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Q96Q27 (ASB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin repeat and SOCS box protein 2

Short name=ASB-2
Gene names
Name:ASB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence 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.10 Ref.11

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.10 Ref.11

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.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96Q27-1)

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 2 (identifier: Q96Q27-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MTRFSYAEYFSLFHSCSAPS → MATQISTRGS...RQPAHFYPWT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Ankyrin repeat and SOCS box protein 2
PRO_0000066925

Regions

Repeat56 – 8530ANK 1
Repeat89 – 11931ANK 2
Repeat123 – 15230ANK 3
Repeat156 – 18530ANK 4
Repeat189 – 21830ANK 5
Repeat222 – 25130ANK 6
Repeat255 – 28430ANK 7
Repeat288 – 31730ANK 8
Repeat320 – 34930ANK 9
Repeat362 – 39130ANK 10
Repeat392 – 42130ANK 11
Repeat428 – 45629ANK 12
Domain533 – 58755SOCS box

Natural variations

Alternative sequence1 – 2020MTRFS…CSAPS → MATQISTRGSQCTIGQEEYS LYSSLSEDELVQMAIEQSLA DKTRGPTTAEATASACTNRQ PAHFYPWT in isoform 2.
VSP_043042
Natural variant1601P → S.
Corresponds to variant rs2295213 [ dbSNP | Ensembl ].
VAR_022089

Experimental info

Mutagenesis5481L → P: No interaction with Elongin BC complex. Ref.11
Mutagenesis551 – 5522LC → PF: No interaction with CUL5 or RNF7. Ref.11
Mutagenesis5521C → P: No interaction with Elongin BC complex. Ref.11
Mutagenesis571 – 5744LPLP → AAAA: No interaction with CUL5 or RNF7. Ref.10
Sequence conflict2241Missing in AAD45345. Ref.9
Sequence conflict4601Missing in AAD45345. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA58765,084
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B91E4EB394531076
Show »

FASTA63570,212

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
[3]"Ubiquitin-interacting motif on ankyrin repeat and SOCS box-containing protein (ASB) 2a and its application to purify polyubiquitinated proteins and associated proteins without denaturation."
Kohroki J., Kuroda S., Takiguchi E., Kawakami T., Nakamura T., Nishiyama T., Masuho Y.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney and Stomach.
[5]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Blood.
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-587 (ISOFORM 1).
Tissue: Uterus.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-587 (ISOFORM 1).
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CUL5 AND RNF7, MUTAGENESIS OF 551-LEU-CYS-552 AND 571-LEU--PRO-574.
[11]"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] [Europe PMC] [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.
AB488462 mRNA. Translation: BAI77868.1.
AK303686 mRNA. Translation: BAG64678.1.
AK315628 mRNA. Translation: BAG37996.1.
AL079302 Genomic DNA. No translation available.
AL132642 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81540.1.
CH471061 Genomic DNA. Translation: EAW81542.1.
BC032354 mRNA. Translation: AAH32354.1.
AL137735 mRNA. Translation: CAB70899.1.
AF159164 mRNA. Translation: AAD45345.1.
PIRT46507.
RefSeqNP_001189358.1. NM_001202429.1.
NP_057234.2. NM_016150.4.
XP_005267815.1. XM_005267758.1.
UniGeneHs.510327.

3D structure databases

ProteinModelPortalQ96Q27.
SMRQ96Q27. Positions 28-521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119674. 18 interactions.
IntActQ96Q27. 5 interactions.
MINTMINT-1187414.
STRING9606.ENSP00000320675.

PTM databases

PhosphoSiteQ96Q27.

Polymorphism databases

DMDM20531999.

Proteomic databases

PaxDbQ96Q27.
PRIDEQ96Q27.

Protocols and materials databases

DNASU51676.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315988; ENSP00000320675; ENSG00000100628. [Q96Q27-1]
ENST00000555019; ENSP00000451575; ENSG00000100628. [Q96Q27-2]
GeneID51676.
KEGGhsa:51676.
UCSCuc001ycc.2. human. [Q96Q27-1]
uc001ycd.3. human. [Q96Q27-2]

Organism-specific databases

CTD51676.
GeneCardsGC14M094400.
HGNCHGNC:16012. ASB2.
HPAHPA001546.
MIM605759. gene.
neXtProtNX_Q96Q27.
PharmGKBPA25030.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000034086.
HOVERGENHBG104037.
InParanoidQ96Q27.
KOK10324.
OMARPLAHLC.
OrthoDBEOG77DJ5P.
PhylomeDBQ96Q27.
TreeFamTF315127.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ96Q27.
BgeeQ96Q27.
CleanExHS_ASB2.
GenevestigatorQ96Q27.

Family and domain databases

Gene3D1.25.40.20. 4 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001496. SOCS_C.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF12796. Ank_2. 3 hits.
PF07525. SOCS_box. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 11 hits.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiASB2.
GenomeRNAi51676.
NextBio55678.
PROQ96Q27.
SOURCESearch...

Entry information

Entry nameASB2_HUMAN
AccessionPrimary (citable) accession number: Q96Q27
Secondary accession number(s): B2RDP9 expand/collapse secondary AC list , B4E166, Q9NSU5, Q9Y567
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM