ID   PJA1_HUMAN              Reviewed;         643 AA.
AC   Q8NG27; A2A322; Q5JUT8; Q5JUT9; Q8NG28; Q9HAC1;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=E3 ubiquitin-protein ligase Praja-1;
DE            Short=Praja1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 70;
DE   AltName: Full=RING-type E3 ubiquitin transferase Praja-1 {ECO:0000305};
GN   Name=PJA1; Synonyms=RNF70;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH UBE2D2.
RC   TISSUE=Brain;
RX   PubMed=12036302; DOI=10.1006/geno.2002.6770;
RA   Yu P., Chen Y., Tagle D.A., Cai T.;
RT   "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
RT   chromosome gene abundantly expressed in brain.";
RL   Genomics 79:869-874(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-432
RP   AND ASP-606.
RC   TISSUE=Brain, Kidney, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-643 (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND THR-277, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
CC       Ubiquitinates MAGED1 antigen leading to its subsequent degradation by
CC       proteasome (By similarity). May be involved in protein sorting.
CC       {ECO:0000250, ECO:0000269|PubMed:12036302}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts
CC       with the ubiquitin-conjugating enzyme, UBE2D2.
CC       {ECO:0000269|PubMed:12036302}.
CC   -!- INTERACTION:
CC       Q8NG27; Q9Y5V3: MAGED1; NbExp=7; IntAct=EBI-714606, EBI-716006;
CC       Q8NG27; Q96MG7: NSMCE3; NbExp=3; IntAct=EBI-714606, EBI-2557356;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8NG27-1; Sequence=Displayed;
CC       Name=2; Synonyms=PJA1-beta, Praja1-beta;
CC         IsoId=Q8NG27-2; Sequence=VSP_007518;
CC       Name=3;
CC         IsoId=Q8NG27-3; Sequence=VSP_046995;
CC   -!- TISSUE SPECIFICITY: Expressed in various regions of the brain including
CC       the cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe,
CC       temporal lobe and putamen. Highest levels in the cerebral cortex.
CC       {ECO:0000269|PubMed:12036302}.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC       conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC   -!- PTM: Substrate for E2-dependent ubiquitination.
CC   -!- MISCELLANEOUS: [Isoform 2]: PubMed:12036302 reported that isoform 2
CC       arises by alternative initiation. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF262024; AAM53039.1; -; mRNA.
DR   EMBL; AF264620; AAM53040.1; -; mRNA.
DR   EMBL; AL157699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471132; EAX05367.1; -; Genomic_DNA.
DR   EMBL; BC048323; AAH48323.1; -; mRNA.
DR   EMBL; BC075803; AAH75803.1; -; mRNA.
DR   EMBL; BC105051; AAI05052.1; -; mRNA.
DR   EMBL; BC105053; AAI05054.1; -; mRNA.
DR   EMBL; AK021892; BAB13928.1; ALT_INIT; mRNA.
DR   CCDS; CCDS14392.1; -. [Q8NG27-2]
DR   CCDS; CCDS14393.1; -. [Q8NG27-1]
DR   CCDS; CCDS35316.1; -. [Q8NG27-3]
DR   RefSeq; NP_001027568.1; NM_001032396.2. [Q8NG27-3]
DR   RefSeq; NP_071763.2; NM_022368.4. [Q8NG27-2]
DR   RefSeq; NP_660095.1; NM_145119.3. [Q8NG27-1]
DR   RefSeq; XP_005262349.1; XM_005262292.1.
DR   RefSeq; XP_011529313.1; XM_011531011.2.
DR   PDB; 2L0B; NMR; -; A=564-643.
DR   PDBsum; 2L0B; -.
DR   AlphaFoldDB; Q8NG27; -.
DR   BMRB; Q8NG27; -.
DR   SMR; Q8NG27; -.
DR   BioGRID; 122109; 123.
DR   IntAct; Q8NG27; 29.
DR   STRING; 9606.ENSP00000355014; -.
DR   GlyGen; Q8NG27; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q8NG27; -.
DR   PhosphoSitePlus; Q8NG27; -.
DR   BioMuta; PJA1; -.
DR   DMDM; 31076980; -.
DR   EPD; Q8NG27; -.
DR   jPOST; Q8NG27; -.
DR   MassIVE; Q8NG27; -.
DR   MaxQB; Q8NG27; -.
DR   PaxDb; 9606-ENSP00000355014; -.
DR   PeptideAtlas; Q8NG27; -.
DR   ProteomicsDB; 246; -.
DR   ProteomicsDB; 73411; -. [Q8NG27-1]
DR   ProteomicsDB; 73412; -. [Q8NG27-2]
DR   Pumba; Q8NG27; -.
DR   Antibodypedia; 402; 189 antibodies from 32 providers.
DR   DNASU; 64219; -.
DR   Ensembl; ENST00000361478.1; ENSP00000355014.1; ENSG00000181191.12. [Q8NG27-1]
DR   Ensembl; ENST00000374571.5; ENSP00000363699.3; ENSG00000181191.12. [Q8NG27-3]
DR   Ensembl; ENST00000374583.1; ENSP00000363711.1; ENSG00000181191.12. [Q8NG27-1]
DR   Ensembl; ENST00000374584.3; ENSP00000363712.3; ENSG00000181191.12. [Q8NG27-2]
DR   GeneID; 64219; -.
DR   KEGG; hsa:64219; -.
DR   MANE-Select; ENST00000374571.5; ENSP00000363699.3; NM_001032396.4; NP_001027568.1. [Q8NG27-3]
DR   UCSC; uc004dxg.4; human. [Q8NG27-1]
DR   AGR; HGNC:16648; -.
DR   DisGeNET; 64219; -.
DR   GeneCards; PJA1; -.
DR   HGNC; HGNC:16648; PJA1.
DR   HPA; ENSG00000181191; Tissue enhanced (epididymis).
DR   MIM; 300420; gene.
DR   neXtProt; NX_Q8NG27; -.
DR   OpenTargets; ENSG00000181191; -.
DR   PharmGKB; PA33342; -.
DR   VEuPathDB; HostDB:ENSG00000181191; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000154585; -.
DR   HOGENOM; CLU_026830_1_0_1; -.
DR   InParanoid; Q8NG27; -.
DR   OMA; FNHDVRE; -.
DR   OrthoDB; 5474929at2759; -.
DR   PhylomeDB; Q8NG27; -.
DR   TreeFam; TF330711; -.
DR   PathwayCommons; Q8NG27; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q8NG27; -.
DR   SIGNOR; Q8NG27; -.
DR   BioGRID-ORCS; 64219; 11 hits in 815 CRISPR screens.
DR   GeneWiki; PJA1; -.
DR   GenomeRNAi; 64219; -.
DR   Pharos; Q8NG27; Tbio.
DR   PRO; PR:Q8NG27; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q8NG27; Protein.
DR   Bgee; ENSG00000181191; Expressed in cortical plate and 193 other cell types or tissues.
DR   ExpressionAtlas; Q8NG27; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   CDD; cd16465; RING-H2_PJA1_2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF2; E3 UBIQUITIN-PROTEIN LIGASE PRAJA-1; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q8NG27; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Metal-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..643
FT                   /note="E3 ubiquitin-protein ligase Praja-1"
FT                   /id="PRO_0000055999"
FT   ZN_FING         595..636
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         277
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55176"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55176"
FT   VAR_SEQ         1..55
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046995"
FT   VAR_SEQ         98..285
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12036302"
FT                   /id="VSP_007518"
FT   VARIANT         432
FT                   /note="S -> N (in dbSNP:rs5937160)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_052088"
FT   VARIANT         606
FT                   /note="E -> D (in dbSNP:rs11539157)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_052089"
FT   HELIX           571..575
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   STRAND          579..581
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   STRAND          587..591
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   TURN            596..598
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   STRAND          607..611
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   TURN            612..614
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   STRAND          615..618
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   HELIX           619..626
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   TURN            633..635
FT                   /evidence="ECO:0007829|PDB:2L0B"
FT   STRAND          638..640
FT                   /evidence="ECO:0007829|PDB:2L0B"
SQ   SEQUENCE   643 AA;  71002 MW;  F3DFD1F77809318D CRC64;
     MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT NSEVPMHRSA
     PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP PREYRASGSR RGMAYGHIDS
     YGADDSEEEG AGPVERPPVR GKTGKFKDDK LYDPEKGARS LAGPPPHFSS FSRDVREERD
     KLDPVPAARC SASRADFLPQ SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI
     CGGGENTSKS AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH
     SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF WTHSDDYYKY
     CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE EREPPQAKVS ASTGTSPGPG
     ASASAGAGAG ASAGSNGSNY LEEVREPSLQ EEQASLEEGE IPWLQYHEND SSSEGDNDSG
     HELMQPGVFM LDGNNNLEDD SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL
     EERLAQAMET ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS
     EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPL
//