosphoserine Ref.17
Modified residue27615-hydroxylysine; by JMJD6 Ref.16

Natural variations

Alternative sequence345 – 3484Missing in isoform 2.
VSP_035414

Experimental info

Mutagenesis921W → A: Decreases affinity for UAF1 by 3 orders of magnitude. Ref.25
Mutagenesis961P → G: Decreases affinity for UAF1 by 2 orders of magnitude. Ref.25
Mutagenesis1041P → G: Decreases affinity for UAF1 by 2 orders of magnitude. Ref.25
Mutagenesis387 – 3882EE → RR: Reduces interaction with SF1.
Mutagenesis391 – 3944DDEE → AAAA: Reduces interaction with SF1.
Mutagenesis391 – 3944DDEE → RRKK: Reduces interaction with SF1.
Mutagenesis396 – 3972EE → AA: No effect.
Mutagenesis396 – 3972EE → GA: Reduces interaction with SF1.
Mutagenesis396 – 3972EE → KK: Reduces interaction with SF1.
Mutagenesis4541F → A: Reduces interaction with SF1. Ref.24

Secondary structure

.............................................................. 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 26AD271CD8FC6211

FASTA47553,501
        10         20         30         40         50         60 
MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR 

        70         80         90        100        110        120 
RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA 

       130        140        150        160        170        180 
LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ 

       190        200        210        220        230        240 
APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE 

       250        260        270        280        290        300 
NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK 

       310        320        330        340        350        360 
GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV 

       370        380        390        400        410        420 
PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP 

       430        440        450        460        470 
VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW 

« Hide

Isoform 2 [UniParc].

Checksum: 3F59A02CD2B03F46
Show »

FASTA47153,121

References

« Hide 'large scale' references
[1]"Cloning and domain structure of the mammalian splicing factor U2AF."
Zamore P.D., Patton J.G., Green M.R.
Nature 355:609-614(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]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].
[3]"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 2).
Tissue: Lymph and Skin.
[4]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[5]"Large-scale proteomic analysis of the human spliceosome."
Rappsilber J., Ryder U., Lamond A.I., Mann M.
Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 261-286, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
[6]"A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
Tronchere H., Wang J., Fu X.D.
Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZRSR2.
[7]"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
Zhang W.-J., Wu J.Y.
Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAF11.
[8]"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly."
Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J.
EMBO J. 18:4549-4559(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SF1.
[9]"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
[12]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing."
Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing."
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., Boettger A.
Science 325:90-93(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HYDROXYLATION AT LYS-15 AND LYS-276.
[17]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing."
Chen Y., Zhang L., Jones K.A.
Genes Dev. 25:701-716(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNW1.
[20]"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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65))."
Ito T., Muto Y., Green M.R., Yokoyama S.
EMBO J. 18:4523-4534(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 148-237.
[24]"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP."
Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M.
Mol. Cell 11:965-976(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, MUTAGENESIS OF 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454.
[25]"A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer."
Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.
Cell 106:595-605(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-112 IN COMPLEX WITH U2AF1, MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64044 mRNA. Translation: CAA45409.1.
CH471135 Genomic DNA. Translation: EAW72404.1.
BC008740 mRNA. Translation: AAH08740.1.
BC030574 mRNA. Translation: AAH30574.1.
PIRS20250.
RefSeqNP_001012496.1. NM_001012478.1.
NP_009210.1. NM_007279.2.
UniGeneHs.528007.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMTX-ray2.20B85-112[»]
1O0PNMR-A372-475[»]
1OPINMR-A372-475[»]
1U2FNMR-A148-237[»]
2G4BX-ray2.50A148-336[»]
2HZCX-ray1.47A148-229[»]
2M0GNMR-B372-475[»]
2U2FNMR-A258-342[»]
2YH0NMR-A148-342[»]
2YH1NMR-A148-342[»]
3VAFX-ray2.49A/B148-336[»]
3VAGX-ray2.19A/B148-336[»]
3VAHX-ray2.50A/B148-336[»]
3VAIX-ray2.20A/B148-336[»]
3VAJX-ray1.90A/B148-336[»]
3VAKX-ray2.17A/B148-336[»]
3VALX-ray2.50A/B/D/I148-336[»]
3VAMX-ray2.40A/B148-336[»]
4FXWX-ray2.29A/C375-475[»]
ProteinModelPortalP26368.
SMRP26368. Positions 148-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116466. 125 interactions.
DIPDIP-2154N.
IntActP26368. 49 interactions.
MINTMINT-1192370.
STRING9606.ENSP00000307863.

PTM databases

PhosphoSiteP26368.

Polymorphism databases

DMDM267188.

Proteomic databases

PaxDbP26368.
PRIDEP26368.

Protocols and materials databases

DNASU11338.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308924; ENSP00000307863; ENSG00000063244. [P26368-1]
ENST00000450554; ENSP00000388475; ENSG00000063244. [P26368-2]
GeneID11338.
KEGGhsa:11338.
UCSCuc002qlt.3. human. [P26368-2]
uc002qlu.3. human. [P26368-1]

Organism-specific databases

CTD11338.
GeneCardsGC19P056165.
HGNCHGNC:23156. U2AF2.
HPACAB010910.
HPA041943.
HPA043562.
MIM191318. gene.
neXtProtNX_P26368.
PharmGKBPA134908683.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298004.
HOGENOMHOG000180745.
HOVERGENHBG062169.
InParanoidP26368.
KOK12837.
OMAYARRETR.
OrthoDBEOG7CNZFZ.
PhylomeDBP26368.
TreeFamTF314111.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressP26368.
BgeeP26368.
CleanExHS_U2AF2.
GenevestigatorP26368.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006529. U2AF_lg.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01642. U2AF_lg. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSU2AF2. human.
EvolutionaryTraceP26368.
GeneWikiU2AF2.
GenomeRNAi11338.
NextBio43079.
PMAP-CutDBP26368.
PROP26368.
SOURCESearch...

Entry information

Entry nameU2AF2_HUMAN
AccessionPrimary (citable) accession number: P26368
Secondary accession number(s): Q96HC5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 163 of the entry and version 4 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

MIM cross-references

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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM