Q9HCM9 (TRI39_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol. Mitochondrion. Note: Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when co-localized 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.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-739510,EBI-739510
NCK1	P16333	2	EBI-739510,EBI-389883
TRIM17	Q9Y577	3	EBI-739510,EBI-743894

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 518

518

E3 ubiquitin-protein ligase TRIM39

PRO_0000056257

Regions

Domain

319 – 514

196

B30.2/SPRY

Zinc finger

29 – 70

42

RING-type

Zinc finger

102 – 143

42

B box-type

Coiled coil

181 – 250

70

Potential

Natural variations

Alternative sequence

269 – 298

30

Missing in isoform 2.

VSP_005755

Experimental info

Sequence conflict

137

1

A → P in BAB16374. Ref.1

Sequence conflict

419

1

E → K in BAD13703. Ref.3

Secondary structure

1

.

.

.

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.

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.

.

.

.

.

.

.

.

.

.

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518

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Helix

50 – 56

7

Turn

108 – 110

3

Beta strand

116 – 121

6

Beta strand

123 – 125

3

Helix

127 – 130

4

Turn

134 – 137

4

Beta strand

140 – 142

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 7, 2004. Version 2. Checksum: 2F946F518B217153	FASTA	518	59,690
	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
	Isoform 2 [UniParc]. Checksum: 102AA8E5C8786A3E	FASTA	488	56,374
	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 DVKSTLEKCE KVKTMEVTSV SIELEKNFSN FPRQYFALRK 310 320 330 340 350 360 ILKQLIADVT LDPETAHPNL VLSEDRKSVK FVETRLRDLP DTPRRFTFYP CVLATEGFTS 370 380 390 400 410 420 GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH 430 440 450 460 470 480 IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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.

IPI

IPI00293604.
IPI00873841.

PIR

JC7387.

RefSeq

NP_067076.2. NM_021253.3.
NP_742013.1. NM_172016.2.

UniGene

Hs.413493.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DID	NMR	-	A	104-143	[»]
2DIF	NMR	-	A	104-143	[»]
2ECJ	NMR	-	A	19-69	[»]

ProteinModelPortal

Q9HCM9.

SMR

Q9HCM9. Positions 13-69, 106-143, 338-513.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HCM9. 25 interactions.

MINT

MINT-1433641.

STRING

9606.ENSP00000398355.

PTM databases

PhosphoSite

Q9HCM9.

Polymorphism databases

DMDM

56405385.

Proteomic databases

PaxDb

Q9HCM9.

PRIDE

Q9HCM9.

Protocols and materials databases

DNASU

56658.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376656; ENSP00000365844; ENSG00000204599.
ENST00000376659; ENSP00000365847; ENSG00000204599.
ENST00000383601; ENSP00000373095; ENSG00000206495.
ENST00000383602; ENSP00000373096; ENSG00000206495.
ENST00000383603; ENSP00000373097; ENSG00000206495.
ENST00000396547; ENSP00000379796; ENSG00000204599.
ENST00000396548; ENSP00000379797; ENSG00000204599.
ENST00000396551; ENSP00000379800; ENSG00000204599.
ENST00000400644; ENSP00000383486; ENSG00000206495.
ENST00000413715; ENSP00000411949; ENSG00000224994.
ENST00000414015; ENSP00000401071; ENSG00000224994.
ENST00000419790; ENSP00000401184; ENSG00000229929.
ENST00000424575; ENSP00000409902; ENSG00000230308.
ENST00000426469; ENSP00000397043; ENSG00000229929.
ENST00000430502; ENSP00000398956; ENSG00000232839.
ENST00000431272; ENSP00000396986; ENSG00000230308.
ENST00000433900; ENSP00000389852; ENSG00000232839.
ENST00000438076; ENSP00000389198; ENSG00000232839.
ENST00000438859; ENSP00000411582; ENSG00000226437.
ENST00000440117; ENSP00000392130; ENSG00000224994.
ENST00000443109; ENSP00000414525; ENSG00000229929.
ENST00000445206; ENSP00000391917; ENSG00000226437.
ENST00000446397; ENSP00000412743; ENSG00000230308.
ENST00000449318; ENSP00000404904; ENSG00000224994.
ENST00000450778; ENSP00000387445; ENSG00000226437.
ENST00000451132; ENSP00000394353; ENSG00000226437.
ENST00000451715; ENSP00000398355; ENSG00000232839.
ENST00000452705; ENSP00000415259; ENSG00000229929.
ENST00000458607; ENSP00000404340; ENSG00000230308.
ENST00000547030; ENSP00000449847; ENSG00000224994.
ENST00000548002; ENSP00000447835; ENSG00000232839.
ENST00000549841; ENSP00000448572; ENSG00000230308.
ENST00000550282; ENSP00000449272; ENSG00000206495.
ENST00000552337; ENSP00000450288; ENSG00000226437.
ENST00000552520; ENSP00000448462; ENSG00000229929.

GeneID

56658.

KEGG

hsa:56658.

UCSC

uc003npz.3. human.
uc010jrz.3. human.

Organism-specific databases

CTD

56658.

GeneCards

GC06P030294.

HGNC

HGNC:10065. TRIM39.

MIM

605700. gene.

neXtProt

NX_Q9HCM9.

PharmGKB

PA35535.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG238084.

HOGENOM

HOG000234133.

HOVERGEN

HBG001357.

InParanoid

Q9HCM9.

KO

K12015.

OMA

KESNRCE.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9HCM9.

Bgee

Q9HCM9.

CleanEx

HS_TRIM39.

Genevestigator

Q9HCM9.

GermOnline

ENSG00000204599. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001870. 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.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

PRINTS

PR01407. BUTYPHLNCDUF.

SMART

SM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9HCM9.

GenomeRNAi

56658.

NextBio

62129.

SOURCE

Search...

Entry information

Entry name

TRI39_HUMAN

Accession

Primary (citable) accession number: Q9HCM9
Secondary accession number(s): Q5STG3 , Q5STG4, Q76BL3, Q8IYT9, Q96IB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.