Ankyrin repeat and SOCS box protein 2

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Reviewed, UniProtKB/Swiss-Prot Q96Q27 (ASB2_HUMAN)

Last modified December 15, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Ankyrin repeat and SOCS box protein 2
Short name=ASB-2

Gene names

Name:

ASB2

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

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Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Ref.6 Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of a probable ECS E3 ubiquitin-protein ligase complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC complex (TCEB1 and TCEB2) and ASB2. Ref.6 Ref.7
Induction	By all-trans retinoic acid (ATRA). Ref.1 Ref.2
Domain	The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes By similarity.
Sequence similarities	Contains 12 ANK repeats. Contains 1 SOCS box domain.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 587

587

Ankyrin repeat and SOCS box protein 2

PRO_0000066925

Regions

Repeat

56 – 85

ANK 1

Repeat

89 – 119

ANK 2

Repeat

123 – 152

ANK 3

Repeat

156 – 185

ANK 4

Repeat

189 – 218

ANK 5

Repeat

222 – 251

ANK 6

Repeat

255 – 284

ANK 7

Repeat

288 – 317

ANK 8

Repeat

320 – 349

ANK 9

Repeat

362 – 391

ANK 10

Repeat

392 – 421

ANK 11

Repeat

428 – 456

ANK 12

Domain

533 – 587

SOCS box

Natural variations

Natural variant

160

P → S: dbSNP rs2295213.

VAR_022089

Experimental info

Mutagenesis

548

L → P: No interaction with Elongin BC complex. Ref.7

Mutagenesis

551 – 552

LC → PF: No interaction with CUL5 or RNF7. Ref.7

Mutagenesis

552

C → P: No interaction with Elongin BC complex. Ref.7

Mutagenesis

571 – 574

LPLP → AAAA: No interaction with CUL5 or RNF7. Ref.6

Sequence conflict

224

Missing in AAD45345. Ref.5

Sequence conflict

460

Missing in AAD45345. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

Q96Q27-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 866A2B6010C4C1F9
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FASTA

587

65,084

        10         20         30         40         50         60 
MTRFSYAEYF SLFHSCSAPS RSTAPPESSP ARAPMGLFQG VMQKYSSSLF KTSQLAPADP 

        70         80         90        100        110        120 
LIKAIKDGDE EALKTMIKEG KNLAEPNKEG WLPLHEAAYY GQVGCLKVLQ RAYPGTIDQR 

       130        140        150        160        170        180 
TLQEETAVYL ATCRGHLDCL LSLLQAGAEP DISNKSRETP LYKACERKNA EAVKILVQHN 

       190        200        210        220        230        240 
ADTNHRCNRG WTALHESVSR NDLEVMQILV SGGAKVESKN AYGITPLFVA AQSGQLEALR 

       250        260        270        280        290        300 
FLAKYGADIN TQASDNASAL YEACKNEHEE VVEFLLSQGA DANKTNKDGL LPLHIASKKG 

       310        320        330        340        350        360 
NYRIVQMLLP VTSRTRIRRS GVSPLHLAAE RNHDEVLEAL LSARFDVNTP LAPERARLYE 

       370        380        390        400        410        420 
DRRSSALYFA VVNNNVYATE LLLQHGADPN RDVISPLLVA IRHGCLRTMQ LLLDHGANID 

       430        440        450        460        470        480 
AYIATHPTAF PATIMFAMKC LSLLKFLMDL GCDGEPCFSC LYGNGPHPPA PQPSSRFNDA 

       490        500        510        520        530        540 
PAADKEPSVV QFCEFVSAPE VSRWAGPIID VLLDYVGNVQ LCSRLKEHID SFEDWAVIKE 

       550        560        570        580 
KAEPPRPLAH LCRLRVRKAI GKYRIKLLDT LPLPGRLIRY LKYENTQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ATRA-regulated Asb-2 gene induced in differentiation of HL-60 leukemia cells." Kohroki J., Fujita S., Itoh N., Yamada Y., Imai H., Yumoto N., Nakanishi T., Tanaka K. FEBS Lett. 505:223-228(2001) [PubMed: 11566180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]	"ASB-2 inhibits growth and promotes commitment in myeloid leukemia cells." Guibal F.C., Moog-Lutz C., Smolewski P., Di Gioia Y., Darzynkiewicz Z., Lutz P.G., Cayre Y.E. J. Biol. Chem. 277:218-224(2002) [PubMed: 11682484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[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]. Tissue: Blood.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-587. Tissue: Uterus.
[5]	"Cloning and characterization of the genes encoding the ankyrin repeat and SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4." Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R., Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J., Alexander W.S. Gene 258:31-41(2000) [PubMed: 11111040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-587.
[6]	"ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase complexes." Kohroki J., Nishiyama T., Nakamura T., Masuho Y. FEBS Lett. 579:6796-6802(2005) [PubMed: 16325183] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CUL5 AND RNF7, MUTAGENESIS OF 551-LEU-CYS-552 AND 571-LEU--PRO-574.
[7]	"ASB2 is an elongin BC-interacting protein that can assemble with cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex." Heuze M.L., Guibal F.C., Banks C.A., Conaway J.W., Conaway R.C., Cayre Y.E., Benecke A., Lutz P.G. J. Biol. Chem. 280:5468-5474(2005) [PubMed: 15590664] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH TCEB1, MUTAGENESIS OF LEU-548 AND CYS-552.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AB056723 mRNA. Translation: BAB64532.1. AJ251238 mRNA. Translation: CAC17765.1. BC032354 mRNA. Translation: AAH32354.1. AL137735 mRNA. Translation: CAB70899.1. AF159164 mRNA. Translation: AAD45345.1.
IPI	IPI00939922.
PIR	T46507.
RefSeq	NP_057234.2.
UniGene	Hs.510327
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q96Q27.
Genome annotation databases
Ensembl	ENST00000315988; ENSP00000320675; ENSG00000100628; Homo sapiens. [Genome view]
GeneID	51676.
KEGG	hsa:51676.
UCSC	uc001ycc.1. human.
Organism-specific databases
CTD	51676.
GeneCards	GC14M093470.
H-InvDB	HIX0011920.
HGNC	HGNC:16012. ASB2.
HPA	HPA001546.
MIM	605759. gene.
PharmGKB	PA25030.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q96Q27.
InParanoid	Q96Q27.
Gene expression databases
ArrayExpress	Q96Q27.
Bgee	Q96Q27.
CleanEx	HS_ASB2.
Genevestigator	Q96Q27.
GermOnline	ENSG00000100628. Homo sapiens.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR001496. SOCS_C. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 2 hits.
Pfam	PF00023. Ank. 10 hits. PF07525. SOCS_box. 1 hit. [Graphical view]
SMART	SM00248. ANK. 11 hits. [Graphical view]
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 9 hits. PS50225. SOCS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55678.
SOURCE	Search...

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Entry information

Entry name

ASB2_HUMAN

Accession

Primary (citable) accession number: Q96Q27
Secondary accession number(s): Q9NSU5, Q9Y567

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	December 1, 2001
Last modified:	December 15, 2009
This is version 75 of the entry and version 1 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.

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