ADNP2_HUMAN
ID ADNP2_HUMAN Reviewed; 1131 AA.
AC Q6IQ32; A8K951; O94943; Q9H9P3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Activity-dependent neuroprotector homeobox protein 2;
DE Short=ADNP homeobox protein 2;
DE AltName: Full=Zinc finger protein 508;
GN Name=ADNP2; Synonyms=KIAA0863, ZNF508;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma, and Testis;
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 [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].
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1032, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-118; LYS-146; LYS-979; LYS-1018
RP AND LYS-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q6IQ32; P83916: CBX1; NbExp=4; IntAct=EBI-2838654, EBI-78129;
CC Q6IQ32; Q13185: CBX3; NbExp=5; IntAct=EBI-2838654, EBI-78176;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74886.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14180.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB020670; BAA74886.2; ALT_INIT; mRNA.
DR EMBL; AK022688; BAB14180.1; ALT_FRAME; mRNA.
DR EMBL; AK292566; BAF85255.1; -; mRNA.
DR EMBL; CH471117; EAW66646.1; -; Genomic_DNA.
DR EMBL; BC071589; AAH71589.1; -; mRNA.
DR CCDS; CCDS32853.1; -.
DR RefSeq; NP_055728.1; NM_014913.3.
DR RefSeq; XP_005266713.1; XM_005266656.4.
DR AlphaFoldDB; Q6IQ32; -.
DR BioGRID; 116522; 46.
DR IntAct; Q6IQ32; 14.
DR MINT; Q6IQ32; -.
DR STRING; 9606.ENSP00000262198; -.
DR iPTMnet; Q6IQ32; -.
DR PhosphoSitePlus; Q6IQ32; -.
DR BioMuta; ADNP2; -.
DR DMDM; 74757998; -.
DR EPD; Q6IQ32; -.
DR jPOST; Q6IQ32; -.
DR MassIVE; Q6IQ32; -.
DR MaxQB; Q6IQ32; -.
DR PaxDb; Q6IQ32; -.
DR PeptideAtlas; Q6IQ32; -.
DR PRIDE; Q6IQ32; -.
DR ProteomicsDB; 66483; -.
DR Antibodypedia; 1760; 66 antibodies from 17 providers.
DR DNASU; 22850; -.
DR Ensembl; ENST00000262198.9; ENSP00000262198.3; ENSG00000101544.9.
DR GeneID; 22850; -.
DR KEGG; hsa:22850; -.
DR MANE-Select; ENST00000262198.9; ENSP00000262198.3; NM_014913.4; NP_055728.1.
DR UCSC; uc032hie.2; human.
DR CTD; 22850; -.
DR DisGeNET; 22850; -.
DR GeneCards; ADNP2; -.
DR HGNC; HGNC:23803; ADNP2.
DR HPA; ENSG00000101544; Tissue enhanced (bone).
DR MIM; 617422; gene.
DR neXtProt; NX_Q6IQ32; -.
DR OpenTargets; ENSG00000101544; -.
DR PharmGKB; PA162375700; -.
DR VEuPathDB; HostDB:ENSG00000101544; -.
DR eggNOG; ENOG502QU0M; Eukaryota.
DR GeneTree; ENSGT00530000063631; -.
DR HOGENOM; CLU_009119_1_0_1; -.
DR InParanoid; Q6IQ32; -.
DR OMA; NLDQMLH; -.
DR OrthoDB; 135860at2759; -.
DR PhylomeDB; Q6IQ32; -.
DR TreeFam; TF328818; -.
DR PathwayCommons; Q6IQ32; -.
DR SignaLink; Q6IQ32; -.
DR BioGRID-ORCS; 22850; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; ADNP2; human.
DR GenomeRNAi; 22850; -.
DR Pharos; Q6IQ32; Tdark.
DR PRO; PR:Q6IQ32; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q6IQ32; protein.
DR Bgee; ENSG00000101544; Expressed in secondary oocyte and 207 other tissues.
DR ExpressionAtlas; Q6IQ32; baseline and differential.
DR Genevisible; Q6IQ32; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR038861; ADNP/ADNP2.
DR InterPro; IPR045762; ADNP_Znf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15740; PTHR15740; 2.
DR Pfam; PF19627; ADNP_N; 2.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1131
FT /note="Activity-dependent neuroprotector homeobox protein
FT 2"
FT /id="PRO_0000280416"
FT ZN_FING 73..96
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 106..128
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 155..178
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..240
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..716
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 747..768
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 770..793
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 875..898
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 913..937
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 1043..1102
FT /note="Homeobox"
FT REGION 274..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 979
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1018
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1032
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1032
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 757
FT /note="S -> P (in Ref. 3; BAB14180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1131 AA; 122833 MW; 73BCB3F755E6906D CRC64;
MFQIPVENLD NIRKVRKKVK GILVDIGLDS CKELLKDLKG FDPGEKYFHN TSWGDVSLWE
PSGKKVRYRT KPYCCGLCKY STKVLTSFKN HLHRYHEDEI DQELVIPCPN CVFASQPKVV
GRHFRMFHAP VRKVQNYTVN ILGETKSSRS DVISFTCLKC NFSNTLYYSM KKHVLVAHFH
YLINSYFGLR TEEMGEQPKT NDTVSIEKIP PPDKYYCKKC NANASSQDAL MYHILTSDIH
RDLENKLRSV ISEHIKRTGL LKQTHIAPKP AAHLAAPANG SAPSAPAQPP CFHLALPQNS
PSPAAGQPVT VAQGAPGSLT HSPPAAGQSH MTLVSSPLPV GQNSLTLQPP APQPVFLSHG
VPLHQSVNPP VLPLSQPVGP VNKSVGTSVL PINQTVRPGV LPLTQPVGPI NRPVGPGVLP
VSPSVTPGVL QAVSPGVLSV SRAVPSGVLP AGQMTPAGQM TPAGVIPGQT ATSGVLPTGQ
MVQSGVLPVG QTAPSRVLPP GQTAPLRVIS AGQVVPSGLL SPNQTVSSSA VVPVNQGVNS
GVLQLSQPVV SGVLPVGQPV RPGVLQLNQT VGTNILPVNQ PVRPGASQNT TFLTSGSILR
QLIPTGKQVN GIPTYTLAPV SVTLPVPPGG LATVAPPQMP IQLLPSGAAA PMAGSMPGMP
SPPVLVNAAQ SVFVQASSSA ADTNQVLKQA KQWKTCPVCN ELFPSNVYQV HMEVAHKHSE
SKSGEKLEPE KLAACAPFLK WMREKTVRCL SCKCLVSEEE LIHHLLMHGL GCLFCPCTFH
DIKGLSEHSR NRHLGKKKLP MDYSNRGFQL DVDANGNLLF PHLDFITILP KEKLGEREVY
LAILAGIHSK SLVPVYVKVR PQAEGTPGST GKRVSTCPFC FGPFVTTEAY ELHLKERHHI
MPTVHTVLKS PAFKCIHCCG VYTGNMTLAA IAVHLVRCRS APKDSSSDLQ AQPGFIHNSE
LLLVSGEVMH DSSFSVKRKL PDGHLGAEDQ RHGEEQPPIL NADAAPGPEK VTSVVPFKRQ
RNESRTEGPI VKDEALQILA LDPKKYEGRS YEEKKQFLKD YFHKKPYPSK KEIELLSSLF
WVWKIDVASF FGKRRYICMK AIKNHKPSVL LGFDMSELKN VKHRLNFEYE P
