Reviewed, UniProtKB/Swiss-Prot Q9BYM8 (UB7I3_HUMAN)

Names and origin

Protein names

Recommended name:
    RanBP-type and C3HC4-type zinc finger-containing protein 1
Alternative name(s):
    Ubiquitin-conjugating enzyme 7-interacting protein 3
    Hepatitis B virus X-associated protein 4
    HBV-associated factor 4
    RING finger protein 54

Gene names

Name:	RBCK1
Synonyms:	C20orf18, RNF54, UBCE7IP3, XAP3, XAP4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Might act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates.
Subunit structure	Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C (PRKCZ) and with UBE2L3. Forms homodimers in vitro By similarity. Interacts with PRKCH. Interacts with the HBV pX/HBx protein, which is required to activate transcription of the viral genome.
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Contains 1 B box-type zinc finger. Contains 1 RanBP2-type zinc finger. Contains 1 RING-type zinc finger. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9BYM8-1)

Also known as: RBCK1;

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 3 (identifier: Q9BYM8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE

Isoform 4 (identifier: Q9BYM8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE
     253-272: RKQQQQEGNYLQHVQLDQRS → GVPAGHHPQQPGGGGLLPLH
     273-510: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 510

510

RanBP-type and C3HC4-type zinc finger-containing protein 1

PRO_0000056295

Regions

Domain

55 – 119

65

Ubiquitin-like

Zinc finger

193 – 222

30

RanBP2-type

Zinc finger

282 – 327

46

RING-type

Zinc finger

376 – 411

36

B box-type

Zinc finger

447 – 473

27

B box-like-type

Coiled coil

233 – 261

29

Potential

Amino acid modifications

Modified residue

330

1

Phosphotyrosine Ref.5

Natural variations

Alternative sequence

1 – 55

55

MDEKT…PTQDI → MGTATPDGREDQE in isoform 3 and isoform 4.

VSP_005766

Alternative sequence

253 – 272

20

RKQQQ…LDQRS → GVPAGHHPQQPGGGGLLPLH in isoform 4.

VSP_005767

Alternative sequence

273 – 510

238

Missing in isoform 4.

VSP_005768

Secondary structure

1

.

.

.

.

.

.

.

510

Helix Strand Turn

Details...

Beta strand

184 – 187

4

Turn

190 – 192

3

Beta strand

204 – 206

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (RBCK1) [UniParc]. Last modified January 15, 2008. Version 2. Checksum: C6EF957B1F152FF2	FASTA	510	57,572
	10 20 30 40 50 60 MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS PTQDIRLWVS 70 80 90 100 110 120 VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ WVIGQRLARD QETLHSHGVR 130 140 150 160 170 180 QNGDSAYLYL LSARNTSLNP QELQRERQLR MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE 190 200 210 220 230 240 PGRGQPDAVP EPPPVGWQCP GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL 250 260 270 280 290 300 AGEEEALRQY QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC 310 320 330 340 350 360 LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY QRFLDLGISI 370 380 390 400 410 420 AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL LCKAIHEQMN CKEYQEDLAL 430 440 450 460 470 480 RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC QIVVQKKDGC DWIRCTVCHT EICWVTKGPR 490 500 510 WGPGGPGDTS GGCRCRVNGI PCHPSCQNCH
	Isoform 3. Checksum: 5B4420D28508EE16	FASTA	468	52,936
	10 20 30 40 50 60 MGTATPDGRE DQERLWVSVE DAQMHTVTIW LTVRPDMTVA SLKDMVFLDY GFPPVLQQWV 70 80 90 100 110 120 IGQRLARDQE TLHSHGVRQN GDSAYLYLLS ARNTSLNPQE LQRERQLRML EDLGFKDLTL 130 140 150 160 170 180 QPRGPLEPGP PKPGVPQEPG RGQPDAVPEP PPVGWQCPGC TFINKPTRPG CEMCCRARPE 190 200 210 220 230 240 AYQVPASYQP DEEERARLAG EEEALRQYQQ RKQQQQEGNY LQHVQLDQRS LVLNTEPAEC 250 260 270 280 290 300 PVCYSVLAPG EAVVLRECLH TFCRECLQGT IRNSQEAEVS CPFIDNTYSC SGKLLEREIK 310 320 330 340 350 360 ALLTPEDYQR FLDLGISIAE NRSAFSYHCK TPDCKGWCFF EDDVNEFTCP VCFHVNCLLC 370 380 390 400 410 420 KAIHEQMNCK EYQEDLALRA QNDVAARQTT EMLKVMLQQG EAMRCPQCQI VVQKKDGCDW 430 440 450 460 IRCTVCHTEI CWVTKGPRWG PGGPGDTSGG CRCRVNGIPC HPSCQNCH
	Isoform 4. Checksum: 8EDB1C28B96BF8D4	FASTA	230	25,654
	10 20 30 40 50 60 MGTATPDGRE DQERLWVSVE DAQMHTVTIW LTVRPDMTVA SLKDMVFLDY GFPPVLQQWV 70 80 90 100 110 120 IGQRLARDQE TLHSHGVRQN GDSAYLYLLS ARNTSLNPQE LQRERQLRML EDLGFKDLTL 130 140 150 160 170 180 QPRGPLEPGP PKPGVPQEPG RGQPDAVPEP PPVGWQCPGC TFINKPTRPG CEMCCRARPE 190 200 210 220 230 AYQVPASYQP DEEERARLAG EEEALRQYQQ GVPAGHHPQQ PGGGGLLPLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The hepatitis B virus X-associated protein, XAP3, is a protein kinase C-binding protein." Cong Y.-S., Yao Y.-L., Yang W.-M., Kuzhandaivelu N., Seto E. J. Biol. Chem. 272:16482-16489(1997) [PubMed: 9195957] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PRKCH AND PX OF HBV.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). Tissue: Lung and Placenta.
[4]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[5]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Solution structure of the ZF-RANBP domain of the protein HBV associated factor." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 184-222.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U67322 mRNA. Translation: AAD00162.1.
AL121747 Genomic DNA. Translation: CAC17516.1.
AL121747 Genomic DNA. Translation: CAC28312.2.
BC000983 mRNA. Translation: AAH00983.3.
BC015219 mRNA. Translation: AAH15219.2. Different initiation.

IPI

IPI00010748.
IPI00220104.
IPI00783058.

RefSeq

NP_112506.2.

UniGene

Hs.247280

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CRC	NMR	-	A	194-232	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9BYM8.

Proteomic databases

PRIDE

Q9BYM8.

Genome annotation databases

Ensembl

ENSG00000125826. Homo sapiens. [Contig view]

GeneID

10616.

Organism-specific databases

GeneCards

GC20P000337.

H-InvDB

HIX0015553.

HGNC

HGNC:15864. RBCK1.

MIM

610924. gene.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BYM8.

HOVERGEN

Q9BYM8.

OMA

Q9BYM8. TQDIRLW.

Gene expression databases

ArrayExpress

Q9BYM8.

Bgee

Q9BYM8.

CleanEx

HS_RBCK1.

GermOnline

ENSG00000125826. Homo sapiens.

Family and domain databases

InterPro

IPR019955. Ubiquitin_supergroup.
IPR018957. Znf_C3HC4_RING-type.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00097. zf-C3HC4. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS50053. UBIQUITIN_2. 1 hit.
PS50119. ZF_BBOX. False negative.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

40334.

SOURCE

Search...

Entry information

Entry name

UB7I3_HUMAN

Accession

Primary (citable) accession number: Q9BYM8
Secondary accession number(s): O95623, Q96BS3, Q9BYM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	January 15, 2008
Last modified:	June 16, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)