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Reviewed, UniProtKB/Swiss-Prot Q8WXK4 (ASB12_HUMAN)

Last modified July 22, 2008. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Ankyrin repeat and SOCS box protein 12
      Short name=ASB-12
Gene names
Name: ASB12
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with CUL5 and RNF7.

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 5 ANK repeats.

Contains 1 SOCS box domain.

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Ontologies

Keywords

   Biological processUbl conjugation pathway
   DomainANK repeat
Repeat

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 309309Ankyrin repeat and SOCS box protein 12

Regions

Repeat63 – 9230ANK 1
Repeat96 – 12530ANK 2
Repeat129 – 15830ANK 3
Repeat171 – 20030ANK 4
Repeat213 – 24331ANK 5
Domain268 – 30841SOCS box

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Sequences

Sequence LengthMass (Da)Tools
Q8WXK4-1 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: 8280C47C544D03D8

FASTA30933,943
        10         20         30         40         50         60 
MNLMDITKIF SLLQPDKEEE DTDTEEKQAL NQAVYDNDSY TLDQLLRQER YKRFINSRSG 

        70         80         90        100        110        120 
WGVPGTPLRL AASYGHLSCL QVLLAHGADV DSLDVKAQTP LFTAVSHGHL DCVRVLLEAG 

       130        140        150        160        170        180 
ASPGGSIYNN CSPVLTAARD GAVAILQELL DHGAEANVKA KLPVWASNIA SCSGPLYLAA 

       190        200        210        220        230        240 
VYGHLDCFRL LLLHGADPDY NCTDQGLLAR VPRPRTLLEI CLHHNCEPEY IQLLIDFGAN 

       250        260        270        280        290        300 
IYLPSLSLDL TSQDDKGIAL LLQARATPRS LLSQVRLVVR RALCQAGQPQ AINQLDIPPM 


LISYLKHQL

« Hide

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References

« Hide 'large scale' references
[1]"SOCS box proteins."
Kile B.T., Nicola N.A.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-308.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [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].
Tissue: Brain.
[4]"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 AS A E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH CUL5 AND RNF7.

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Cross-references

Sequence databases

AF403030 mRNA. Translation: AAL57349.1.
AL356317 Genomic DNA. Translation: CAI39932.1.
BC069436 mRNA. Translation: AAH69436.1.
BC069555 mRNA. Translation: AAH69555.1.
BC093883 mRNA. Translation: AAH93883.1.
BC104946 mRNA. Translation: AAI04947.1.
RefSeqNP_569059.2.
UniGeneHs.56281

3D structure databases

HSSPHSSP built from PDB template 1AWC based on UniProtKB Q00420.
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000198881. Homo sapiens. [Contig view]
GeneID142689.
KEGGhsa:142689.

Organism-specific databases

HGNCHGNC:19763. ASB12.
PharmGKBPA134937084.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ8WXK4.

Gene expression databases

ArrayExpressQ8WXK4.
CleanExHS_ASB12.
GermOnlineENSG00000198881. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR001496. SOCS_C.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 5 hits.
PF07525. SOCS_box. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 5 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50225. SOCS. False negative.
[Graphical view]
ProDomQ8WXK4.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameASB12_HUMAN
AccessionPrimary (citable) accession number: Q8WXK4
Secondary accession number(s): Q2M3D5, Q52LK4, Q6ISF9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: April 12, 2005
Last modified: July 22, 2008
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome X

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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