[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-561. TISSUE=Mammary gland; DOI=10.1210/me.12.11.1733; PubMed=9817599 [NCBI, ExPASy, EBI, Israel, Japan] Liu H.-L.C., Golder-Novoselsky E., Seto M.H., Webster L., McClary J., Zajchowski D.A.; "The novel estrogen-responsive B box protein (EBBP) gene is tamoxifen regulated in cells expressing an estrogen receptor DNA-binding domain mutant."; Mol. Endocrinol. 12:1733-1748(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-561. DOI=10.1074/jbc.M111233200; PubMed=11919186 [NCBI, ExPASy, EBI, Israel, Japan] Beer H.-D., Munding C., Dubois N., Mamie C., Hohl D., Werner S.; "The estrogen-responsive B box protein: a novel regulator of keratinocyte differentiation."; J. Biol. Chem. 277:20740-20749(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-561. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-561. TISSUE=Placenta, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).

Comments

FUNCTION: May play a role in the regulation of keratinocyte differentiation.
SUBCELLULAR LOCATION: Cytoplasm.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	Alpha
Isoform ID	O95361-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	Beta
Isoform ID	O95361-2
Features which should be applied to build the isoform sequence: VSP_009098.

TISSUE SPECIFICITY: Highest levels found in testis, ovary, small intestine, colon, placenta, heart, skeletal muscle and mammary gland. More highly expressed in the fetus than in the corresponding adult tissues. Expressed in basal keratinocytes.
SIMILARITY: Belongs to the TRIM/RBCC family.
SIMILARITY: Contains 2 B box-type zinc fingers.
SIMILARITY: Contains 1 B30.2/SPRY domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF096870; AAC79080.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457136; CAG33417.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001564; AAH01564.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053514; AAH53514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067096; AAH67096.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00007955; -.
IPI00394650; -.

RefSeq

NP_006461.3; -.

UniGene

Hs.123534

3D structure databases

ModBase

O95361.

Protein-protein interaction databases

IntAct

O95361; 1.

PTM databases

PhosphoSite

O95361; -.

Organism-specific databases

GC17M015472; -.

HIX0013608; -.

HGNC:17241; TRIM16.

609505; gene. [NCBI / EBI]

PharmGKB

PA38215; -.

Gene expression databases

O95361; -.

O95361; -.

HS_TRIM16; -.

ENSG00000108448; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0016605;	Cellular component: PML body (inferred from direct assay from UniProtKB).
GO:0003677;	Molecular function: DNA binding (inferred from direct assay from UniProtKB).
GO:0019966;	Molecular function: interleukin-1 binding (inferred from physical interaction from UniProtKB).
GO:0032089;	Molecular function: NACHT domain binding (inferred from physical interaction from UniProtKB).
GO:0016563;	Molecular function: transcription activator activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0043966;	Biological process: histone H3 acetylation (inferred from direct assay from UniProtKB).
GO:0043967;	Biological process: histone H4 acetylation (inferred from direct assay from UniProtKB).
GO:0043193;	Biological process: positive regulation of gene-specific transcription (inferred from direct assay from UniProtKB).
GO:0050718;	Biological process: positive regulation of interleukin-1 beta secretion (inferred from mutant phenotype from UniProtKB).
GO:0045618;	Biological process: positive regulation of keratinocyte differentiation (inferred from direct assay from UniProtKB).
GO:0048386;	Biological process: positive regulation of retinoic acid receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0060416;	Biological process: response to growth hormone stimulus (inferred from direct assay from UniProtKB).
GO:0046683;	Biological process: response to organophosphorus (inferred from expression pattern from UniProtKB).
GO:0032526;	Biological process: response to retinoic acid (inferred from expression pattern from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001870; B302.
IPR003879; Butyrophylin.
IPR006574; PRY.
IPR018355; SPla/RYanodine_receptor_sg.
IPR003877; SPRY_rcpt.
IPR000315; Znf_B-box.
Graphical view of domain structure.

Pfam

PF00622; SPRY; 1.
PF00643; zf-B_box; 1.
Pfam graphical view of domain structure.

PRINTS

PR01407; BUTYPHLNCDUF.

SMART

SM00336; BBOX; 2.
SM00589; PRY; 1.
SM00449; SPRY; 1.
SMART graphical view of domain structure.

PROSITE

PS50188; B302_SPRY; 1.
PS50119; ZF_BBOX; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O95361; -.

Genome annotation databases

Ensembl

ENSG00000108448; Homo sapiens. [Contig view]

GeneID

10626; -.

KEGG

hsa:10626; -.

Phylogenomic databases

HOVERGEN

O95361; -.

OMA

O95361; AENAINK.

Other

NextBio

40372; -.

SOURCE

TRIM16; Homo sapiens.

ProtoNet

O95361.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Polymorphism; Repeat; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 564`	`564`	`Tripartite motif-containing protein 16.`	`PRO_0000056222`
`DOMAIN`	`355 553`	`199`	`B30.2/SPRY.`
`ZN_FING`	`72 122`	`51`	`B box-type 1.`
`ZN_FING`	`126 165`	`40`	`B box-type 2.`
`COILED`	`165 203`	`39`	`Potential.`
`COILED`	`243 274`	`32`	`Potential.`
`COILED`	`320 340`	`21`	`Potential.`
`MOD_RES`	`60 60`		`Phosphoserine.`
`VAR_SEQ`	`1 216`		`Missing (in isoform 2).`	`VSP_009098`
`VARIANT`	`121 121`	`1`	`E -> D (in dbSNP:rs2074890 [NCBI]).`	`VAR_017412`
`VARIANT`	`493 493`	`1`	`R -> W (in dbSNP:rs3174720 [NCBI]).`	`VAR_052133`
`VARIANT`	`561 561`	`1`	`G -> V (in dbSNP:rs1060903 [NCBI]).`	`VAR_031668`
`CONFLICT`	`235 235`		`L -> P (in Ref. 1; AAC79080 and 2).`
`CONFLICT`	`246 246`		`S -> N (in Ref. 1; AAC79080 and 2).`
`CONFLICT`	`465 465`		`F -> L (in Ref. 4; AAH01564).`
`CONFLICT`	`521 521`		`K -> N (in Ref. 1; AAC79080 and 2).`
`CONFLICT`	`541 541`		`N -> S (in Ref. 1; AAC79080 and 2).`

Sequence information

Length: 564 AA [This is the length of the unprocessed precursor]

Molecular weight: 63955 Da [This is the MW of the unprocessed precursor]

CRC64: A6760717937D82F8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAELDLMAPG PLPRATAQPP APLSPDSGSP SPDSGSASPV EEEDVGSSEK LGRETEEQDS 

        70         80         90        100        110        120 
DSAEQGDPAG EGKEVLCDFC LDDTRRVKAV KSCLTCMVNY CEEHLQPHQV NIKLQSHLLT 

       130        140        150        160        170        180 
EPVKDHNWRY CPAHHSPLSA FCCPDQQCIC QDCCQEHSGH TIVSLDAARR DKEAELQCTQ 

       190        200        210        220        230        240 
LDLERKLKLN ENAISRLQAN QKSVLVSVSE VKAVAEMQFG ELLAAVRKAQ ANVMLFLEEK 

       250        260        270        280        290        300 
EQAALSQANG IKAHLEYRSA EMEKSKQELE RMAAISNTVQ FLEEYCKFKN TEDITFPSVY 

       310        320        330        340        350        360 
VGLKDKLSGI RKVITESTVH LIQLLENYKK KLQEFSKEEE YDIRTQVSAV VQRKYWTSKP 

       370        380        390        400        410        420 
EPSTREQFLQ YAYDITFDPD TAHKYLRLQE ENRKVTNTTP WEHPYPDLPS RFLHWRQVLS 

       430        440        450        460        470        480 
QQSLYLHRYY FEVEIFGAGT YVGLTCKGID RKGEERNSCI SGNNFSWSLQ WNGKEFTAWY 

       490        500        510        520        530        540 
SDMETPLKAG PFRRLGVYID FPGGILSFYG VEYDTMTLVH KFACKFSEPV YAAFWLSKKE 

       550        560 
NAIRIVDLGE EPEKPAPSLV GTAP

O95361 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools