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Q27974 (AUXI_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative tyrosine-protein phosphatase auxilin
EC=3.1.3.48
Alternative name(s):
DnaJ homolog subfamily C member 6
Gene names
Name:DNAJC6
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Ref.4

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with HSPA8/HSC70. Interacts with clathrin heavy chains. Ref.3

Tissue specificity

Brain.

Post-translational modification

The N-terminus is blocked.

Target for coat-associated casein kinase II in vitro.

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 J domain.

Contains 1 phosphatase tensin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 910910Putative tyrosine-protein phosphatase auxilin
PRO_0000215902

Regions

Repeat33 – 3641
Repeat37 – 4042
Repeat41 – 4443
Domain52 – 219168Phosphatase tensin-type
Domain225 – 363139C2 tensin-type
Domain846 – 91065J
Region33 – 44123 X 4 AA approximate tandem repeats
Motif406 – 4149SH3-binding Potential
Compositional bias463 – 757295Pro-rich
Compositional bias526 – 5294Poly-Gly

Sites

Active site1611Phosphocysteine intermediate Potential

Amino acid modifications

Modified residue5601Phosphoserine By similarity
Modified residue5671Phosphoserine By similarity

Experimental info

Mutagenesis8471K → C: Strongly reduces interaction with HSPA8. Ref.3
Mutagenesis8491K → C: Slightly reduces interaction with HSPA8. Ref.3
Mutagenesis8761D → A: Loss of interaction with HSPA8. Ref.3

Secondary structure

1 ...................................................................................... 910
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27974 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: BC156DC1CF3487FD

FASTA91099,512
        10         20         30         40         50         60 
MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI QSVTSYTKGD 

        70         80         90        100        110        120 
LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL DHYTVYNLSP KSYRTAKFHS 

       130        140        150        160        170        180 
RVSECSWPIR QAPSLHNLFA VCRNMYNWLL QNPKNVCVVH CLDGRAASSI LVGAMFIFCN 

       190        200        210        220        230        240 
LYSTPGPAVR LLYAKRPGIG LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF 

       250        260        270        280        290        300 
FNKQRNGCRP YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL 

       310        320        330        340        350        360 
RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY PQLFQVTLDV 

       370        380        390        400        410        420 
ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV LGGQAPIDIP PDNPRHFGQG 

       430        440        450        460        470        480 
GFFSTLCWQD QKSEKSFCEE DHAALVNQES EQSDDELLTL SSPHGNANGD KPHAARKPSK 

       490        500        510        520        530        540 
KQQEPAAPAP PEDVDLLGLE GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG 

       550        560        570        580        590        600 
VDDVFHPSGP TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA 

       610        620        630        640        650        660 
SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK SAATSPTGSS 

       670        680        690        700        710        720 
HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG FPPLSSPQKA SPQPMGGGWQ 

       730        740        750        760        770        780 
QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN VSFSSMPGGQ NERGKAAANL EGKQKAADFE 

       790        800        810        820        830        840 
DLLSGQGFNA HKDKKGPRTI AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV 

       850        860        870        880        890        900 
LWAGETKWKP VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE 

       910 
FENQGQKPLY

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References

[1]"Primary structure of the neuronal clathrin-associated protein auxilin and its expression in bacteria."
Schroeder S., Morris S.A., Knorr R., Plessmann U., Weber K., Vinh N.G., Ungewickell E.
Eur. J. Biochem. 228:297-304(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]"1H, 15N, and 13C NMR backbone assignments and secondary structure of the C-terminal recombinant fragment of auxilin including the J-domain."
Han C.J., Gruschus J.M., Greener T., Greene L.E., Ferretti J., Eisenberg E.
J. Biomol. NMR 17:281-282(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 713-910.
[3]"Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface."
Jiang J., Taylor A.B., Prasad K., Ishikawa-Brush Y., Hart P.J., Lafer E.M., Sousa R.
Biochemistry 42:5748-5753(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 810-910, MUTAGENESIS OF LYS-847; LYS-849 AND ASP-876, INTERACTION WITH HSPA8.
[4]"Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating."
Fotin A., Cheng Y., Grigorieff N., Walz T., Harrison S.C., Kirchhausen T.
Nature 432:649-653(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 797-910 IN COMPLEX WITH CLATHRIN COATS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U09237 mRNA. Translation: AAA79037.1.
IPIIPI00707709.
PIRS68983.
RefSeqNP_777261.1. NM_174836.2.
UniGeneBt.111572.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4CNMR-A737-910[»]
1NZ6X-ray2.50A/B810-910[»]
1Q2Gmodel-A776-910[»]
1XI5electron microscopy12.00J/K/L/M/N/O/P/Q/R797-910[»]
2QWNX-ray2.40B812-905[»]
2QWOX-ray1.70B813-904[»]
2QWPX-ray1.75B813-904[»]
2QWQX-ray2.21B813-904[»]
2QWRX-ray2.21B813-904[»]
3N0AX-ray2.20A40-400[»]
DisProtDP00351.
ProteinModelPortalQ27974.
SMRQ27974. Positions 734-910.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-205318.
STRING9913.ENSBTAP00000021828.

Proteomic databases

PRIDEQ27974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID317659.
KEGGbta:317659.

Organism-specific databases

CTD9829.

Phylogenomic databases

eggNOGNOG269956.
HOGENOMHOG000034235.
HOVERGENHBG004322.
InParanoidQ27974.
KOK09526.
OrthoDBEOG4T4CTX.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
InterProIPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR001623. DnaJ_domain.
IPR014019. Phosphatase_tensin-typ.
IPR014020. Tensin_phosphatase_C2-dom.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF46565. DnaJ_N. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ27974.
NextBio20807135.

Entry information

Entry nameAUXI_BOVIN
AccessionPrimary (citable) accession number: Q27974
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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