Reviewed, UniProtKB/Swiss-Prot Q9Y4X5 (ARI1_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein ariadne-1 homolog
      Short name=ARI-1
Alternative name(s):
    Ubiquitin-conjugating enzyme E2-binding protein 1
    UbcH7-binding protein
    UbcM4-interacting protein
    HHARI
    H7-AP2
    Monocyte protein 6
      Short name=MOP-6

Gene names

Name:	ARIH1
Synonyms:	ARI, MOP6, UBCH7BP
ORF Names:	HUSSY-27

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	557 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 UBE2L3. Ref.10
Subcellular location	Cytoplasm. Note: Mainly cytoplasmic.
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the RBR family. Ariadne subfamily. Contains 1 IBR-type zinc finger. Contains 2 RING-type zinc fingers.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	protein binding Ref.1 Inferred from physical interaction. Source: UniProtKB small conjugating protein ligase activity Ref.1 Traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 557

557

Protein ariadne-1 homolog

PRO_0000055752

Regions

Zinc finger

186 – 236

51

RING-type 1; atypical

Zinc finger

256 – 317

62

IBR-type

Zinc finger

344 – 375

32

RING-type 2

Region

186 – 254

69

Interaction with UBE2L3

Coiled coil

433 – 449

17

Potential

Compositional bias

10 – 38

29

Asp/Glu-rich (acidic)

Compositional bias

51 – 92

42

Gly-rich

Experimental info

Mutagenesis

187 – 188

2

QI → HV: No loss of interaction with UBE2L3. Ref.10

Mutagenesis

188

1

I → A: Loss of interaction with UBE2L3. Ref.10

Mutagenesis

208

1

C → A or H: Loss of interaction with UBE2L3. Ref.10

Mutagenesis

258

1

Y → A: No loss of interaction with UBE2L3. Ref.10

Sequence conflict

122

1

E → D in AAD28088. Ref.2

Sequence conflict

237

1

D → N in CAA10274. Ref.3

Sequence conflict

303

1

F → S in CAA08817. Ref.7

Sequence conflict

309 – 316

8

ENWHDPVK → AIGMILFQ in CAA08817. Ref.7

Sequence conflict

322

1

K → T in CAA08817. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

557

Helix Strand Turn

Details...

Turn

345 – 347

3

Beta strand

359 – 361

3

Helix

366 – 368

3

Beta strand

372 – 375

4

Helix

380 – 383

4

Beta strand

385 – 389

5

Sequences

	Sequence		Length	Mass (Da)
	Q9Y4X5-1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: DFFF8965DAB41DC8	FASTA	557	64,118
	10 20 30 40 50 60 MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDTL DLGEVELVEP GLGVGGERDG 70 80 90 100 110 120 LLCGETGGGG GSALGPGGGG GGGGGGGGGG PGHEQEEDYR YEVLTAEQIL QHMVECIREV 130 140 150 160 170 180 NEVIQNPATI TRILLSHFNW DKEKLMERYF DGNLEKLFAE CHVINPSKKS RTRQMNTRSS 190 200 210 220 230 240 AQDMPCQICY LNYPNSYFTG LECGHKFCMQ CWSEYLTTKI MEEGMGQTIS CPAHGCDILV 250 260 270 280 290 300 DDNTVMRLIT DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG 310 320 330 340 350 360 RQFCFNCGEN WHDPVKCKWL KKWIKKCDDD SETSNWIAAN TKECPKCHVT IEKDGGCNHM 370 380 390 400 410 420 VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA RDAQERSRAA LQRYLFYCNR 430 440 450 460 470 480 YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM SWIEVQFLKK AVDVLCQCRA TLMYTYVFAF 490 500 510 520 530 540 YLKKNNQSII FENNQADLEN ATEVLSGYLE RDISQDSLQD IKQKVQDKYR YCESRRRVLL 550 QHVHEGYEKD LWEYIED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1." Moynihan T.P., Ardley H.C., Nuber U., Rose S.A., Jones P.F., Markham A.F., Scheffner M., Robinson P.A. J. Biol. Chem. 274:30963-30968(1999) [PubMed: 10521492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	Ardley H.C. Unpublished observations (MAY-2002) Cited for: SEQUENCE REVISION TO 227.
[3]	"Human ariadne homolog." Trockenbacher A., Marksteiner R., Schneider R. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Ariadne-1: a vital Drosophila gene is required in development and defines a new conserved family of ring-finger proteins." Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A. Genetics 155:1231-1244(2000) [PubMed: 10880484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-557.
[8]	"Characterization of 16 novel human genes showing high similarity to yeast sequences." Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G. Yeast 18:69-80(2001) [PubMed: 11124703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 298-557. Tissue: Brain.
[9]	"Molecular and biological characterization of a new ring finger protein, MOP-6 which is highly expressed in activated human monocytes." Fujii Y., Takayama K., Ukai Y., Yoshimoto M. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-557. Tissue: Monocyte.
[10]	"Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7." Ardley H.C., Tan N.G.S., Rose S.A., Markham A.F., Robinson P.A. J. Biol. Chem. 276:19640-19647(2001) [PubMed: 11278816] [Abstract] Cited for: INTERACTION WITH UBE2L3, MUTAGENESIS OF 187-GLN-ILE-188; ILE-188; CYS-208 AND TYR-258.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ243190 mRNA. Translation: CAB45870.1. Sequence problems.
AF072832 mRNA. Translation: AAD28088.1.
AK312715 mRNA. Translation: BAG35590.1.
CH471082 Genomic DNA. Translation: EAW77907.1.
BC051877 mRNA. Translation: AAH51877.1.
AJ130976 mRNA. Translation: CAA10274.1.
AJ009771 mRNA. Translation: CAA08817.1.
AB014774 mRNA. Translation: BAB19786.1.

IPI

IPI00294943.

RefSeq

NP_005735.2.

UniGene

Hs.268787

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WD2	NMR	-	A	336-394	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9Y4X5.

Proteomic databases

PeptideAtlas

Q9Y4X5.

PRIDE

Q9Y4X5.

Genome annotation databases

Ensembl

ENST00000379887; ENSP00000369217; ENSG00000166233; Homo sapiens. [Genome view]

GeneID

25820.

KEGG

hsa:25820.

UCSC

uc002aut.2. human.

Organism-specific databases

CTD

25820.

GeneCards

GC15P070553.

H-InvDB

HIX0012409.
HIX0022573.

HGNC

HGNC:689. ARIH1.

HPA

HPA003295.

MIM

605624. gene.

PharmGKB

PA24982.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y4X5.

HOVERGEN

Q9Y4X5.

OMA

QCRQTLM

OrthoDB

EOG9SXQZ2

Gene expression databases

ArrayExpress

Q9Y4X5.

Bgee

Q9Y4X5.

CleanEx

HS_ARIH1.

Genevestigator

Q9Y4X5.

GermOnline

ENSG00000166233. Homo sapiens.

Family and domain databases

InterPro

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

Pfam

PF01485. IBR. 1 hit.
[Graphical view]

SMART

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

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

47071.

SOURCE

Search...

Entry information

Entry name

ARI1_HUMAN

Accession

Primary (citable) accession number: Q9Y4X5
Secondary accession number(s): B2R6U3 , O76026, Q9H3T6, Q9UEN0, Q9UP39

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 10, 2002
Last modified:	November 24, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.