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Q6ZNA4 (RN111_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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 Arkadia

EC=6.3.2.-
Alternative name(s):
RING finger protein 111
Gene names
Name:RNF111
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length994 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin-protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Ref.6 Ref.7 Ref.8

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with SMAD6, SMAD7, AXIN1, AXIN2 and SKIL isoform SNON Part of a complex containing RNF111, AXIN1 and SMAD7. Interacts (via SIM domains) with SUMO1 and SUMO2. Ref.7 Ref.8 Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: Upon TGF-beta treatment, translocates from nucleus to cytosol. Ref.7

Tissue specificity

Broadly expressed. Ref.6

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAH10369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC04531.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAD18633.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
Ligase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

pattern specification process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ubiquitin-dependent SMAD protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSUMO polymer binding

Inferred from direct assay Ref.9. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AXIN1O151692EBI-2129175,EBI-710484

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZNA4-1)

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: Q6ZNA4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     914-921: Missing.
Isoform 3 (identifier: Q6ZNA4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     766-766: T → TGLFVFCVSR
Note: No experimental confirmation available.
Isoform 4 (identifier: Q6ZNA4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     766-766: T → TGLFVFCVSR
     914-921: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 994994E3 ubiquitin-protein ligase Arkadia
PRO_0000280690

Regions

Zinc finger942 – 98342RING-type; atypical
Region241 – 404164Interaction with AXIN1
Motif300 – 3045SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates
Motif325 – 3317SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates
Motif382 – 3865SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substrates
Compositional bias252 – 464213Ser-rich
Compositional bias494 – 52330His-rich
Compositional bias629 – 781153Pro-rich

Natural variations

Alternative sequence7661T → TGLFVFCVSR in isoform 3 and isoform 4.
VSP_023840
Alternative sequence914 – 9218Missing in isoform 2 and isoform 4.
VSP_023841
Natural variant91N → K. Ref.1 Ref.2 Ref.5
Corresponds to variant rs2899642 [ dbSNP | Ensembl ].
VAR_031185
Natural variant7181A → T.
Corresponds to variant rs34086812 [ dbSNP | Ensembl ].
VAR_057216

Experimental info

Mutagenesis3821V → A: Abolishes SUMO binding. Ref.9
Mutagenesis3821V → L: Loss of affinity to SUMO1 and SUMO2. Ref.9
Mutagenesis3821V → Y: No loss of affinity toward SUMO1 and SUMO2. Ref.9
Mutagenesis3831V → A: Abolishes SUMO binding. Ref.9
Mutagenesis3831V → I: No loss of affinity toward SUMO1 and SUMO2. Ref.9
Mutagenesis3841D → A: Abolishes SUMO binding. Ref.9
Mutagenesis3841D → E: Loss of affinity to SUMO1 and SUMO2. Ref.9
Mutagenesis3841D → N: Loss of affinity to SUMO1 and SUMO2. Ref.9
Mutagenesis3851L → A: Abolishes SUMO binding. Ref.9
Mutagenesis3851L → I: Loss of affinity to SUMO1 and SUMO2. Ref.9
Mutagenesis3861T → A: Abolishes SUMO binding. Ref.9
Mutagenesis3861T → S: Loss of affinity to SUMO1 and SUMO2. Ref.9
Mutagenesis3861T → V: Loss of affinity to SUMO1 and SUMO2. Ref.9
Sequence conflict1651H → R in BX647259. Ref.2
Sequence conflict4731A → E in CAD98031. Ref.2
Sequence conflict5621Missing in AAH60862. Ref.3
Sequence conflict5621Missing in AAH20984. Ref.3
Sequence conflict6251M → T in BX647259. Ref.2
Sequence conflict7381T → I in BX647259. Ref.2
Sequence conflict8091E → G in CAD98031. Ref.2
Sequence conflict9311E → G in CAD98031. Ref.2
Sequence conflict9381T → A in BX647259. Ref.2
Sequence conflict9741I → V in BAD18471. Ref.1

Secondary structure

.............. 994
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 3.
Checksum: 7E387321E5F61FAB

FASTA994108,862
        10         20         30         40         50         60 
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP AGVEMINSKV 

        70         80         90        100        110        120 
GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA GPSYVQNCVK ENQGILGLRQ 

       130        140        150        160        170        180 
HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR 

       190        200        210        220        230        240 
SHKWPRTETE SVSGLLMKRP CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE 

       250        260        270        280        290        300 
VLARRKYALL PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 

       310        320        330        340        350        360 
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ GSSSHASRPQ 

       370        380        390        400        410        420 
EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA RMESQATSAS INNSNPSTSE 

       430        440        450        460        470        480 
QASDTASAVT SSQPSTVSET SATLTSNSTT GTSIGDDSRR TTSSAVTETG PPAMPRLPSC 

       490        500        510        520        530        540 
CPQHSPCGGS SQNHHALGHP HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE 

       550        560        570        580        590        600 
RPPQVQAPCG ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 

       610        620        630        640        650        660 
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY ASLTRPLHHQ 

       670        680        690        700        710        720 
ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA TSHPVAPPPP THLASTAAPI 

       730        740        750        760        770        780 
PQHLPPTHQP ISHHIPATAP PAQRLHPHEV MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH 

       790        800        810        820        830        840 
PNYGHGHHIH VPQTMSSHPR QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH 

       850        860        870        880        890        900 
HLQLGALPLM VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG 

       910        920        930        940        950        960 
TIERCTYPHK YKKVTTDWFS QRKLHCKQDG EEGTEEDTEE KCTICLSILE EGEDVRRLPC 

       970        980        990 
MHLFHQVCVD QWLITNKKCP ICRVDIEAQL PSES 

« Hide

Isoform 2 [UniParc].

Checksum: BD07D5D2C2B6AEB4
Show »

FASTA986107,896
Isoform 3 [UniParc].

Checksum: 9F0D0B05B5EB39A8
Show »

FASTA1,003109,871
Isoform 4 [UniParc].

Checksum: A648717F19CFB655
Show »

FASTA995108,906

References

« Hide 'large scale' references
[1]"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 3), VARIANT LYS-9.
Tissue: Thymus and Tongue.
[2]"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] (ISOFORMS 2 AND 4), VARIANT LYS-9.
Tissue: Amygdala and Endometrium.
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton 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].
[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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-994 (ISOFORM 1), VARIANT LYS-9.
Tissue: Brain, Colon and Placenta.
[6]"Arkadia amplifies TGF-beta superfamily signaling through degradation of Smad7."
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A., Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.
EMBO J. 22:6458-6470(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1 AND AXIN2, IDENTIFICATION IN COMPLEX WITH AXIN1 AND SMAD7, SUBCELLULAR LOCATION, FUNCTION.
[8]"Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation."
Levy L., Howell M., Das D., Harkin S., Episkopou V., Hill C.S.
Mol. Cell. Biol. 27:6068-6083(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKIL, FUNCTION.
[9]"PolySUMO-binding proteins identified through a string search."
Sun H., Hunter T.
J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SUMO1 AND SUMO2, MUTAGENESIS OF VAL-382; VAL-383; ASP-384; LEU-385 AND THR-386.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK095327 mRNA. Translation: BAC04531.1. Different initiation.
AK131304 mRNA. Translation: BAD18471.1.
AK131488 mRNA. Translation: BAD18633.1. Different initiation.
AL157474 mRNA. Translation: CAB75669.2.
BX538130 mRNA. Translation: CAD98031.1.
BX647259 mRNA. No translation available.
AC025918 Genomic DNA. No translation available.
AC090515 Genomic DNA. No translation available.
AC092757 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77561.1.
BC010369 mRNA. Translation: AAH10369.1. Different initiation.
BC020984 mRNA. Translation: AAH20984.1.
BC060862 mRNA. Translation: AAH60862.1.
PIRT46904.
RefSeqNP_001257457.1. NM_001270528.1.
NP_001257458.1. NM_001270529.1.
NP_001257459.1. NM_001270530.1.
NP_060080.6. NM_017610.7.
XP_005254536.1. XM_005254479.1.
UniGeneHs.404423.
Hs.603489.
Hs.741727.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KIZNMR-A927-994[»]
ProteinModelPortalQ6ZNA4.
SMRQ6ZNA4. Positions 898-994.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120146. 45 interactions.
IntActQ6ZNA4. 33 interactions.
MINTMINT-1187466.
STRING9606.ENSP00000288199.

PTM databases

PhosphoSiteQ6ZNA4.

Polymorphism databases

DMDM308153555.

Proteomic databases

PaxDbQ6ZNA4.
PRIDEQ6ZNA4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348370; ENSP00000288199; ENSG00000157450. [Q6ZNA4-2]
ENST00000434298; ENSP00000393641; ENSG00000157450. [Q6ZNA4-3]
ENST00000557998; ENSP00000452732; ENSG00000157450. [Q6ZNA4-1]
ENST00000559209; ENSP00000453872; ENSG00000157450. [Q6ZNA4-4]
ENST00000561186; ENSP00000453015; ENSG00000157450. [Q6ZNA4-3]
GeneID54778.
KEGGhsa:54778.
UCSCuc002afs.4. human. [Q6ZNA4-2]
uc002afv.4. human. [Q6ZNA4-1]
uc002afw.4. human. [Q6ZNA4-3]

Organism-specific databases

CTD54778.
GeneCardsGC15P059160.
HGNCHGNC:17384. RNF111.
HPAHPA038576.
HPA038577.
MIM605840. gene.
neXtProtNX_Q6ZNA4.
PharmGKBPA134868772.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291583.
HOVERGENHBG093884.
InParanoidQ6ZNA4.
KOK10635.
OMAPCRKRFV.
OrthoDBEOG7WHH9N.
PhylomeDBQ6ZNA4.
TreeFamTF331862.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkQ6ZNA4.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ6ZNA4.
BgeeQ6ZNA4.
CleanExHS_RNF111.
GenevestigatorQ6ZNA4.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRNF111.
GenomeRNAi54778.
NextBio57437.
PROQ6ZNA4.
SOURCESearch...

Entry information

Entry nameRN111_HUMAN
AccessionPrimary (citable) accession number: Q6ZNA4
Secondary accession number(s): C9JUS4 expand/collapse secondary AC list , H0YN55, Q6P9A4, Q6ZMU2, Q7L428, Q7Z346, Q8N1P9, Q8WUA3, Q9NSR1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 102 of the entry and version 3 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 15

Human chromosome 15: entries, gene names and cross-references to MIM