GDAP2_HUMAN
ID GDAP2_HUMAN Reviewed; 497 AA.
AC Q9NXN4; Q96DZ0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ganglioside-induced differentiation-associated protein 2;
GN Name=GDAP2;
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] (ISOFORM 1).
RC TISSUE=Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP INVOLVEMENT IN SCAR27, AND VARIANT SCAR27 316-GLN--LEU-497 DEL.
RX PubMed=30084953; DOI=10.1093/brain/awy198;
RA Eidhof I., Baets J., Kamsteeg E.J., Deconinck T., van Ninhuijs L.,
RA Martin J.J., Schuele R., Zuechner S., De Jonghe P., Schenck A.,
RA van de Warrenburg B.P.;
RT "GDAP2 mutations implicate susceptibility to cellular stress in a new form
RT of cerebellar ataxia.";
RL Brain 141:2592-2604(2018).
CC -!- INTERACTION:
CC Q9NXN4; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-10316460, EBI-742887;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXN4-2; Sequence=VSP_033186;
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 27 (SCAR27)
CC [MIM:618369]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAR27 is a progressive disease
CC characterized by gait difficulties, eye movement abnormalities,
CC dysarthria, and difficulty writing. Some patients may lose independent
CC ambulation. Additional features include spasticity of the lower limbs
CC and cognitive impairment. {ECO:0000269|PubMed:30084953}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GDAP2 family. {ECO:0000305}.
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DR EMBL; AK000149; BAA90976.1; -; mRNA.
DR EMBL; AL122007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56682.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56683.1; -; Genomic_DNA.
DR EMBL; BC013132; AAH13132.1; -; mRNA.
DR CCDS; CCDS44201.1; -. [Q9NXN4-2]
DR CCDS; CCDS897.1; -. [Q9NXN4-1]
DR RefSeq; NP_001129061.1; NM_001135589.2. [Q9NXN4-2]
DR RefSeq; NP_060156.1; NM_017686.3. [Q9NXN4-1]
DR PDB; 4UML; X-ray; 1.90 A; A=1-228.
DR PDBsum; 4UML; -.
DR AlphaFoldDB; Q9NXN4; -.
DR SMR; Q9NXN4; -.
DR BioGRID; 120187; 11.
DR IntAct; Q9NXN4; 5.
DR MINT; Q9NXN4; -.
DR STRING; 9606.ENSP00000358451; -.
DR iPTMnet; Q9NXN4; -.
DR PhosphoSitePlus; Q9NXN4; -.
DR BioMuta; GDAP2; -.
DR DMDM; 74753050; -.
DR EPD; Q9NXN4; -.
DR jPOST; Q9NXN4; -.
DR MassIVE; Q9NXN4; -.
DR MaxQB; Q9NXN4; -.
DR PaxDb; Q9NXN4; -.
DR PeptideAtlas; Q9NXN4; -.
DR PRIDE; Q9NXN4; -.
DR ProteomicsDB; 83115; -. [Q9NXN4-1]
DR ProteomicsDB; 83116; -. [Q9NXN4-2]
DR Antibodypedia; 46950; 120 antibodies from 20 providers.
DR DNASU; 54834; -.
DR Ensembl; ENST00000369442.3; ENSP00000358450.3; ENSG00000196505.11. [Q9NXN4-2]
DR Ensembl; ENST00000369443.10; ENSP00000358451.4; ENSG00000196505.11. [Q9NXN4-1]
DR GeneID; 54834; -.
DR KEGG; hsa:54834; -.
DR MANE-Select; ENST00000369443.10; ENSP00000358451.4; NM_017686.4; NP_060156.1.
DR UCSC; uc001ehf.4; human. [Q9NXN4-1]
DR CTD; 54834; -.
DR DisGeNET; 54834; -.
DR GeneCards; GDAP2; -.
DR HGNC; HGNC:18010; GDAP2.
DR HPA; ENSG00000196505; Low tissue specificity.
DR MalaCards; GDAP2; -.
DR MIM; 618128; gene.
DR MIM; 618369; phenotype.
DR neXtProt; NX_Q9NXN4; -.
DR OpenTargets; ENSG00000196505; -.
DR PharmGKB; PA28628; -.
DR VEuPathDB; HostDB:ENSG00000196505; -.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000156336; -.
DR HOGENOM; CLU_026877_0_0_1; -.
DR InParanoid; Q9NXN4; -.
DR OMA; LYFPRDR; -.
DR OrthoDB; 937161at2759; -.
DR PhylomeDB; Q9NXN4; -.
DR TreeFam; TF324164; -.
DR PathwayCommons; Q9NXN4; -.
DR SignaLink; Q9NXN4; -.
DR BioGRID-ORCS; 54834; 15 hits in 1077 CRISPR screens.
DR ChiTaRS; GDAP2; human.
DR GenomeRNAi; 54834; -.
DR Pharos; Q9NXN4; Tbio.
DR PRO; PR:Q9NXN4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NXN4; protein.
DR Bgee; ENSG00000196505; Expressed in caput epididymis and 155 other tissues.
DR Genevisible; Q9NXN4; HS.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR CDD; cd02905; Macro_GDAP2-like; 1.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035793; Macro_GDAP2.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Spinocerebellar ataxia.
FT CHAIN 1..497
FT /note="Ganglioside-induced differentiation-associated
FT protein 2"
FT /id="PRO_0000331394"
FT DOMAIN 43..223
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 333..481
FT /note="CRAL-TRIO"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 483..497
FT /note="ENGPYYTSYPPSPDL -> VRSTRSSPSPGMVY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033186"
FT VARIANT 95
FT /note="P -> R (in dbSNP:rs12752437)"
FT /id="VAR_042843"
FT VARIANT 106
FT /note="G -> S (in dbSNP:rs12753610)"
FT /id="VAR_042844"
FT VARIANT 312
FT /note="Q -> P (in dbSNP:rs12145577)"
FT /id="VAR_042845"
FT VARIANT 316..497
FT /note="Missing (in SCAR27)"
FT /evidence="ECO:0000269|PubMed:30084953"
FT /id="VAR_082087"
FT VARIANT 489
FT /note="T -> A (in dbSNP:rs34924570)"
FT /id="VAR_042846"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4UML"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 178..196
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4UML"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4UML"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:4UML"
SQ SEQUENCE 497 AA; 56225 MW; 96D8EF2AC79D5AEF CRC64;
MDPLGAPSQF VDVDTLPSWG DSCQDELNSS DTTAEIFQED TVRSPFLYNK DVNGKVVLWK
GDVALLNCTA IVNTSNESLT DKNPVSESIF MLAGPDLKED LQKLKGCRTG EAKLTKGFNL
AARFIIHTVG PKYKSRYRTA AESSLYSCYR NVLQLAKEQS MSSVGFCVIN SAKRGYPLED
ATHIALRTVR RFLEIHGETI EKVVFAVSDL EEGTYQKLLP LYFPRSLKEE NRSLPYLPAD
IGNAEGEPVV PERQIRISEK PGAPEDNQEE EDEGLGVDLS FIGSHAFARM EGDIDKQRKL
ILQGQLSEAA LQKQHQRNYN RWLCQARSED LSDIASLKAL YQTGVDNCGR TVMVVVGRNI
PVTLIDMDKA LLYFIHVMDH IAVKEYVLVY FHTLTSEYNH LDSDFLKKLY DVVDVKYKRN
LKAVYFVHPT FRSKVSTWFF TTFSVSGLKD KIHHVDSLHQ LFSAISPEQI DFPPFVLEYD
ARENGPYYTS YPPSPDL
