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Q9HCM9 (TRI39_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM39

EC=6.3.2.-
Alternative name(s):
RING finger protein 23
Testis-abundant finger protein
Tripartite motif-containing protein 39
Gene names
Name:TRIM39
Synonyms:RNF23, TFP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1. Ref.9 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with MOAP1. Ref.9

Subcellular location

Cytoplasmcytosol. Mitochondrion. Note: Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when colocalized with MOAP1. Ref.9

Tissue specificity

Ubiquitous; highly expressed in brain, heart, kidney, liver, skeletal muscle, spleen and testis. Ref.9

Post-translational modification

Autoubiquitinated.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 1 B30.2/SPRY domain.

Contains 1 RING-type zinc finger.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCM9-1)

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: Q9HCM9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     269-298: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518E3 ubiquitin-protein ligase TRIM39
PRO_0000056257

Regions

Domain319 – 514196B30.2/SPRY
Zinc finger29 – 7042RING-type
Zinc finger102 – 14342B box-type
Coiled coil181 – 25070 Potential

Natural variations

Alternative sequence269 – 29830Missing in isoform 2.
VSP_005755

Experimental info

Sequence conflict1371A → P in BAB16374. Ref.1
Sequence conflict4191E → K in BAD13703. Ref.3

Secondary structure

................. 518
Helix Strand Turn

Details...

Sequences

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

Last modified December 7, 2004. Version 2.
Checksum: 2F946F518B217153

FASTA51859,690
        10         20         30         40         50         60 
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL 

        70         80         90        100        110        120 
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK IRDESLCPQH HEALSLFCYE 

       130        140        150        160        170        180 
DQEAVCLICA ISHTHRAHTV VPLDDATQEY KEKLQKCLEP LEQKLQEITR CKSSEEKKPG 

       190        200        210        220        230        240 
ELKRLVESRR QQILREFEEL HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL 

       250        260        270        280        290        300 
AHLAAEVEGK CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE 

       310        320        330        340        350        360 
KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL VLSEDRKSVK 

       370        380        390        400        410        420 
FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL 

       430        440        450        460        470        480 
TPLPETGYWR VRLWNGDKYA ATTTPFTPLH IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI 

       490        500        510 
YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE 

« Hide

Isoform 2 [UniParc].

Checksum: 102AA8E5C8786A3E
Show »

FASTA48856,374

References

« Hide 'large scale' references
[1]"Molecular cloning of testis-abundant finger protein/ring finger protein 23 (RNF23), a novel RING-B box-coiled coil-B30.2 protein on the class I region of the human MHC."
Orimo A., Yamagishi T., Tominaga N., Yamauchi Y., Hishinuma T., Okada K., Suzuki M., Sato M., Nogi Y., Suzuki H., Inoue S., Yoshimura K., Shimizu Y., Muramatsu M.
Biochem. Biophys. Res. Commun. 276:45-51(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Siamak B., Inoko H.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Testis.
[5]"Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A. expand/collapse author list , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Tissue: Peripheral blood leukocyte.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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] (ISOFORM 2).
Tissue: Colon and Testis.
[9]"TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process."
Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C.
Exp. Cell Res. 315:1313-1325(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MOAP1.
[10]"The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1."
Huang N.J., Zhang L., Tang W., Chen C., Yang C.S., Kornbluth S.
J. Cell Biol. 197:361-367(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOUBIQUITINATION.
[11]"One sequence two fold ? correct fold of the ZF-B-box domain from human tripartite motif protein 39."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 104-143.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046381 mRNA. Translation: BAB16374.1.
BT007370 mRNA. Translation: AAP36034.1.
AB110937 Genomic DNA. Translation: BAD13703.1.
AK292512 mRNA. Translation: BAF85201.1.
AB110938 Genomic DNA. Translation: BAD13704.1.
AB202089 Genomic DNA. Translation: BAE78608.1.
AL662832 Genomic DNA. Translation: CAI17501.1.
AL662795 Genomic DNA. Translation: CAI18251.1.
AL773535 Genomic DNA. Translation: CAI41818.1.
AL773535 Genomic DNA. Translation: CAI41819.1.
BX248580 Genomic DNA. Translation: CAM25899.1.
BX248580 Genomic DNA. Translation: CAM25900.1.
CR759928 Genomic DNA. Translation: CAQ08313.1.
CR759928 Genomic DNA. Translation: CAQ08314.1.
BX927214 Genomic DNA. Translation: CAQ08383.1.
BX927214 Genomic DNA. Translation: CAQ08384.1.
CR759281 Genomic DNA. Translation: CAQ09020.1.
CR759281 Genomic DNA. Translation: CAQ09021.1.
CH471081 Genomic DNA. Translation: EAX03283.1.
CH471081 Genomic DNA. Translation: EAX03284.1.
BC007661 mRNA. Translation: AAH07661.1.
BC034985 mRNA. Translation: AAH34985.1.
PIRJC7387.
RefSeqNP_067076.2. NM_021253.3.
NP_742013.1. NM_172016.2.
UniGeneHs.413493.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIDNMR-A104-143[»]
2DIFNMR-A104-143[»]
2ECJNMR-A19-69[»]
ProteinModelPortalQ9HCM9.
SMRQ9HCM9. Positions 13-69, 106-143, 338-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121170. 37 interactions.
IntActQ9HCM9. 31 interactions.
MINTMINT-1433641.
STRING9606.ENSP00000398355.

PTM databases

PhosphoSiteQ9HCM9.

Polymorphism databases

DMDM56405385.

Proteomic databases

PaxDbQ9HCM9.
PRIDEQ9HCM9.

Protocols and materials databases

DNASU56658.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376656; ENSP00000365844; ENSG00000204599. [Q9HCM9-1]
ENST00000376659; ENSP00000365847; ENSG00000204599. [Q9HCM9-2]
ENST00000383601; ENSP00000373095; ENSG00000206495. [Q9HCM9-2]
ENST00000383602; ENSP00000373096; ENSG00000206495. [Q9HCM9-1]
ENST00000383603; ENSP00000373097; ENSG00000206495. [Q9HCM9-2]
ENST00000396547; ENSP00000379796; ENSG00000204599. [Q9HCM9-1]
ENST00000396548; ENSP00000379797; ENSG00000204599. [Q9HCM9-2]
ENST00000396551; ENSP00000379800; ENSG00000204599. [Q9HCM9-2]
ENST00000400644; ENSP00000383486; ENSG00000206495. [Q9HCM9-2]
ENST00000413715; ENSP00000411949; ENSG00000224994. [Q9HCM9-1]
ENST00000414015; ENSP00000401071; ENSG00000224994. [Q9HCM9-2]
ENST00000419790; ENSP00000401184; ENSG00000229929. [Q9HCM9-2]
ENST00000424575; ENSP00000409902; ENSG00000230308. [Q9HCM9-1]
ENST00000426469; ENSP00000397043; ENSG00000229929. [Q9HCM9-1]
ENST00000430502; ENSP00000398956; ENSG00000232839. [Q9HCM9-2]
ENST00000431272; ENSP00000396986; ENSG00000230308. [Q9HCM9-2]
ENST00000433900; ENSP00000389852; ENSG00000232839. [Q9HCM9-2]
ENST00000438076; ENSP00000389198; ENSG00000232839. [Q9HCM9-2]
ENST00000438859; ENSP00000411582; ENSG00000226437. [Q9HCM9-2]
ENST00000440117; ENSP00000392130; ENSG00000224994. [Q9HCM9-2]
ENST00000443109; ENSP00000414525; ENSG00000229929. [Q9HCM9-2]
ENST00000445206; ENSP00000391917; ENSG00000226437. [Q9HCM9-1]
ENST00000446397; ENSP00000412743; ENSG00000230308. [Q9HCM9-2]
ENST00000449318; ENSP00000404904; ENSG00000224994. [Q9HCM9-2]
ENST00000450778; ENSP00000387445; ENSG00000226437. [Q9HCM9-2]
ENST00000451132; ENSP00000394353; ENSG00000226437. [Q9HCM9-2]
ENST00000451715; ENSP00000398355; ENSG00000232839. [Q9HCM9-1]
ENST00000452705; ENSP00000415259; ENSG00000229929. [Q9HCM9-2]
ENST00000458607; ENSP00000404340; ENSG00000230308. [Q9HCM9-2]
ENST00000547030; ENSP00000449847; ENSG00000224994. [Q9HCM9-1]
ENST00000548002; ENSP00000447835; ENSG00000232839. [Q9HCM9-1]
ENST00000549841; ENSP00000448572; ENSG00000230308. [Q9HCM9-1]
ENST00000550282; ENSP00000449272; ENSG00000206495. [Q9HCM9-1]
ENST00000552337; ENSP00000450288; ENSG00000226437. [Q9HCM9-1]
ENST00000552520; ENSP00000448462; ENSG00000229929. [Q9HCM9-1]
GeneID56658.
KEGGhsa:56658.
UCSCuc003npz.3. human. [Q9HCM9-2]
uc010jrz.3. human. [Q9HCM9-1]

Organism-specific databases

CTD56658.
GeneCardsGC06P030294.
GC06Pi30302.
GC06Pj30284.
GC06Pk30284.
GC06Pl30338.
GC06Pn30283.
GC06Po30283.
HGNCHGNC:10065. TRIM39.
HPAHPA051120.
MIM605700. gene.
neXtProtNX_Q9HCM9.
PharmGKBPA35535.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238084.
HOGENOMHOG000234133.
HOVERGENHBG001357.
InParanoidQ9HCM9.
KOK12015.
OMAVECRRQQ.
PhylomeDBQ9HCM9.
TreeFamTF342569.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9HCM9.
BgeeQ9HCM9.
CleanExHS_TRIM39.
GenevestigatorQ9HCM9.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9HCM9.
GenomeRNAi56658.
NextBio62129.
PROQ9HCM9.
SOURCESearch...

Entry information

Entry nameTRI39_HUMAN
AccessionPrimary (citable) accession number: Q9HCM9
Secondary accession number(s): Q5STG3 expand/collapse secondary AC list , Q5STG4, Q76BL3, Q8IYT9, Q96IB6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 132 of the entry and version 2 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 6

Human chromosome 6: entries, gene names and cross-references to MIM