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P78317 (RNF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RNF4

EC=6.3.2.-
Alternative name(s):
RING finger protein 4
Small nuclear ring finger protein
Short name=Protein SNURF
Gene names
Name:RNF4
Synonyms:SNURF
ORF Names:RES4-26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. Ref.7 Ref.9 Ref.12 Ref.14 Ref.15 Ref.16

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer (via RING-type zinc finger domain). Interacts with GSC2 By similarity. Interacts with AR/the androgen receptor and TBP By similarity. Interacts with TCF20 By similarity. Interacts with PATZ1. Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent. Interacts with PARP1. Interacts with PML (isoform PML-1 isoform PML-2 isoform PML-3 isoform PML-4 isoform PML-5and isoform PML-6) Ref.6 Ref.7 Ref.8 Ref.11 Ref.15 Ref.17

Subcellular location

Cytoplasm. Nucleus. NucleusPML body. Nucleusnucleoplasm Ref.7 Ref.8 Ref.15.

Tissue specificity

Widely expressed at low levels in many tissues; highly expressed in testis. Ref.2

Domain

The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates By similarity.

Post-translational modification

Sumoylated; conjugated by one or two SUMO1 moieties By similarity.

Autoubiquitinated By similarity.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Ligase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.9Ref.14Ref.15. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K6-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of kinetochore assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of spindle assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

response to arsenic-containing substance

Inferred from direct assay Ref.15. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

SUMO polymer binding

Inferred from sequence or structural similarity. Source: UniProtKB

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

nucleosome binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.14. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 9710597. Source: ProtInc

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 9710597. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78317-1)

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: P78317-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-113: ERRRPRRNAR...RDVYVTTHTP → GPQVLSVVPS...SSVASASVIP
     114-190: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190E3 ubiquitin-protein ligase RNF4
PRO_0000056043

Regions

Zinc finger132 – 17746RING-type
Region1 – 1616Required for ubiquitination activity By similarity
Region4 – 6158Mediates interaction with TRPS1 By similarity
Motif36 – 394SUMO interaction motif 1; mediates the binding to polysumoylated substrates
Motif46 – 494SUMO interaction motif 2; mediates the binding to polysumoylated substrates
Motif57 – 593SUMO interaction motif 3; mediates the binding to polysumoylated substrates
Motif67 – 704SUMO interaction motif 4; mediates the binding to polysumoylated substrates

Amino acid modifications

Modified residue941Phosphoserine Ref.10 Ref.13
Modified residue951Phosphoserine Ref.10 Ref.13

Natural variations

Alternative sequence72 – 11342ERRRP…TTHTP → GPQVLSVVPSAWTDTQRSCR MDVSSFPQNAAMSSVASASV IP in isoform 2.
VSP_045789
Alternative sequence114 – 19077Missing in isoform 2.
VSP_045790

Secondary structure

................. 190
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 1997. Version 1.
Checksum: E5E3AE4A9B28CF9D

FASTA19021,319
        10         20         30         40         50         60 
MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT CESLEPVVVD 

        70         80         90        100        110        120 
LTHNDSVVIV DERRRPRRNA RRLPQDHADS CVVSSDDEEL SRDRDVYVTT HTPRNARDEG 

       130        140        150        160        170        180 
ATGLRPSGTV SCPICMDGYS EIVQNGRLIV STECGHVFCS QCLRDSLKNA NTCPTCRKKI 

       190 
NHKRYHPIYI 

« Hide

Isoform 2 [UniParc].

Checksum: C65BF8B284670597
Show »

FASTA11312,126

References

« Hide 'large scale' references
[1]"The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3."
Hadano S., Ishida Y., Ikeda J.-E.
DNA Res. 5:177-186(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Identification and characterization of a novel RING-finger gene (RNF4) mapping at 4p16.3."
Chiariotti L., Benvenuto G., Fedele M., Santoro M., Simeone A., Fusco A., Bruni C.B.
Genomics 47:258-265(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
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. 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] (ISOFORMS 1 AND 2).
Tissue: Hair follicle dermal papilla, Testis and Tongue.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Testis.
[6]"A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING finger protein and acts as a transcriptional repressor."
Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F., Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A., Chiatiotti L.
J. Biol. Chem. 275:7894-7901(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PATZ1.
[7]"The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor."
Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.
J. Biol. Chem. 278:38780-38785(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRPS1, SUBCELLULAR LOCATION.
[8]"SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies."
Haekli M., Karvonen U., Jaenne O.A., Palvimo J.J.
Exp. Cell Res. 304:224-233(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PML, SUBCELLULAR LOCATION.
[9]"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARP1.
[12]"Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3."
Guo B., Sharrocks A.D.
Mol. Cell. Biol. 29:3204-3218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"The SUMO protease SENP6 is essential for inner kinetochore assembly."
Mukhopadhyay D., Arnaoutov A., Dasso M.
J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies."
Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T.
Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUMOYLATED PML, SUBCELLULAR LOCATION.
[16]"RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha."
van Hagen M., Overmeer R.M., Abolvardi S.S., Vertegaal A.C.
Nucleic Acids Res. 38:1922-1931(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms."
Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K.
PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PML.
[18]"Solution structure of the RING domain of the human RING finger protein 4."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 122-183.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000468 mRNA. Translation: BAA19122.1.
U95140 mRNA. Translation: AAC52022.1.
AK128038 mRNA. Translation: BAG54620.1.
AK309509 mRNA. No translation available.
AK312534 mRNA. Translation: BAG35433.1.
AL110117 Genomic DNA. No translation available.
AL645924 Genomic DNA. No translation available.
BX322586 Genomic DNA. No translation available.
CR450722 Genomic DNA. No translation available.
CR545473 Genomic DNA. No translation available.
BC031935 mRNA. Translation: AAH31935.1.
CCDSCCDS47001.1. [P78317-1]
CCDS54713.1. [P78317-2]
RefSeqNP_001171938.1. NM_001185009.2. [P78317-1]
NP_001171939.1. NM_001185010.2. [P78317-2]
NP_002929.1. NM_002938.4. [P78317-1]
UniGeneHs.66394.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EA6NMR-A122-183[»]
2XEUX-ray1.50A130-190[»]
4PPEX-ray2.00A/B120-190[»]
ProteinModelPortalP78317.
SMRP78317. Positions 124-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111974. 44 interactions.
IntActP78317. 19 interactions.
MINTMINT-271054.
STRING9606.ENSP00000315212.

PTM databases

PhosphoSiteP78317.

Polymorphism databases

DMDM18202358.

Proteomic databases

MaxQBP78317.
PaxDbP78317.
PRIDEP78317.

Protocols and materials databases

DNASU6047.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314289; ENSP00000315212; ENSG00000063978. [P78317-1]
ENST00000506706; ENSP00000424076; ENSG00000063978. [P78317-1]
ENST00000511600; ENSP00000426503; ENSG00000063978. [P78317-1]
ENST00000511859; ENSP00000426615; ENSG00000063978. [P78317-2]
GeneID6047.
KEGGhsa:6047.
UCSCuc003gfb.3. human. [P78317-1]

Organism-specific databases

CTD6047.
GeneCardsGC04P002463.
HGNCHGNC:10067. RNF4.
HPAHPA049356.
MIM602850. gene.
neXtProtNX_P78317.
PharmGKBPA34439.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327779.
HOGENOMHOG000059548.
HOVERGENHBG018577.
InParanoidP78317.
OMATHRQYHP.
PhylomeDBP78317.
TreeFamTF328387.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP78317.
BgeeP78317.
CleanExHS_RNF4.
GenevestigatorP78317.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF4. human.
EvolutionaryTraceP78317.
GeneWikiRNF4.
GenomeRNAi6047.
NextBio23561.
PROP78317.
SOURCESearch...

Entry information

Entry nameRNF4_HUMAN
AccessionPrimary (citable) accession number: P78317
Secondary accession number(s): B2R6D6, D6RF58, Q49AR8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 133 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 4

Human chromosome 4: entries, gene names and cross-references to MIM