TERB1_HUMAN
ID TERB1_HUMAN Reviewed; 727 AA.
AC Q8NA31; A0AUW1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Telomere repeats-binding bouquet formation protein 1 {ECO:0000250|UniProtKB:Q8C0V1};
DE AltName: Full=Coiled-coil domain-containing protein 79 {ECO:0000312|HGNC:HGNC:26675};
GN Name=TERB1 {ECO:0000312|HGNC:HGNC:26675};
GN Synonyms=CCDC79 {ECO:0000312|HGNC:HGNC:26675};
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 3).
RC TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 [4]
RP VARIANTS SPGF60 GLY-326 AND 568-SER--SER-727 DEL, AND INVOLVEMENT IN
RP SPGF60.
RX PubMed=33211200; DOI=10.1007/s00439-020-02236-1;
RG GEMINI Consortium;
RA Salas-Huetos A., Tuettelmann F., Wyrwoll M.J., Kliesch S., Lopes A.M.,
RA Goncalves J., Boyden S.E., Woeste M., Hotaling J.M., Nagirnaja L.,
RA Conrad D.F., Carrell D.T., Aston K.I.;
RT "Disruption of human meiotic telomere complex genes TERB1, TERB2 and MAJIN
RT in men with non-obstructive azoospermia.";
RL Hum. Genet. 140:217-227(2021).
RN [5]
RP ERRATUM OF PUBMED:33211200.
RX PubMed=33377991; DOI=10.1007/s00439-020-02244-1;
RG GEMINI Consortium;
RA Salas-Huetos A., Tuettelmann F., Wyrwoll M.J., Kliesch S., Lopes A.M.,
RA Goncalves J., Boyden S.E., Woeste M., Hotaling J.M., Nagirnaja L.,
RA Conrad D.F., Carrell D.T., Aston K.I.;
RL Hum. Genet. 140:229-229(2021).
CC -!- FUNCTION: Meiosis-specific telomere-associated protein involved in
CC meiotic telomere attachment to the nucleus inner membrane, a crucial
CC step for homologous pairing and synapsis. Component of the MAJIN-TERB1-
CC TERB2 complex, which promotes telomere cap exchange by mediating
CC attachment of telomeric DNA to the inner nuclear membrane and
CC replacement of the protective cap of telomeric chromosomes: in early
CC meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA
CC and the shelterin/telosome complex. During prophase, the complex
CC matures and promotes release of the shelterin/telosome complex from
CC telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably
CC mediates association with the shelterin/telosome complex via
CC interaction with TERF1, promoting priming telomeric DNA attachment'.
CC Promotes telomere association with the nuclear envelope and deposition
CC of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to
CC develop structural rigidity. {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN,
CC TERB1 and TERB2. Interacts with TERF1, STAG3 and SUN1. Interacts (via
CC Myb-like domain) with the cohesin complex; probably mediated via
CC interaction with STAG3. {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- INTERACTION:
CC Q8NA31; P54274: TERF1; NbExp=4; IntAct=EBI-21942840, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during
CC meiotic prophase. In leptotene spermatocytes, localizes to telomeres
CC that localize to the nucleus inner membrane.
CC {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NA31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NA31-2; Sequence=VSP_031614, VSP_031615;
CC Name=3;
CC IsoId=Q8NA31-3; Sequence=VSP_031613, VSP_031614, VSP_031615;
CC -!- PTM: Phosphorylated by CDK. Phosphorylation by CDK takes place in late
CC prophase when the cap exchange is prominent. is important for the
CC stabilization of telomere attachment but dispenable for the cap
CC exchange. {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- DISEASE: Spermatogenic failure 60 (SPGF60) [MIM:619646]: An autosomal
CC recessive male infertility disorder characterized by non-obstructive
CC azoospermia, due to sperm maturation arrest before the pachytene stage.
CC {ECO:0000269|PubMed:33211200}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TERB1 family. {ECO:0000305}.
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DR EMBL; AK093213; BAC04098.1; -; mRNA.
DR EMBL; AC044802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126109; AAI26110.1; -; mRNA.
DR RefSeq; NP_001129977.1; NM_001136505.1. [Q8NA31-1]
DR RefSeq; XP_011521306.1; XM_011523004.2.
DR RefSeq; XP_011521307.1; XM_011523005.2. [Q8NA31-1]
DR RefSeq; XP_011521308.1; XM_011523006.2.
DR RefSeq; XP_011521309.1; XM_011523007.2.
DR RefSeq; XP_011521310.1; XM_011523008.2. [Q8NA31-1]
DR RefSeq; XP_011521311.1; XM_011523009.2. [Q8NA31-1]
DR RefSeq; XP_011521320.1; XM_011523018.1.
DR PDB; 5WIR; X-ray; 2.10 A; C/D=642-656.
DR PDB; 5XUP; X-ray; 2.10 A; C/D=644-655.
DR PDB; 6J07; X-ray; 3.30 A; B=590-649.
DR PDBsum; 5WIR; -.
DR PDBsum; 5XUP; -.
DR PDBsum; 6J07; -.
DR AlphaFoldDB; Q8NA31; -.
DR SMR; Q8NA31; -.
DR BioGRID; 129681; 1.
DR IntAct; Q8NA31; 1.
DR STRING; 9606.ENSP00000463762; -.
DR iPTMnet; Q8NA31; -.
DR PhosphoSitePlus; Q8NA31; -.
DR BioMuta; TERB1; -.
DR DMDM; 322510134; -.
DR MassIVE; Q8NA31; -.
DR PaxDb; Q8NA31; -.
DR PeptideAtlas; Q8NA31; -.
DR PRIDE; Q8NA31; -.
DR ProteomicsDB; 72629; -. [Q8NA31-1]
DR ProteomicsDB; 72630; -. [Q8NA31-2]
DR ProteomicsDB; 72631; -. [Q8NA31-3]
DR Antibodypedia; 72088; 47 antibodies from 9 providers.
DR DNASU; 283847; -.
DR Ensembl; ENST00000313294.7; ENSP00000464579.1; ENSG00000249961.10. [Q8NA31-3]
DR Ensembl; ENST00000433154.6; ENSP00000463762.1; ENSG00000249961.10. [Q8NA31-1]
DR Ensembl; ENST00000558713.6; ENSP00000462883.1; ENSG00000249961.10. [Q8NA31-1]
DR GeneID; 283847; -.
DR KEGG; hsa:283847; -.
DR MANE-Select; ENST00000433154.6; ENSP00000463762.1; NM_001136505.2; NP_001129977.1.
DR UCSC; uc002eqc.2; human. [Q8NA31-1]
DR CTD; 283847; -.
DR GeneCards; TERB1; -.
DR HGNC; HGNC:26675; TERB1.
DR HPA; ENSG00000249961; Tissue enriched (testis).
DR MIM; 617332; gene.
DR MIM; 619646; phenotype.
DR neXtProt; NX_Q8NA31; -.
DR OpenTargets; ENSG00000249961; -.
DR VEuPathDB; HostDB:ENSG00000249961; -.
DR eggNOG; ENOG502QQER; Eukaryota.
DR GeneTree; ENSGT00390000005075; -.
DR HOGENOM; CLU_022991_1_0_1; -.
DR InParanoid; Q8NA31; -.
DR OMA; RENCQDN; -.
DR OrthoDB; 196162at2759; -.
DR PhylomeDB; Q8NA31; -.
DR TreeFam; TF335845; -.
DR PathwayCommons; Q8NA31; -.
DR SignaLink; Q8NA31; -.
DR SIGNOR; Q8NA31; -.
DR BioGRID-ORCS; 283847; 4 hits in 275 CRISPR screens.
DR ChiTaRS; TERB1; human.
DR GenomeRNAi; 283847; -.
DR Pharos; Q8NA31; Tdark.
DR PRO; PR:Q8NA31; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NA31; protein.
DR Bgee; ENSG00000249961; Expressed in right testis and 98 other tissues.
DR ExpressionAtlas; Q8NA31; baseline and differential.
DR Genevisible; Q8NA31; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0070187; C:shelterin complex; IEA:Ensembl.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR042359; TERB1.
DR PANTHER; PTHR14014; PTHR14014; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Coiled coil;
KW Disease variant; Meiosis; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Telomere.
FT CHAIN 1..727
FT /note="Telomere repeats-binding bouquet formation protein
FT 1"
FT /id="PRO_0000320156"
FT REPEAT 101..144
FT /note="ARM 1"
FT REPEAT 339..382
FT /note="ARM 2"
FT DOMAIN 666..719
FT /note="Myb-like"
FT REGION 457..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..662
FT /note="Interaction with TERF1"
FT /evidence="ECO:0000250"
FT COILED 398..446
FT /evidence="ECO:0000255"
FT COMPBIAS 457..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0V1"
FT VAR_SEQ 329..371
FT /note="EENQYDLFKNNGLPLMIQALTESQNEELNKAATFVLHNCKKIT -> A (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031613"
FT VAR_SEQ 540..550
FT /note="SDHVFKHPVHI -> RSIYIMFRYNK (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031614"
FT VAR_SEQ 551..727
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031615"
FT VARIANT 326
FT /note="E -> G (in SPGF60; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33211200"
FT /id="VAR_086535"
FT VARIANT 568..727
FT /note="Missing (in SPGF60)"
FT /evidence="ECO:0000269|PubMed:33211200"
FT /id="VAR_086536"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:6J07"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 607..613
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 619..641
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6J07"
SQ SEQUENCE 727 AA; 83064 MW; 266C9F347B9D4966 CRC64;
MESEDTKKTQ EMKTDLNLLL ECLKYQMDNA FSQKEALVTI HSICQQNSNA SVYFREIGGL
MFVKNLAKSS EHSMVKEAAL YTLGAIAEKN VYCQQTLCTS ELFEDLTWFL SNDSNINLKR
MSVYVILVLV SNNRTGQTLV RETGCITVLS RLFRTVISKH ELDLSDKNVF QSYQLWSSVC
STLCVCVNNP QNDENQMFCC SLFPHANEWL KNCTTPEIIR PICSFIGLTL ANNTYVQKYF
VSVGGLDVLS QVLMQLESDS HETLSSAKLA VVVTKTVDAC IADNPTFGIV LSKYHIVSKL
LALLLHESLD SGEKFSIMLT LGHCTEDCEE NQYDLFKNNG LPLMIQALTE SQNEELNKAA
TFVLHNCKKI TEKLSLSLGE YPFDENETQQ LKDISVKENN LEEHWRKAKE ILHRIEQLER
EGNEEEIQRE NYQDNISSMN ISIQNTWKHL HADRIGRGSK AEDEDKSHSR QLQSYKSHGV
MSKACTNDDQ MKTPLKSANP VHACYRESEQ NKTLYKAKSS CNQNLHEETT FEKNFVSQSS
DHVFKHPVHI AKNIKQQLPV TDPFTLCSDI INKEVVSFLA TPSCSEMLTY RCSGCIAVEK
SLNSRNFSKL LHSCPYQCDR HKVIVEAEDR YKSELRKSLI CNKKILLTPR RRQRLSNEST
TPGGIKKRRI RKNFTEEEVN YLFNGVKKMG NHWNSILWSF PFQQGRKAVD LAHKYHKLTK
HPTCAAS
