PRKN_PEDHC
ID PRKN_PEDHC Reviewed; 461 AA.
AC E0VIU9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000303|PubMed:26161729};
DE EC=2.3.2.31 {ECO:0000269|PubMed:26161729};
GN Name=park {ECO:0000250|UniProtKB:Q7KTX7};
GN Synonyms=parkin {ECO:0000303|PubMed:26161729};
GN ORFNames=Phum_PHUM233570 {ECO:0000312|EMBL:EEB13305.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224 {ECO:0000312|Proteomes:UP000009046};
RN [1] {ECO:0000312|Proteomes:UP000009046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA {ECO:0000312|Proteomes:UP000009046};
RX PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., Clark J.M.,
RA Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., Gerlach D.,
RA Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., Veenstra J.A.,
RA Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., Johnston J.S., Reese J.T.,
RA Popadic A., Tojo M., Raoult D., Reed D.L., Tomoyasu Y., Krause E.,
RA Mittapalli O., Margam V.M., Li H.M., Meyer J.M., Johnson R.M.,
RA Romero-Severson J., Vanzee J.P., Alvarez-Ponce D., Vieira F.G., Aguade M.,
RA Guirao-Rico S., Anzola J.M., Yoon K.S., Strycharz J.P., Unger M.F.,
RA Christley S., Lobo N.F., Seufferheld M.J., Wang N., Dasch G.A.,
RA Struchiner C.J., Madey G., Hannick L.I., Bidwell S., Joardar V., Caler E.,
RA Shao R., Barker S.C., Cameron S., Bruggner R.V., Regier A., Johnson J.,
RA Viswanathan L., Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M.,
RA Venter J.C., Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA Pittendrigh B.R.;
RT "Genome sequences of the human body louse and its primary endosymbiont
RT provide insights into the permanent parasitic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
RN [2] {ECO:0007744|PDB:5CAW}
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 141-461 IN COMPLEX WITH ZINC,
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=26161729; DOI=10.1038/nature14879;
RA Wauer T., Simicek M., Schubert A., Komander D.;
RT "Mechanism of phospho-ubiquitin-induced PARKIN activation.";
RL Nature 524:370-374(2015).
RN [3] {ECO:0000305}
RP ERRATUM OF PUBMED:26161729.
RX PubMed=26416742; DOI=10.1038/nature15531;
RA Wauer T., Simicek M., Schubert A., Komander D.;
RL Nature 526:728-728(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates, such as Marf,
CC Opa1, Sep1, Tom20 and porin (By similarity). Mediates
CC monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and
CC 'Lys-63'-linked polyubiquitination of substrates, depending on the
CC context (PubMed:26161729). Protects against mitochondrial dysfunction
CC during cellular stress, by acting downstream of Pink1, to coordinate
CC mitochondrial quality control mechanisms that remove and replace
CC dysfunctional mitochondrial components (By similarity). Depending on
CC the severity of mitochondrial damage and/or dysfunction, activity
CC ranges from preventing apoptosis and stimulating mitochondrial
CC biogenesis to regulating mitochondrial dynamics and eliminating
CC severely damaged mitochondria via mitophagy (By similarity). Appears to
CC be particularly important in maintaining the physiology and function of
CC cells with high energy demands that are undergoing stress or altered
CC metabolic environment, including spermatids, muscle cells and neurons
CC such as the dopaminergic (DA) neurons (By similarity). Activation and
CC recruitment onto the outer membrane of damaged/dysfunctional
CC mitochondria (OMM) requires Pink1-mediated phosphorylation of both park
CC and ubiquitin (By similarity). In depolarized mitochondria, mediates
CC the decision between mitophagy or preventing apoptosis by inducing
CC either the poly- or monoubiquitination of porin/VDAC;
CC polyubiquitination of porin promotes mitophagy, while
CC monoubiquitination of porin decreases mitochondrial calcium influx
CC which ultimately inhibits apoptosis (By similarity). When cellular
CC stress results in irreversible mitochondrial damage, promotes the
CC autophagic degradation of dysfunctional depolarized mitochondria
CC (mitophagy) by promoting the ubiquitination of mitochondrial proteins
CC (By similarity). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-
CC 63'-linked polyubiquitin chains following mitochondrial damage, leading
CC to mitophagy (By similarity). In developing tissues, inhibits JNK-
CC mediated apoptosis by negatively regulating bsk transcription (By
CC similarity). The Pink1-park pathway also promotes fission and/or
CC inhibits fusion of damaged mitochondria by mediating the ubiquitination
CC and subsequent degradation of proteins involved in mitochondrial
CC fusion/fission such as Marf and Opa1 (By similarity). This prevents the
CC refusion of unhealthy mitochondria with the healthy mitochondrial
CC network and/or initiates mitochondrial fragmentation facilitating their
CC later engulfment by autophagosomes (By similarity). Regulates motility
CC of damaged mitochondria by phosphorylating Miro which likely promotes
CC its park-dependent degradation by the proteasome; in motor neurons,
CC this inhibits mitochondrial intracellular anterograde transport along
CC the axons which probably increases the chance of the mitochondria being
CC eliminated in the soma (By similarity). The Pink1-park pathway is also
CC involved in mitochondrial regeneration processes such as promoting
CC mitochondrial biogenesis, activating localized mitochondrial repair,
CC promoting selective turnover of mitochondrial proteins and initiating
CC the mitochondrial import of endogenous proteins (By similarity).
CC Involved in mitochondrial biogenesis via the ubiquitination of
CC transcriptional repressor Paris which leads to its subsequent
CC proteasomal degradation and allows activation of the transcription
CC factor srl (By similarity). Promotes localized mitochondrial repair by
CC activating the translation of specific nuclear-encoded mitochondrial
CC RNAs (nc-mtRNAs) on the mitochondrial surface, including several key
CC electron transport chain component nc-mtRNAs (By similarity).
CC {ECO:0000250|UniProtKB:Q7KTX7, ECO:0000269|PubMed:26161729}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000269|PubMed:26161729};
CC -!- ACTIVITY REGULATION: In the autoinhibited state the side chain of Phe-
CC 460 inserts into a hydrophobic groove in RING-0, occluding the
CC ubiquitin acceptor site Cys-428, whereas the REP repressor element
CC binds RING-1 and blocks its E2-binding site (PubMed:26161729).
CC Activation of park requires 2 steps: (1) phosphorylation at Ser-92 by
CC Pink1 and (2) binding to phosphorylated ubiquitin, leading to unlock
CC repression of the catalytic Cys-428 by the RING-0 region via an
CC allosteric mechanism and converting park to its fully-active form
CC (PubMed:26161729). According to another report, phosphorylation at Ser-
CC 92 by Pink1 is not essential for activation and only binding to
CC phosphorylated ubiquitin is essential to unlock repression (By
CC similarity). {ECO:0000250|UniProtKB:O60260,
CC ECO:0000269|PubMed:26161729}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:26161729}.
CC -!- SUBUNIT: Forms an E3 ubiquitin ligase complex with E2 ubiquitin-
CC conjugating enzymes. {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7KTX7}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7KTX7}. Note=Translocates
CC from the cytosol to dysfunctional mitochondria that have lost their
CC mitochondrial membrane potential; recruitment to mitochondria is Pink1-
CC dependent. {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- DOMAIN: The RING-type 1 zinc finger domain is required for
CC ubiquitination activity. {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases (By
CC similarity). They interact with E2 conjugating enzymes and function
CC like HECT-type E3 enzymes: they bind E2s via the first RING domain, but
CC require an obligate trans-thiolation step during the ubiquitin
CC transfer, requiring a conserved cysteine residue in the second RING
CC domain (By similarity). {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own
CC degradation. {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- PTM: Phosphorylated (By similarity). Activation requires
CC phosphorylation at Ser-92 by Pink1 and binding to Pink1-phosphorylated
CC polyubiquitin chains (By similarity). Phosphorylation at Thr-176 by
CC Pink1 is also important for mitochondrial localization (By similarity).
CC {ECO:0000250|UniProtKB:Q7KTX7}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily. {ECO:0000305}.
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DR EMBL; AAZO01002709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235206; EEB13305.1; -; Genomic_DNA.
DR RefSeq; XP_002426043.1; XM_002425998.1.
DR PDB; 5CAW; X-ray; 2.62 A; A/C=141-461.
DR PDBsum; 5CAW; -.
DR SMR; E0VIU9; -.
DR DIP; DIP-61596N; -.
DR STRING; 121225.PHUM233570-PA; -.
DR EnsemblMetazoa; PHUM233570-RA; PHUM233570-PA; PHUM233570.
DR GeneID; 8230172; -.
DR KEGG; phu:Phum_PHUM233570; -.
DR CTD; 8230172; -.
DR VEuPathDB; VectorBase:PHUM233570; -.
DR eggNOG; KOG0006; Eukaryota.
DR HOGENOM; CLU_050804_0_0_1; -.
DR InParanoid; E0VIU9; -.
DR OMA; FAEFFFK; -.
DR PhylomeDB; E0VIU9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009046; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR003977; Parkin.
DR InterPro; IPR041565; Parkin_Znf-RING.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR041170; Znf-RING_14.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF17976; zf-RING_12; 1.
DR Pfam; PF17978; zf-RING_14; 1.
DR PIRSF; PIRSF037880; Parkin; 1.
DR PRINTS; PR01475; PARKIN.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..461
FT /note="E3 ubiquitin-protein ligase parkin"
FT /id="PRO_0000454928"
FT DOMAIN 30..90
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 145..227
FT /note="RING-type 0; atypical"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT ZN_FING 240..295
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 315..373
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 411..452
FT /note="IBR-type"
FT /evidence="ECO:0000255"
FT ZN_FING 415..446
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 236..461
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:26161729, ECO:0007744|PDB:5CAW"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:26161729,
FT ECO:0007744|PDB:5CAW"
FT SITE 304
FT /note="Implicated in binding to phosphorylated ubiquitin"
FT /evidence="ECO:0000269|PubMed:26161729"
FT SITE 307
FT /note="Implicated in binding to phosphorylated ubiquitin"
FT /evidence="ECO:0000269|PubMed:26161729"
FT SITE 314
FT /note="Implicated in binding to phosphorylated ubiquitin"
FT /evidence="ECO:0000269|PubMed:26161729"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KTX7"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KTX7"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 206..216
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5CAW"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5CAW"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:5CAW"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:5CAW"
SQ SEQUENCE 461 AA; 51864 MW; B874A02614DC7C52 CRC64;
MSILEWFWNI LCGMAQYLTF SKNLTNDNLV NIYVKSNVGG TISVNLDPKS DIKNVKELVA
PKLGLEPDDV KIIFAGKELL DSTVIEVLDF FSDILHAVKV NKKIKNVIPD KPLCETLEEL
HQLNDQKNVE SIEESNLKNE GKNKAHFFIY CANPCKKINT GKLRVCCSEC KHGAFTVDTD
PQSWADVLDK NKITGVCNNV GCEGLYAKFY FKCASHPSQG ENDTAVPLNL IKRNHKKIPC
LACTDICDPV LVFSCDNRHV TCLECFKNYC GSRLKDRQFL SHPDFGYTLP CPAGCSNSFI
EEVHHFRLLT DAQYEQYHRF ATEEFILQAG GVLCPQPGCG QGILIDQNCN RVQCSCGYVF
CGKCLEGFHL GECLNPTDVP FLSQNCDYPL DPEKLEKARW DEASSTVIKV LTKPCPKCRT
STERAGGCMH MICTRANCGF HWCWVCQGPW ERDCMASHWF G
