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Q96PU4 (UHRF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
E3 ubiquitin-protein ligase UHRF2

EC=6.3.2.-
Alternative name(s):
Np95/ICBP90-like RING finger protein
Short name=Np95-like RING finger protein
Nuclear protein 97
Nuclear zinc finger protein Np97
RING finger protein 107
Ubiquitin-like PHD and RING finger domain-containing protein 2
Ubiquitin-like-containing PHD and RING finger domains protein 2
Gene names
Name:UHRF2
Synonyms:NIRF, RNF107
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131. Ref.1 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer; disulfide-linked. Binds methylated CpG containing oligonucleotides. Interacts with H3: the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3) By similarity. Interacts with PCNP, HDAC1 and CDK2 (inactive form). Component of a complex at least composed of UHRF2, CDK2 and CCNE1. Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1 phosphorylation. Interacts with CCND1; the interaction ubiquitinates CCND1 and appears independent of CCND1 phosphorylation. Interacts with p53/TP53 and RB1. Interacts with UBE2I. Ref.1 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.15

Subcellular location

Nucleus. Note: Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 By similarity. Ref.1 Ref.12

Induction

Up-regulated in proliferating fetal lung fibroblasts and in U-937 myeloid leukemia cells. Down-regulated in these cells by growth arrest and differentiation. In other cell types which cannot leave the cell cycle, such as tumoral HT-1080 and Hep-G2, levels are consistently up-regulated. Ref.1

Post-translational modification

May be autoubiquitinated; which may lead to proteasomal degradation.

Phosphorylated. Phosphorylation may be mediated by CDK2. Ref.6

Autosumoylated. Ref.12

Involvement in disease

Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.

Sequence similarities

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 ubiquitin-like domain.

Contains 1 YDG domain.

Sequence caution

The sequence CAH74120.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI13295.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMDisulfide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from expression pattern Ref.1. Source: HGNC

cell proliferation

Inferred from expression pattern Ref.1. Source: HGNC

positive regulation of cell cycle arrest

Inferred from direct assay Ref.6. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.7. Source: HGNC

protein ubiquitination

Inferred from direct assay Ref.7. Source: HGNC

regulation of cell cycle

Traceable author statement Ref.7. Source: HGNC

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7. Source: HGNC

   Cellular_componentnuclear heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: HGNC

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.7. Source: HGNC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PU4-1)

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: Q96PU4-2)

Also known as: a;

The sequence of this isoform differs from the canonical sequence as follows:
     500-503: DRGD → LTEL
     504-802: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 802802E3 ubiquitin-protein ligase UHRF2
PRO_0000056147

Regions

Domain1 – 7878Ubiquitin-like
Domain448 – 612165YDG
Zinc finger344 – 39552PHD-type
Zinc finger733 – 77240RING-type
Region117 – 311195Required for interaction with histone H3 By similarity
Region194 – 28895Interaction with PCNP
Region414 – 644231Methyl-CpG binding and interaction with HDAC1

Amino acid modifications

Modified residue6671Phosphoserine Ref.9
Disulfide bond704Interchain Ref.15

Natural variations

Alternative sequence500 – 5034DRGD → LTEL in isoform 2.
VSP_013874
Alternative sequence504 – 802299Missing in isoform 2.
VSP_013875
Natural variant871I → N in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035961

Experimental info

Mutagenesis3071K → R: No effect on autosumoylation. Ref.12
Mutagenesis5481K → R: No effect on autosumoylation. Ref.12
Mutagenesis7351C → S: No effect on autosumoylation, nor on ZNF131 sumoylation. Ref.12
Sequence conflict2871L → M in AAH28397. Ref.4
Sequence conflict3291P → T in AAH28397. Ref.4
Sequence conflict4161P → Q in AAH28397. Ref.4

Secondary structure

................................................................................. 802
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: 190E26D5A347A7FA

FASTA80289,985
        10         20         30         40         50         60 
MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD 

        70         80         90        100        110        120 
YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSNQ PSTSARARLI 

       130        140        150        160        170        180 
DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH 

       190        200        210        220        230        240 
KSKENTNKLD SVPSTSNSDC VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN 

       250        260        270        280        290        300 
ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII 

       310        320        330        340        350        360 
SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC GGKHEPNMQL 

       370        380        390        400        410        420 
LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST 

       430        440        450        460        470        480 
ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG 

       490        500        510        520        530        540 
RSNDGAYSLV LAGGFADEVD RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN 

       550        560        570        580        590        600 
CDAPLDDKIG AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS 

       610        620        630        640        650        660 
HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP KGQSKKQPSG 

       670        680        690        700        710        720 
TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI REDCQNQKLW DEVLSHLVEG 

       730        740        750        760        770        780 
PNFLKKLEQS FMCVCCQELV YQPVTTECFH NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI 

       790        800 
MIPNEILQTL LDLFFPGYSK GR 

« Hide

Isoform 2 (a) [UniParc].

Checksum: 6C81BFDFEC2FC512
Show »

FASTA50356,077

References

« Hide 'large scale' references
[1]"NIRF, a novel RING finger protein, is involved in cell-cycle regulation."
Mori T., Li Y., Hata H., Ono K., Kochi H.
Biochem. Biophys. Res. Commun. 296:530-536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH PCNP.
Tissue: Fetal brain.
[2]"LMO2-induced T cell leukemias overexpress a novel gene, Uhr1, containing RING and PHD zinc fingers and an ubiquitin-like domain."
Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-802 (ISOFORM 1).
Tissue: Testis.
[6]"NIRF induces G1 arrest and associates with Cdk2."
Li Y., Mori T., Hata H., Homma Y., Kochi H.
Biochem. Biophys. Res. Commun. 319:464-468(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE, PHOSPHORYLATION, INTERACTION WITH CDK2, IDENTIFICATION IN A COMPLEX WITH CDK2 AND CCNE1.
[7]"NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein."
Mori T., Li Y., Hata H., Kochi H.
FEBS Lett. 557:209-214(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH PCNP, FUNCTION.
[8]"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
Unoki M., Nishidate T., Nakamura Y.
Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HDAC1.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCDN1; CCNE1; TP53 AND RB1, ASSOCIATION WITH TUMORIGENESIS.
[12]"UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131."
Oh Y., Chung K.C.
J. Biol. Chem. 288:9102-9111(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOSUMOYLATION, INTERACTION WITH UBE2I, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-307; LYS-548 AND CYS-735.
[13]"Solution structure of the N-terminal ubiquitin-like domain in human NP95/ICBP90-like RING finger protein (NIRF)."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-76.
[14]"2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF."
Structural genomics consortium (SGC)
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802 IN COMPLEX WITH ZINC IONS.
[15]"2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802, SUBUNIT, DISULFIDE BOND.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-87.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB071698 mRNA. Translation: BAB68317.1.
AF274049 mRNA. Translation: AAM33799.1.
AL353718, AL133480 Genomic DNA. Translation: CAH74119.1.
AL133480, AL353718 Genomic DNA. Translation: CAI13293.1.
AL353718, AL133480 Genomic DNA. Translation: CAH74120.1. Sequence problems.
AL133480, AL353718 Genomic DNA. Translation: CAI13295.1. Sequence problems.
BC028397 mRNA. Translation: AAH28397.1.
AL137728 mRNA. Translation: CAH56383.1.
RefSeqNP_690856.1. NM_152896.2.
UniGeneHs.493401.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WY8NMR-A1-76[»]
1Z6UX-ray2.10A/B672-802[»]
2E6SNMR-A326-395[»]
3OLNX-ray2.30A/B419-648[»]
ProteinModelPortalQ96PU4.
SMRQ96PU4. Positions 1-121, 124-395, 441-632, 688-802.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125434. 54 interactions.
IntActQ96PU4. 37 interactions.
MINTMINT-1196856.
STRING9606.ENSP00000276893.

PTM databases

PhosphoSiteQ96PU4.

Polymorphism databases

DMDM67462076.

Proteomic databases

PaxDbQ96PU4.
PeptideAtlasQ96PU4.
PRIDEQ96PU4.

Protocols and materials databases

DNASU115426.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276893; ENSP00000276893; ENSG00000147854. [Q96PU4-1]
ENST00000468435; ENSP00000434182; ENSG00000147854. [Q96PU4-2]
GeneID115426.
KEGGhsa:115426.
UCSCuc003zjy.3. human. [Q96PU4-1]

Organism-specific databases

CTD115426.
GeneCardsGC09P006405.
HGNCHGNC:12557. UHRF2.
HPAHPA026633.
HPA026697.
MIM615211. gene.
neXtProtNX_Q96PU4.
PharmGKBPA37197.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3440.
HOGENOMHOG000124662.
HOVERGENHBG059298.
InParanoidQ96PU4.
KOK15713.
OMAYNVESPG.
OrthoDBEOG76DTRX.
PhylomeDBQ96PU4.
TreeFamTF106434.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ96PU4.
BgeeQ96PU4.
CleanExHS_UHRF2.
GenevestigatorQ96PU4.

Family and domain databases

Gene3D2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.
InterProIPR021991. DUF3590.
IPR015947. PUA-like_domain.
IPR014722. Rib_L2_dom2.
IPR003105. SRA_YDG.
IPR000626. Ubiquitin-like.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF12148. DUF3590. 1 hit.
PF00628. PHD. 1 hit.
PF02182. SAD_SRA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
SM00466. SRA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
SSF88697. SSF88697. 1 hit.
PROSITEPS50053. UBIQUITIN_2. 1 hit.
PS51015. YDG. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUHRF2. human.
EvolutionaryTraceQ96PU4.
GeneWikiUHRF2.
GenomeRNAi115426.
NextBio79598.
PROQ96PU4.
SOURCESearch...

Entry information

Entry nameUHRF2_HUMAN
AccessionPrimary (citable) accession number: Q96PU4
Secondary accession number(s): Q5VYR1 expand/collapse secondary AC list , Q5VYR3, Q659C8, Q8TAG7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 119 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM