Q8WV44 (TRI41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase TRIM41
EC=6.3.2.-

Alternative name(s):
RING finger-interacting protein with C kinase
Short name=RINCK
Tripartite motif-containing protein 41

Gene names

Name:	TRIM41
Synonyms:	RINCK

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	630 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. Ref.8
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with PRKCA. Ref.8
Subcellular location	Cytoplasm. Nucleus Ref.1.
Tissue specificity	Expressed in multiple tissues with the highest levels in heart and skeletal muscle. Ref.8
Post-translational modification	Auto-ubiquitinated.
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	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus 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
Prkcb	P68403-2	3	EBI-726015,EBI-397092	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WV44-1)

Also known as: TRIM41a; TRIM41alpha;

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: Q8WV44-2)

Also known as: TRIM41b; TRIM41beta; RINCK1;

The sequence of this isoform differs from the canonical sequence as follows:
     490-518: VEVGGRRGWAVGAARESTHHKEKVGPGGS → EPKEPSWPPAQPSLTYYVCPTDRPEFSFT
     519-630: Missing.

Isoform 3 (identifier: Q8WV44-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-420: Missing.

Isoform 4 (identifier: Q8WV44-4)

Also known as: RINCK2;

The sequence of this isoform differs from the canonical sequence as follows:
     381-381: D → V
     382-630: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 630

630

E3 ubiquitin-protein ligase TRIM41

PRO_0000056262

Regions

Domain

413 – 630

218

B30.2/SPRY

Zinc finger

20 – 61

42

RING-type

Zinc finger

222 – 263

42

B box-type

Coiled coil

264 – 373

110

Potential

Compositional bias

51 – 163

113

Glu-rich

Amino acid modifications

Modified residue

447

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1 – 420

420

Missing in isoform 3.

VSP_012515

Alternative sequence

381

1

D → V in isoform 4.

VSP_012516

Alternative sequence

382 – 630

249

Missing in isoform 4.

VSP_012517

Alternative sequence

490 – 518

29

VEVGG…GPGGS → EPKEPSWPPAQPSLTYYVCP TDRPEFSFT in isoform 2.

VSP_010395

Alternative sequence

519 – 630

112

Missing in isoform 2.

VSP_010396

Natural variant

78

1

A → T.
Corresponds to variant rs6601178 [ dbSNP | Ensembl ].

VAR_027914

Natural variant

438

1

D → G.
Corresponds to variant rs2241371 [ dbSNP | Ensembl ].

VAR_027915

Experimental info

Mutagenesis

20

1

C → A: Abolishes E3 ligase activity. Ref.8

Sequence conflict

276

1

G → E in BAD07472. Ref.1

Sequence conflict

276

1

G → E in BAD07473. Ref.1

Sequence conflict

276

1

G → E in BAB70617. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

630

Helix Strand Turn

Details...

Turn

228 – 230

3

Beta strand

236 – 238

3

Turn

239 – 242

4

Beta strand

243 – 245

3

Helix

247 – 251

5

Helix

253 – 256

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TRIM41a) (TRIM41alpha) [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 8E704CBEAB928BF5	FASTA	630	71,670
	10 20 30 40 50 60 MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD 70 80 90 100 110 120 REEEEEDGEE EEVEAVGAGA GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMSRSSWDNM 130 140 150 160 170 180 DYVWEEEDEE EDLDYYLGDM EEEDLRGEDE EDEEEVLEEV EEEDLDPVTP LPPPPAPRRC 190 200 210 220 230 240 FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VTDQGICPKH QEALKLFCEV 250 260 270 280 290 300 DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT 310 320 330 340 350 360 ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA SRLAEQAAQL 370 380 390 400 410 420 SRLLAEAQER SQQGGLRLLQ DIKETFNRCE EVQLQPPEVW SPDPCQPHSH DFLTDAIVRK 430 440 450 460 470 480 MSRMFCQAAR VDLTLDPDTA HPALMLSPDR RGVRLAERRQ EVADHPKRFS ADCCVLGAQG 490 500 510 520 530 540 FRSGRHYWEV EVGGRRGWAV GAARESTHHK EKVGPGGSSV GSGDASSSRH HHRRRRLHLP 550 560 570 580 590 600 QQPLLQREVW CVGTNGKRYQ AQSSTEQTLL SPSEKPRRFG VYLDYEAGRL GFYNAETLAH 610 620 630 VHTFSAAFLG ERVFPFFRVL SKGTRIKLCP
	Isoform 2 (TRIM41b) (TRIM41beta) (RINCK1) [UniParc]. Checksum: 88078577B9A3C98E	FASTA	518	59,302
	10 20 30 40 50 60 MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD 70 80 90 100 110 120 REEEEEDGEE EEVEAVGAGA GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMSRSSWDNM 130 140 150 160 170 180 DYVWEEEDEE EDLDYYLGDM EEEDLRGEDE EDEEEVLEEV EEEDLDPVTP LPPPPAPRRC 190 200 210 220 230 240 FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VTDQGICPKH QEALKLFCEV 250 260 270 280 290 300 DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT 310 320 330 340 350 360 ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA SRLAEQAAQL 370 380 390 400 410 420 SRLLAEAQER SQQGGLRLLQ DIKETFNRCE EVQLQPPEVW SPDPCQPHSH DFLTDAIVRK 430 440 450 460 470 480 MSRMFCQAAR VDLTLDPDTA HPALMLSPDR RGVRLAERRQ EVADHPKRFS ADCCVLGAQG 490 500 510 FRSGRHYWEE PKEPSWPPAQ PSLTYYVCPT DRPEFSFT
	Isoform 3 [UniParc]. Checksum: 6354BEB70AFB1C7C	FASTA	210	23,608
	10 20 30 40 50 60 MSRMFCQAAR VDLTLDPDTA HPALMLSPDR RGVRLAERRQ EVADHPKRFS ADCCVLGAQG 70 80 90 100 110 120 FRSGRHYWEV EVGGRRGWAV GAARESTHHK EKVGPGGSSV GSGDASSSRH HHRRRRLHLP 130 140 150 160 170 180 QQPLLQREVW CVGTNGKRYQ AQSSTEQTLL SPSEKPRRFG VYLDYEAGRL GFYNAETLAH 190 200 210 VHTFSAAFLG ERVFPFFRVL SKGTRIKLCP
	Isoform 4 (RINCK2) [UniParc]. Checksum: 2716AF100B4CA18B	FASTA	381	43,491
	10 20 30 40 50 60 MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD 70 80 90 100 110 120 REEEEEDGEE EEVEAVGAGA GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMSRSSWDNM 130 140 150 160 170 180 DYVWEEEDEE EDLDYYLGDM EEEDLRGEDE EDEEEVLEEV EEEDLDPVTP LPPPPAPRRC 190 200 210 220 230 240 FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VTDQGICPKH QEALKLFCEV 250 260 270 280 290 300 DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT 310 320 330 340 350 360 ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA SRLAEQAAQL 370 380 SRLLAEAQER SQQGGLRLLQ V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Intracellular localization and domain organization of human TRIM41 proteins." Tanaka M., Fukuda Y., Mashima K., Hanai R. Mol. Biol. Rep. 32:87-93(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION.
[2]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[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 2).
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-630 (ISOFORM 4). Tissue: Lung, Pancreas and Uterus.
[7]	"M phase-specific association of human topoisomerase IIIbeta with chromosomes." Kobayashi M., Hanai R. Biochem. Biophys. Res. Commun. 287:282-287(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-630 (ISOFORM 2).
[8]	"Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase." Chen D., Gould C., Garza R., Gao T., Hampton R.Y., Newton A.C. J. Biol. Chem. 282:33776-33787(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), TISSUE SPECIFICITY, AUTOUBIQUITINATION, INTERACTION WITH PRKCA, MUTAGENESIS OF CYS-20.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Solution structure of the ZF-b_box domain from human tripartite motif protein 41." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 214-263.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB100366 mRNA. Translation: BAD07472.1.
AB100367 mRNA. Translation: BAD07473.1.
AF258579 mRNA. Translation: AAG23782.1.
CR457349 mRNA. Translation: CAG33630.1.
AK027601 mRNA. Translation: BAG51358.1.
CH471165 Genomic DNA. Translation: EAW53712.1.
CH471165 Genomic DNA. Translation: EAW53708.1.
CH471165 Genomic DNA. Translation: EAW53709.1.
BC004956 mRNA. Translation: AAH04956.1.
BC009762 mRNA. Translation: AAH09762.2.
BC018765 mRNA. Translation: AAH18765.2.
BC071887 mRNA. Translation: AAH71887.1.
BC090953 mRNA. Translation: AAH90953.1.
AB063180 mRNA. Translation: BAB70617.1.

IPI

IPI00414021.
IPI00414022.
IPI00514646.
IPI00909892.

RefSeq

NP_291027.3. NM_033549.4.
NP_963921.1. NM_201627.2.

UniGene

Hs.441488.
Hs.700303.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EGM	NMR	-	A	214-263	[»]

ProteinModelPortal

Q8WV44.

SMR

Q8WV44. Positions 11-47, 220-263, 431-617.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WV44. 22 interactions.

MINT

MINT-1377793.

STRING

9606.ENSP00000320869.

PTM databases

PhosphoSite

Q8WV44.

Polymorphism databases

DMDM

116242826.

Proteomic databases

PaxDb

Q8WV44.

PRIDE

Q8WV44.

Protocols and materials databases

DNASU

90933.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315073; ENSP00000320869; ENSG00000146063.
ENST00000351937; ENSP00000336749; ENSG00000146063.

GeneID

90933.

KEGG

hsa:90933.

UCSC

uc003mnc.2. human.
uc003mnd.2. human.
uc003mne.2. human.
uc003mng.1. human.

Organism-specific databases

CTD

90933.

GeneCards

GC05P180649.

H-InvDB

HIX0121034.

HGNC

HGNC:19013. TRIM41.

HPA

HPA021194.
HPA024204.

MIM

610530. gene.

neXtProt

NX_Q8WV44.

PharmGKB

PA134918519.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325772.

HOVERGEN

HBG001357.

InParanoid

Q8WV44.

KO

K12017.

OMA

FWTSGMG.

OrthoDB

EOG47M1XP.

PhylomeDB

Q8WV44.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q8WV44.

Bgee

Q8WV44.

CleanEx

HS_TRIM41.

Genevestigator

Q8WV44.

GermOnline

ENSG00000146063. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 2 hits.

InterPro

IPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR006574. PRY.
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.
[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

ChiTaRS

TRIM41. human.

EvolutionaryTrace

Q8WV44.

GenomeRNAi

90933.

NextBio

77034.

SOURCE

Search...

Entry information

Entry name

TRI41_HUMAN

Accession

Primary (citable) accession number: Q8WV44
Secondary accession number(s): B3KNJ6 , D3DWR9, Q5BKT0, Q7L484, Q96Q10, Q9BSL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 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.