DPF1_HUMAN
ID DPF1_HUMAN Reviewed; 387 AA.
AC Q92782; B3KSY8; Q08AJ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc finger protein neuro-d4 {ECO:0000305};
DE AltName: Full=BRG1-associated factor 45B;
DE Short=BAF45B;
DE AltName: Full=D4, zinc and double PHD fingers family 1;
GN Name=DPF1 {ECO:0000312|HGNC:HGNC:20225}; Synonyms=BAF45B, NEUD4;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8812431; DOI=10.1006/geno.1996.0440;
RA Chestkov A.V., Baka I.D., Kost M.V., Georgiev G.P., Buchman V.L.;
RT "The d4 gene family in the human genome.";
RL Genomics 36:174-177(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala, and Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-129 AND LYS-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May have an important role in developing neurons by
CC participating in regulation of cell survival, possibly as a
CC neurospecific transcription factor. Belongs to the neuron-specific
CC chromatin remodeling complex (nBAF complex). During neural development
CC a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC mechanism occurs as neurons exit the cell cycle and become committed to
CC their adult state. The transition from proliferating neural
CC stem/progenitor cells to postmitotic neurons requires a switch in
CC subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of neuron-specific chromatin remodeling complex
CC (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q92782-2; Q92870-2: APBB2; NbExp=3; IntAct=EBI-23669343, EBI-21535880;
CC Q92782-2; P55212: CASP6; NbExp=3; IntAct=EBI-23669343, EBI-718729;
CC Q92782-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-23669343, EBI-25837549;
CC Q92782-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-23669343, EBI-10976677;
CC Q92782-2; Q01658: DR1; NbExp=3; IntAct=EBI-23669343, EBI-750300;
CC Q92782-2; P41091: EIF2S3; NbExp=3; IntAct=EBI-23669343, EBI-1054228;
CC Q92782-2; O75460-2: ERN1; NbExp=3; IntAct=EBI-23669343, EBI-25852368;
CC Q92782-2; P22607: FGFR3; NbExp=3; IntAct=EBI-23669343, EBI-348399;
CC Q92782-2; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-23669343, EBI-10226858;
CC Q92782-2; P14136: GFAP; NbExp=3; IntAct=EBI-23669343, EBI-744302;
CC Q92782-2; P62873: GNB1; NbExp=3; IntAct=EBI-23669343, EBI-357130;
CC Q92782-2; P06396: GSN; NbExp=3; IntAct=EBI-23669343, EBI-351506;
CC Q92782-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-23669343, EBI-1054873;
CC Q92782-2; P54652: HSPA2; NbExp=3; IntAct=EBI-23669343, EBI-356991;
CC Q92782-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-23669343, EBI-21591415;
CC Q92782-2; O00483: NDUFA4; NbExp=3; IntAct=EBI-23669343, EBI-1049381;
CC Q92782-2; O43189: PHF1; NbExp=3; IntAct=EBI-23669343, EBI-530034;
CC Q92782-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-23669343, EBI-5280197;
CC Q92782-2; P62826: RAN; NbExp=3; IntAct=EBI-23669343, EBI-286642;
CC Q92782-2; P53985-2: SLC16A1; NbExp=3; IntAct=EBI-23669343, EBI-25891616;
CC Q92782-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-23669343, EBI-5235340;
CC Q92782-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-23669343, EBI-372899;
CC Q92782-2; Q8NE91: TM4SF1; NbExp=3; IntAct=EBI-23669343, EBI-25875545;
CC Q92782-2; Q9Y649; NbExp=3; IntAct=EBI-23669343, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=2;
CC IsoId=Q92782-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q92782-1; Sequence=VSP_061235, VSP_061236;
CC Name=3;
CC IsoId=Q92782-3; Sequence=VSP_061234;
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; U43843; AAC50685.1; -; mRNA.
DR EMBL; AK094632; BAG52900.1; -; mRNA.
DR EMBL; AC011479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW56763.1; -; Genomic_DNA.
DR EMBL; BC125153; AAI25154.1; -; mRNA.
DR CCDS; CCDS33008.2; -. [Q92782-1]
DR CCDS; CCDS46064.1; -. [Q92782-2]
DR CCDS; CCDS46065.1; -. [Q92782-3]
DR RefSeq; NP_001128627.1; NM_001135155.2.
DR RefSeq; NP_001128628.1; NM_001135156.2. [Q92782-3]
DR RefSeq; NP_001276907.1; NM_001289978.1.
DR RefSeq; NP_004638.2; NM_004647.3.
DR AlphaFoldDB; Q92782; -.
DR SMR; Q92782; -.
DR BioGRID; 113836; 86.
DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR IntAct; Q92782; 85.
DR MINT; Q92782; -.
DR iPTMnet; Q92782; -.
DR PhosphoSitePlus; Q92782; -.
DR SwissPalm; Q92782; -.
DR BioMuta; DPF1; -.
DR DMDM; 313104100; -.
DR EPD; Q92782; -.
DR jPOST; Q92782; -.
DR MassIVE; Q92782; -.
DR MaxQB; Q92782; -.
DR PeptideAtlas; Q92782; -.
DR PRIDE; Q92782; -.
DR ProteomicsDB; 75460; -. [Q92782-1]
DR ProteomicsDB; 75461; -. [Q92782-2]
DR ProteomicsDB; 75462; -. [Q92782-3]
DR Antibodypedia; 16434; 179 antibodies from 28 providers.
DR DNASU; 8193; -.
DR Ensembl; ENST00000355526.10; ENSP00000347716.5; ENSG00000011332.22. [Q92782-2]
DR Ensembl; ENST00000412732.5; ENSP00000412098.1; ENSG00000011332.22. [Q92782-3]
DR Ensembl; ENST00000414789.5; ENSP00000391884.1; ENSG00000011332.22. [Q92782-3]
DR Ensembl; ENST00000420980.8; ENSP00000397354.3; ENSG00000011332.22. [Q92782-1]
DR GeneID; 8193; -.
DR KEGG; hsa:8193; -.
DR MANE-Select; ENST00000355526.10; ENSP00000347716.5; NM_001135155.3; NP_001128627.2.
DR UCSC; uc002ohl.4; human. [Q92782-2]
DR CTD; 8193; -.
DR DisGeNET; 8193; -.
DR GeneCards; DPF1; -.
DR HGNC; HGNC:20225; DPF1.
DR HPA; ENSG00000011332; Tissue enriched (brain).
DR MIM; 601670; gene.
DR neXtProt; NX_Q92782; -.
DR OpenTargets; ENSG00000011332; -.
DR PharmGKB; PA134879894; -.
DR VEuPathDB; HostDB:ENSG00000011332; -.
DR GeneTree; ENSGT00940000160692; -.
DR InParanoid; Q92782; -.
DR OMA; WIPEAQR; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; Q92782; -.
DR PathwayCommons; Q92782; -.
DR SignaLink; Q92782; -.
DR BioGRID-ORCS; 8193; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; DPF1; human.
DR GenomeRNAi; 8193; -.
DR Pharos; Q92782; Tbio.
DR PRO; PR:Q92782; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q92782; protein.
DR Bgee; ENSG00000011332; Expressed in cortical plate and 160 other tissues.
DR ExpressionAtlas; Q92782; baseline and differential.
DR Genevisible; Q92782; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038046; DPF1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615:SF12; PTHR10615:SF12; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..387
FT /note="Zinc finger protein neuro-d4"
FT /id="PRO_0000168145"
FT ZN_FING 195..218
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..328
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 325..375
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /id="VSP_061234"
FT VAR_SEQ 199..243
FT /note="ICGKRYKNRPGLSYHYTHTHLAEEEGEENAERHALPFHRKNNHKQ -> K
FT (in isoform 1)"
FT /id="VSP_061235"
FT VAR_SEQ 337
FT /note="D -> DGASWAGLTPQ (in isoform 1)"
FT /id="VSP_061236"
FT CONFLICT 7
FT /note="G -> S (in Ref. 1; AAC50685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44128 MW; D8D63199D4915DEE CRC64;
MATVIPGPLS LGEDFYREAI EHCRSYNARL CAERSLRLPF LDSQTGVAQN NCYIWMEKTH
RGPGLAPGQI YTYPARCWRK KRRLNILEDP RLRPCEYKID CEAPLKKEGG LPEGPVLEAL
LCAETGEKKI ELKEEETIMD CQKQQLLEFP HDLEVEDLED DIPRRKNRAK GKAYGIGGLR
KRQDTASLED RDKPYVCDIC GKRYKNRPGL SYHYTHTHLA EEEGEENAER HALPFHRKNN
HKQFYKELAW VPEAQRKHTA KKAPDGTVIP NGYCDFCLGG SKKTGCPEDL ISCADCGRSG
HPSCLQFTVN MTAAVRTYRW QCIECKSCSL CGTSENDDQL LFCDDCDRGY HMYCLSPPMA
EPPEGSWSCH LCLRHLKEKA SAYITLT
