Q96Q27 (ASB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.8 Ref.9
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.8 Ref.9
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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular signal transduction 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 – 587	587	Ankyrin repeat and SOCS box protein 2		PRO_0000066925
Regions
	Repeat	56 – 85	30	ANK 1
	Repeat	89 – 119	31	ANK 2
	Repeat	123 – 152	30	ANK 3
	Repeat	156 – 185	30	ANK 4
	Repeat	189 – 218	30	ANK 5
	Repeat	222 – 251	30	ANK 6
	Repeat	255 – 284	30	ANK 7
	Repeat	288 – 317	30	ANK 8
	Repeat	320 – 349	30	ANK 9
	Repeat	362 – 391	30	ANK 10
	Repeat	392 – 421	30	ANK 11
	Repeat	428 – 456	29	ANK 12
	Domain	533 – 587	55	SOCS box
Natural variations
	Natural variant	160	1	P → S. Corresponds to variant rs2295213 [ dbSNP | Ensembl ].		VAR_022089
Experimental info
	Mutagenesis	548	1	L → P: No interaction with Elongin BC complex. Ref.9
	Mutagenesis	551 – 552	2	LC → PF: No interaction with CUL5 or RNF7. Ref.9
	Mutagenesis	552	1	C → P: No interaction with Elongin BC complex. Ref.9
	Mutagenesis	571 – 574	4	LPLP → AAAA: No interaction with CUL5 or RNF7. Ref.8
	Sequence conflict	224	1	Missing in AAD45345. Ref.7
	Sequence conflict	460	1	Missing in AAD45345. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q96Q27 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 866A2B6010C4C1F9	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

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]	"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: Stomach.
[4]	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].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB056723 mRNA. Translation: BAB64532.1. AJ251238 mRNA. Translation: CAC17765.1. AK315628 mRNA. Translation: BAG37996.1. CH471061 Genomic DNA. Translation: EAW81540.1. BC032354 mRNA. Translation: AAH32354.1. AL137735 mRNA. Translation: CAB70899.1. AF159164 mRNA. Translation: AAD45345.1.
IPI	IPI00939922.
PIR	T46507.
RefSeq	NP_057234.2. NM_016150.4.
UniGene	Hs.510327.
3D structure databases
ProteinModelPortal	Q96Q27.
SMR	Q96Q27. Positions 28-521, 544-582.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96Q27. 1 interaction.
MINT	MINT-1187414.
STRING	Q96Q27.
PTM databases
PhosphoSite	Q96Q27.
Polymorphism databases
DMDM	20531999.
Proteomic databases
PRIDE	Q96Q27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000315988; ENSP00000320675; ENSG00000100628.
GeneID	51676.
KEGG	hsa:51676.
UCSC	uc001ycc.1. human.
Organism-specific databases
CTD	51676.
GeneCards	GC14M094400.
H-InvDB	HIX0011920.
HGNC	HGNC:16012. ASB2.
HPA	HPA001546.
MIM	605759. gene.
neXtProt	NX_Q96Q27.
PharmGKB	PA25030.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19768.
GeneTree	ENSGT00530000063050.
HOVERGEN	HBG104037.
InParanoid	Q96Q27.
PhylomeDB	Q96Q27.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
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. 4 hits.
KO	K10324.
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 4 hits. PF07525. SOCS_box. 1 hit. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 11 hits. SM00969. SOCS_box. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 9 hits. PS50225. SOCS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	55678.
SOURCE	Search...

Entry information

Entry name

ASB2_HUMAN

Accession

Primary (citable) accession number: Q96Q27
Secondary accession number(s): B2RDP9, Q9NSU5, Q9Y567

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.