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   17-JUN-2020, entry version 125.
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).
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   -!- 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   SMR; Q8NA31; -.
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; 43 antibodies.
DR   Ensembl; ENST00000313294; ENSP00000464579; ENSG00000249961. [Q8NA31-3]
DR   Ensembl; ENST00000433154; ENSP00000463762; ENSG00000249961. [Q8NA31-1]
DR   Ensembl; ENST00000558713; ENSP00000462883; ENSG00000249961. [Q8NA31-1]
DR   GeneID; 283847; -.
DR   KEGG; hsa:283847; -.
DR   UCSC; uc002eqc.2; human. [Q8NA31-1]
DR   CTD; 283847; -.
DR   EuPathDB; HostDB:ENSG00000249961.9; -.
DR   GeneCards; TERB1; -.
DR   HGNC; HGNC:26675; TERB1.
DR   HPA; ENSG00000249961; Tissue enriched (testis).
DR   MIM; 617332; gene.
DR   neXtProt; NX_Q8NA31; -.
DR   OpenTargets; ENSG00000249961; -.
DR   eggNOG; ENOG410IFKY; Eukaryota.
DR   eggNOG; ENOG4111AM1; LUCA.
DR   GeneTree; ENSGT00390000005075; -.
DR   HOGENOM; CLU_022991_1_0_1; -.
DR   InParanoid; Q8NA31; -.
DR   OMA; MDNAFSQ; -.
DR   OrthoDB; 196162at2759; -.
DR   PhylomeDB; Q8NA31; -.
DR   TreeFam; TF335845; -.
DR   BioGRID-ORCS; 283847; 0 hits in 64 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 testis and 60 other tissues.
DR   ExpressionAtlas; Q8NA31; baseline and differential.
DR   Genevisible; Q8NA31; HS.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:0000784; C:nuclear 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:0003677; F:DNA binding; IEA:InterPro.
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   GO; GO:0007129; P:synapsis; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR009057; Homeobox-like_sf.
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; Meiosis;
KW   Membrane; Nucleus; Phosphoprotein; 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          523..662
FT                   /note="Interaction with TERF1"
FT                   /evidence="ECO:0000250"
FT   COILED          398..446
FT                   /evidence="ECO:0000255"
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   TURN            593..595
FT                   /evidence="ECO:0000244|PDB:6J07"
FT   TURN            604..606
FT                   /evidence="ECO:0000244|PDB:6J07"
FT   HELIX           607..613
FT                   /evidence="ECO:0000244|PDB:6J07"
FT   HELIX           619..641
FT                   /evidence="ECO:0000244|PDB:6J07"
FT   STRAND          642..644
FT                   /evidence="ECO:0000244|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
//