TRI36_HUMAN
ID TRI36_HUMAN Reviewed; 728 AA.
AC Q9NQ86; A1L3Z1; A6NDD0; B7Z3V4; B7ZAV7; E9PFI8; Q0P5Z9;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM36;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q80WG7};
DE AltName: Full=RING finger protein 98;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM36 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 36;
DE AltName: Full=Zinc-binding protein Rbcc728;
GN Name=TRIM36; Synonyms=RBCC728, RNF98;
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), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS ARG-428; SER-456 AND ASN-678.
RC TISSUE=Brain;
RX PubMed=15145053; DOI=10.1016/j.gene.2004.02.045;
RA Balint I., Muller A., Nagy A., Kovacs G.;
RT "Cloning and characterisation of the RBCC728/TRIM36 zinc-binding protein
RT from the tumor suppressor gene region at chromosome 5q22.3.";
RL Gene 332:45-50(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ASN-678.
RC TISSUE=Testis, and Thalamus;
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 MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-678.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ARG-428 AND ASN-678.
RC TISSUE=Brain;
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 [7]
RP INVOLVEMENT IN ANPH1, VARIANT ANPH1 ASN-518, CHARACTERIZATION OF VARIANT
RP ANPH1 ASN-518, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=28087737; DOI=10.1093/hmg/ddx020;
RA Singh N., Kumble Bhat V., Tiwari A., Kodaganur S.G., Tontanahal S.J.,
RA Sarda A., Malini K.V., Kumar A.;
RT "A homozygous mutation in TRIM36 causes autosomal recessive anencephaly in
RT an Indian family.";
RL Hum. Mol. Genet. 26:1104-1114(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. Involved in
CC chromosome segregation and cell cycle regulation (PubMed:28087737). May
CC play a role in the acrosome reaction and fertilization.
CC {ECO:0000250|UniProtKB:Q80WG7, ECO:0000269|PubMed:28087737}.
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; Evidence={ECO:0000250|UniProtKB:Q80WG7};
CC -!- SUBUNIT: Interacts with CENPH. {ECO:0000250|UniProtKB:Q80WG7}.
CC -!- INTERACTION:
CC Q9NQ86; Q9Y297: BTRC; NbExp=3; IntAct=EBI-2341518, EBI-307461;
CC Q9NQ86; Q14240: EIF4A2; NbExp=3; IntAct=EBI-2341518, EBI-73473;
CC Q9NQ86; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-2341518, EBI-10232522;
CC Q9NQ86; O76003: GLRX3; NbExp=6; IntAct=EBI-2341518, EBI-374781;
CC Q9NQ86; Q14451: GRB7; NbExp=3; IntAct=EBI-2341518, EBI-970191;
CC Q9NQ86; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-2341518, EBI-765817;
CC Q9NQ86; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-2341518, EBI-2682299;
CC Q9NQ86; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2341518, EBI-740727;
CC Q9NQ86; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-2341518, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28087737}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q80WG7}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q80WG7}. Note=Found in the acrosomal region of
CC elongated spermatids and mature sperm. {ECO:0000250|UniProtKB:Q80WG7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NQ86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ86-2; Sequence=VSP_043511, VSP_043512;
CC Name=3;
CC IsoId=Q9NQ86-3; Sequence=VSP_045791, VSP_045792;
CC Name=4;
CC IsoId=Q9NQ86-4; Sequence=VSP_053818;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, prostate and brain
CC (PubMed:15145053). Weakly expressed in kidney, lung and heart
CC (PubMed:15145053). Expressed in fetal tissues (PubMed:28087737).
CC {ECO:0000269|PubMed:15145053, ECO:0000269|PubMed:28087737}.
CC -!- DISEASE: Anencephaly 1 (ANPH1) [MIM:206500]: An extreme form of neural
CC tube defect resulting in the absence of brain tissues, and death in
CC utero or perinatally. Infants are born with intact spinal cords,
CC cerebellums, and brainstems, but lack formation of neural structures
CC above this level. The skull is only partially formed. ANPH1 inheritance
CC is autosomal recessive. {ECO:0000269|PubMed:28087737}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AJ272269; CAB94831.1; -; mRNA.
DR EMBL; BX460627; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK316422; BAH14793.1; -; mRNA.
DR EMBL; AK296389; BAH12340.1; -; mRNA.
DR EMBL; AC008494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC094104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48972.1; -; Genomic_DNA.
DR EMBL; BC045164; AAH45164.1; -; mRNA.
DR EMBL; BC046096; AAH46096.1; -; mRNA.
DR EMBL; BC130334; AAI30335.1; -; mRNA.
DR CCDS; CCDS34211.1; -. [Q9NQ86-2]
DR CCDS; CCDS34212.1; -. [Q9NQ86-3]
DR CCDS; CCDS4115.1; -. [Q9NQ86-1]
DR CCDS; CCDS75287.1; -. [Q9NQ86-4]
DR RefSeq; NP_001017397.1; NM_001017397.1. [Q9NQ86-2]
DR RefSeq; NP_001017398.1; NM_001017398.1. [Q9NQ86-3]
DR RefSeq; NP_001287681.1; NM_001300752.1.
DR RefSeq; NP_001287688.1; NM_001300759.1. [Q9NQ86-4]
DR RefSeq; NP_061170.2; NM_018700.3. [Q9NQ86-1]
DR AlphaFoldDB; Q9NQ86; -.
DR BioGRID; 120695; 135.
DR IntAct; Q9NQ86; 15.
DR MINT; Q9NQ86; -.
DR STRING; 9606.ENSP00000282369; -.
DR iPTMnet; Q9NQ86; -.
DR PhosphoSitePlus; Q9NQ86; -.
DR BioMuta; TRIM36; -.
DR DMDM; 313104034; -.
DR EPD; Q9NQ86; -.
DR jPOST; Q9NQ86; -.
DR MassIVE; Q9NQ86; -.
DR MaxQB; Q9NQ86; -.
DR PaxDb; Q9NQ86; -.
DR PeptideAtlas; Q9NQ86; -.
DR PRIDE; Q9NQ86; -.
DR ProteomicsDB; 20113; -.
DR ProteomicsDB; 82103; -. [Q9NQ86-1]
DR Antibodypedia; 25412; 238 antibodies from 28 providers.
DR DNASU; 55521; -.
DR Ensembl; ENST00000282369.7; ENSP00000282369.3; ENSG00000152503.10. [Q9NQ86-1]
DR Ensembl; ENST00000379617.2; ENSP00000368937.2; ENSG00000152503.10. [Q9NQ86-3]
DR Ensembl; ENST00000379618.6; ENSP00000368938.2; ENSG00000152503.10. [Q9NQ86-2]
DR Ensembl; ENST00000513154.6; ENSP00000423934.1; ENSG00000152503.10. [Q9NQ86-4]
DR GeneID; 55521; -.
DR KEGG; hsa:55521; -.
DR MANE-Select; ENST00000513154.6; ENSP00000423934.1; NM_001300759.2; NP_001287688.1. [Q9NQ86-4]
DR UCSC; uc003kqs.4; human. [Q9NQ86-1]
DR CTD; 55521; -.
DR DisGeNET; 55521; -.
DR GeneCards; TRIM36; -.
DR HGNC; HGNC:16280; TRIM36.
DR HPA; ENSG00000152503; Group enriched (retina, testis).
DR MalaCards; TRIM36; -.
DR MIM; 206500; phenotype.
DR MIM; 609317; gene.
DR neXtProt; NX_Q9NQ86; -.
DR OpenTargets; ENSG00000152503; -.
DR PharmGKB; PA38111; -.
DR VEuPathDB; HostDB:ENSG00000152503; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158373; -.
DR HOGENOM; CLU_013137_19_3_1; -.
DR InParanoid; Q9NQ86; -.
DR OMA; MYCELCK; -.
DR OrthoDB; 180330at2759; -.
DR PhylomeDB; Q9NQ86; -.
DR TreeFam; TF315216; -.
DR PathwayCommons; Q9NQ86; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NQ86; -.
DR BioGRID-ORCS; 55521; 7 hits in 1104 CRISPR screens.
DR ChiTaRS; TRIM36; human.
DR GenomeRNAi; 55521; -.
DR Pharos; Q9NQ86; Tbio.
DR PRO; PR:Q9NQ86; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NQ86; protein.
DR Bgee; ENSG00000152503; Expressed in sperm and 151 other tissues.
DR ExpressionAtlas; Q9NQ86; baseline and differential.
DR Genevisible; Q9NQ86; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007340; P:acrosome reaction; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12894; SPRY_PRY_TRIM36; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR035727; SPRY/PRY_TRIM36.
DR InterPro; IPR027726; Trim36.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24099:SF18; PTHR24099:SF18; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Disease variant; Metal-binding; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="E3 ubiquitin-protein ligase TRIM36"
FT /id="PRO_0000056252"
FT DOMAIN 356..413
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 419..510
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 508..720
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 33..84
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 154..192
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 207..249
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 271..345
FT /evidence="ECO:0000255"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..21
FT /note="MSESGEMSEFGYIMELIAKGK -> MEGDGSDSP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053818"
FT VAR_SEQ 22..61
FT /note="VTIKNIERELICPACKELFTHPLILPCQHSICHKCVKELL -> ASAMGLQQ
FT THEHSRLTSKGGEARCPFEISEVGKQSLPRRT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045791"
FT VAR_SEQ 22..60
FT /note="VTIKNIERELICPACKELFTHPLILPCQHSICHKCVKEL -> MPDWRRGYR
FT CRQGCGKTTELATATDFSQTGNKSGKHFKT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043511"
FT VAR_SEQ 61..728
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043512"
FT VAR_SEQ 62..728
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045792"
FT VARIANT 428
FT /note="K -> R (in dbSNP:rs79290430)"
FT /evidence="ECO:0000269|PubMed:15145053,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023197"
FT VARIANT 456
FT /note="N -> S (in dbSNP:rs17137481)"
FT /evidence="ECO:0000269|PubMed:15145053"
FT /id="VAR_023198"
FT VARIANT 518
FT /note="D -> N (in ANPH1; decreases protein stability; leads
FT to microtubules disruption; exhibits multipolar spindles;
FT exhibits abnormal cytokinesis)"
FT /evidence="ECO:0000269|PubMed:28087737"
FT /id="VAR_079581"
FT VARIANT 678
FT /note="D -> N (in dbSNP:rs2974617)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15145053, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_020490"
FT VARIANT 725
FT /note="Q -> E (in dbSNP:rs3749745)"
FT /id="VAR_057221"
FT CONFLICT 313
FT /note="R -> G (in Ref. 2; BAH12340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 83013 MW; 1D1B4F98325BD73C CRC64;
MSESGEMSEF GYIMELIAKG KVTIKNIERE LICPACKELF THPLILPCQH SICHKCVKEL
LLTLDDSFND VGSDNSNQSS PRLRLPSPSM DKIDRINRPG WKRNSLTPRT TVFPCPGCEH
DVDLGERGIN GLFRNFTLET IVERYRQAAR AATAIMCDLC KPPPQESTKS CMDCSASYCN
ECFKIHHPWG TIKAQHEYVG PTTNFRPKIL MCPEHETERI NMYCELCRRP VCHLCKLGGN
HANHRVTTMS SAYKTLKEKL SKDIDYLIGK ESQVKSQISE LNLLMKETEC NGERAKEEAI
THFEKLFEVL EERKSSVLKA IDSSKKLRLD KFQTQMEEYQ GLLENNGLVG YAQEVLKETD
QSCFVQTAKQ LHLRIQKATE SLKSFRPAAQ TSFEDYVVNT SKQTELLGEL SFFSSGIDVP
EINEEQSKVY NNALINWHHP EKDKADSYVL EYRKINRDDE MSWNEIEVCG TSKIIQDLEN
SSTYAFRVRA YKGSICSPCS RELILHTPPA PVFSFLFDEK CGYNNEHLLL NLKRDRVESR
AGFNLLLAAE RIQVGYYTSL DYIIGDTGIT KGKHFWAFRV EPYSYLVKVG VASSDKLQEW
LRSPRDAVSP RYEQDSGHDS GSEDACFDSS QPFTLVTIGM QKFFIPKSPT SSNEPENRVL
PMPTSIGIFL DCDKGKVDFY DMDQMKCLYE RQVDCSHTLY PAFALMGSGG IQLEEPITAK
YLEYQEDM
