SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q27974

- AUXI_BOVIN

UniProt

Q27974 - AUXI_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Putative tyrosine-protein phosphatase auxilin

Gene
DNAJC6
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons By similarity.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611Phosphocysteine intermediate Reviewed prediction

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tyrosine-protein phosphatase auxilin (EC:3.1.3.48)
Alternative name(s):
DnaJ homolog subfamily C member 6
Gene namesi
Name:DNAJC6
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi847 – 8471K → C: Strongly reduces interaction with HSPA8. 1 Publication
Mutagenesisi849 – 8491K → C: Slightly reduces interaction with HSPA8. 1 Publication
Mutagenesisi876 – 8761D → A: Loss of interaction with HSPA8. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 910910Putative tyrosine-protein phosphatase auxilinPRO_0000215902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei560 – 5601Phosphoserine By similarity
Modified residuei567 – 5671Phosphoserine By similarity

Post-translational modificationi

The N-terminus is blocked.
Target for coat-associated casein kinase II in vitro.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ27974.

Expressioni

Tissue specificityi

Brain.

Interactioni

Subunit structurei

Interacts with HSPA8/HSC70. Interacts with clathrin heavy chains.1 Publication

Protein-protein interaction databases

DIPiDIP-41952N.
MINTiMINT-205318.
STRINGi9913.ENSBTAP00000021828.

Structurei

Secondary structure

1
910
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 607
Beta strandi62 – 7413
Helixi89 – 9911
Beta strandi103 – 1075
Beta strandi109 – 1113
Helixi114 – 1163
Helixi119 – 1213
Beta strandi122 – 1243
Beta strandi129 – 1313
Helixi135 – 15117
Beta strandi156 – 1616
Helixi166 – 17813
Helixi185 – 19511
Helixi203 – 21614
Beta strandi217 – 2193
Beta strandi228 – 23710
Beta strandi245 – 2484
Beta strandi250 – 2567
Beta strandi259 – 2635
Helixi268 – 2703
Helixi276 – 2783
Beta strandi281 – 2899
Beta strandi291 – 30414
Beta strandi310 – 32314
Helixi324 – 3263
Beta strandi333 – 3375
Helixi338 – 3403
Helixi347 – 3493
Beta strandi355 – 3628
Helixi374 – 3774
Helixi385 – 3884
Helixi392 – 3987
Beta strandi738 – 7403
Beta strandi751 – 7544
Beta strandi757 – 7593
Helixi781 – 7833
Beta strandi786 – 7894
Helixi801 – 8099
Helixi814 – 82613
Helixi830 – 8367
Helixi837 – 8393
Helixi853 – 8553
Beta strandi856 – 8583
Helixi859 – 87214
Helixi875 – 8784
Helixi884 – 90320

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00351.
ProteinModelPortaliQ27974.
SMRiQ27974. Positions 734-910.

Miscellaneous databases

EvolutionaryTraceiQ27974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati33 – 3641
Repeati37 – 4042
Repeati41 – 4443
Domaini52 – 219168Phosphatase tensin-typeAdd
BLAST
Domaini225 – 363139C2 tensin-typeAdd
BLAST
Domaini846 – 91065JAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 44123 X 4 AA approximate tandem repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi406 – 4149SH3-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi463 – 757295Pro-richAdd
BLAST
Compositional biasi526 – 5294Poly-Gly

Sequence similaritiesi

Contains 1 J domain.

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG269956.
HOGENOMiHOG000034235.
HOVERGENiHBG004322.
InParanoidiQ27974.
KOiK09526.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27974-1 [UniParc]FASTAAdd to Basket

« Hide

MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI    50
QSVTSYTKGD LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL 100
DHYTVYNLSP KSYRTAKFHS RVSECSWPIR QAPSLHNLFA VCRNMYNWLL 150
QNPKNVCVVH CLDGRAASSI LVGAMFIFCN LYSTPGPAVR LLYAKRPGIG 200
LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF FNKQRNGCRP 250
YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL 300
RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY 350
PQLFQVTLDV ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV 400
LGGQAPIDIP PDNPRHFGQG GFFSTLCWQD QKSEKSFCEE DHAALVNQES 450
EQSDDELLTL SSPHGNANGD KPHAARKPSK KQQEPAAPAP PEDVDLLGLE 500
GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG VDDVFHPSGP 550
TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA 600
SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK 650
SAATSPTGSS HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG 700
FPPLSSPQKA SPQPMGGGWQ QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN 750
VSFSSMPGGQ NERGKAAANL EGKQKAADFE DLLSGQGFNA HKDKKGPRTI 800
AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV LWAGETKWKP 850
VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE 900
FENQGQKPLY 910
Length:910
Mass (Da):99,512
Last modified:November 1, 1997 - v1
Checksum:iBC156DC1CF3487FD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09237 mRNA. Translation: AAA79037.1.
PIRiS68983.
RefSeqiNP_777261.1. NM_174836.2.
UniGeneiBt.111572.

Genome annotation databases

GeneIDi317659.
KEGGibta:317659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09237 mRNA. Translation: AAA79037.1 .
PIRi S68983.
RefSeqi NP_777261.1. NM_174836.2.
UniGenei Bt.111572.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N4C NMR - A 737-910 [» ]
1NZ6 X-ray 2.50 A/B 810-910 [» ]
1Q2G model - A 776-910 [» ]
1XI5 electron microscopy 12.00 J/K/L/M/N/O/P/Q/R 797-910 [» ]
2QWN X-ray 2.40 B 812-905 [» ]
2QWO X-ray 1.70 B 813-904 [» ]
2QWP X-ray 1.75 B 813-904 [» ]
2QWQ X-ray 2.21 B 813-904 [» ]
2QWR X-ray 2.21 B 813-904 [» ]
3N0A X-ray 2.20 A 40-400 [» ]
DisProti DP00351.
ProteinModelPortali Q27974.
SMRi Q27974. Positions 734-910.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41952N.
MINTi MINT-205318.
STRINGi 9913.ENSBTAP00000021828.

Proteomic databases

PRIDEi Q27974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 317659.
KEGGi bta:317659.

Organism-specific databases

CTDi 9829.

Phylogenomic databases

eggNOGi NOG269956.
HOGENOMi HOG000034235.
HOVERGENi HBG004322.
InParanoidi Q27974.
KOi K09526.

Miscellaneous databases

EvolutionaryTracei Q27974.
NextBioi 20807135.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view ]
Pfami PF00226. DnaJ. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view ]
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEi PS51182. C2_TENSIN. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAUXI_BOVIN
AccessioniPrimary (citable) accession number: Q27974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi