Reviewed, UniProtKB/Swiss-Prot P50876 (R144A_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable E3 ubiquitin-protein ligase RNF144A
    EC=6.3.2.-
Alternative name(s):
    RING finger protein 144A
    Ubiquitin-conjugating enzyme 7-interacting protein 4
    UbcM4-interacting protein 4

Gene names

Name:	RNF144A
Synonyms:	KIAA0161, RNF144, UBCE7IP4

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

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates By similarity.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2L3.
Subcellular location	Membrane; Single-pass membrane proteinPotential.
Sequence similarities	Belongs to the RNF144 family. Contains 2 IBR-type zinc fingers. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 292

292

Probable E3 ubiquitin-protein ligase RNF144A

PRO_0000056298

Regions

Transmembrane

250 – 270

21

Potential

Zinc finger

20 – 69

50

RING-type; degenerate

Zinc finger

91 – 156

66

IBR-type 1

Zinc finger

168 – 232

65

IBR-type 2

Natural variations

Natural variant

4

1

T → A: dbSNP rs364891.

VAR_035375

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

292

Helix Strand Turn

Details...

Beta strand

21 – 23

3

Helix

29 – 31

3

Beta strand

32 – 35

4

Turn

36 – 39

4

Beta strand

40 – 43

4

Helix

44 – 57

14

Helix

78 – 84

7

Helix

87 – 99

13

Sequences

	Sequence		Length	Mass (Da)
	P50876-1 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: E5BE7BC9560DCF93	FASTA	292	32,890
	10 20 30 40 50 60 MTTTRYRPTW DLALDPLVSC KLCLGEYPVE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE 70 80 90 100 110 120 TAISCPDAAC PKQGHLQENE IECMVAAEIM QRYKKLQFER EVLFDPCRTW CPASTCQAVC 130 140 150 160 170 180 QLQDVGLQTP QPVQCKACRM EFCSTCKASW HPGQGCPETM PITFLPGETS AAFKMEEDDA 190 200 210 220 230 240 PIKRCPKCKV YIERDEGCAQ MMCKNCKHAF CWYCLESLDD DFLLIHYDKG PCRNKLGHSR 250 260 270 280 290 ASVIWHRTQV VGIFAGFGLL LLVASPFLLL ATPFVLCCKC KCSKGDDDPL PT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed: 8724849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-4. Tissue: Bone marrow.
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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], VARIANT ALA-4. Tissue: Ovary.
[4]	"A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4." Martinez-Noel G., Niedenthal R., Tamura T., Harbers K. FEBS Lett. 454:257-261(1999) [PubMed: 10431818] [Abstract] Cited for: INTERACTION WITH UBE2L3.
[5]	"Solution structure of the ring finger domain of the human UbcM4-interacting protein 4." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 20-100.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D79983 mRNA. Translation: BAA11478.2. Different initiation.
AC068481 Genomic DNA. Translation: AAX82010.1.
BC050373 mRNA. Translation: AAH50373.1.

RefSeq

NP_055561.2.

UniGene

Hs.699230

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WIM	NMR	-	A	20-100	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSG00000151692. Homo sapiens. [Contig view]

GeneID

9781.

KEGG

hsa:9781.

Organism-specific databases

H-InvDB

HIX0001799.

HGNC

HGNC:20457. RNF144A.

PharmGKB

PA134900632.

HUGE

Search...

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P50876.

HOVERGEN

P50876.

Gene expression databases

ArrayExpress

P50876.

CleanEx

HS_RNF144A.

Family and domain databases

InterPro

IPR002867. Znf_C6HC.
IPR001841. Znf_RING.
[Graphical view]

Pfam

PF01485. IBR. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

SMART

SM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

36828.

Entry information

Entry name

R144A_HUMAN

Accession

Primary (citable) accession number: P50876
Secondary accession number(s): Q585H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 23, 2007
Last modified:	November 25, 2008
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)