TERB2_HUMAN
ID TERB2_HUMAN Reviewed; 220 AA.
AC Q8NHR7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Telomere repeats-binding bouquet formation protein 2 {ECO:0000250|UniProtKB:Q9D494};
GN Name=TERB2; Synonyms=C15orf43;
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=Testis;
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 [2]
RP INVOLVEMENT IN SPGF59.
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 [3]
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).
RN [4]
RP VARIANTS ARG-103 AND ASN-190.
RX PubMed=26063658; DOI=10.1093/brain/awv155;
RA Verdura E., Herve D., Scharrer E., del Mar Amador M., Guyant-Marechal L.,
RA Philippi A., Corlobe A., Bergametti F., Gazal S., Prieto-Morin C.,
RA Beaufort N., Le Bail B., Viakhireva I., Dichgans M., Chabriat H.,
RA Haffner C., Tournier-Lasserve E.;
RT "Heterozygous HTRA1 mutations are associated with autosomal dominant
RT cerebral small vessel disease.";
RL Brain 138:2347-2358(2015).
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. {ECO:0000250|UniProtKB:Q9D494}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN,
CC TERB1 and TERB2. {ECO:0000250|UniProtKB:Q9D494}.
CC -!- INTERACTION:
CC Q8NHR7; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-23751757, EBI-18015780;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9D494}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q9D494}. Note=Localizes to telomeres throughout
CC meiotic prophase I and disappears in metaphase I. In leptotene
CC spermatocytes, localizes to telomeres that localize to the nucleus
CC inner membrane. {ECO:0000250|UniProtKB:Q9D494}.
CC -!- DISEASE: Spermatogenic failure 59 (SPGF59) [MIM:619645]: An autosomal
CC recessive male infertility disorder characterized by non-obstructive
CC azoospermia, due to sperm maturation arrest.
CC {ECO:0000269|PubMed:33377991}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TERB2 family. {ECO:0000305}.
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DR EMBL; BC029537; AAH29537.1; -; mRNA.
DR CCDS; CCDS10115.1; -.
DR RefSeq; NP_689661.1; NM_152448.2.
DR PDB; 6GNX; X-ray; 2.90 A; B/D=169-220.
DR PDB; 6GNY; X-ray; 1.85 A; B/D=168-207.
DR PDB; 6J07; X-ray; 3.30 A; A=4-110.
DR PDB; 6J08; X-ray; 2.90 A; D/E/F=174-209.
DR PDBsum; 6GNX; -.
DR PDBsum; 6GNY; -.
DR PDBsum; 6J07; -.
DR PDBsum; 6J08; -.
DR AlphaFoldDB; Q8NHR7; -.
DR SMR; Q8NHR7; -.
DR BioGRID; 126925; 2.
DR IntAct; Q8NHR7; 1.
DR STRING; 9606.ENSP00000340644; -.
DR iPTMnet; Q8NHR7; -.
DR PhosphoSitePlus; Q8NHR7; -.
DR BioMuta; TERB2; -.
DR MassIVE; Q8NHR7; -.
DR PaxDb; Q8NHR7; -.
DR PeptideAtlas; Q8NHR7; -.
DR PRIDE; Q8NHR7; -.
DR Antibodypedia; 52480; 6 antibodies from 3 providers.
DR DNASU; 145645; -.
DR Ensembl; ENST00000340827.4; ENSP00000340644.3; ENSG00000167014.11.
DR GeneID; 145645; -.
DR KEGG; hsa:145645; -.
DR MANE-Select; ENST00000340827.4; ENSP00000340644.3; NM_152448.3; NP_689661.1.
DR UCSC; uc001zuk.5; human.
DR CTD; 145645; -.
DR GeneCards; TERB2; -.
DR HGNC; HGNC:28520; TERB2.
DR HPA; ENSG00000167014; Tissue enriched (testis).
DR MIM; 617131; gene.
DR MIM; 619645; phenotype.
DR neXtProt; NX_Q8NHR7; -.
DR OpenTargets; ENSG00000167014; -.
DR PharmGKB; PA143485393; -.
DR VEuPathDB; HostDB:ENSG00000167014; -.
DR eggNOG; ENOG502S1BT; Eukaryota.
DR GeneTree; ENSGT00390000012336; -.
DR HOGENOM; CLU_109637_0_0_1; -.
DR InParanoid; Q8NHR7; -.
DR OMA; SPEKHFI; -.
DR OrthoDB; 1206947at2759; -.
DR PhylomeDB; Q8NHR7; -.
DR TreeFam; TF336969; -.
DR PathwayCommons; Q8NHR7; -.
DR SignaLink; Q8NHR7; -.
DR SIGNOR; Q8NHR7; -.
DR BioGRID-ORCS; 145645; 8 hits in 1038 CRISPR screens.
DR ChiTaRS; TERB2; human.
DR GenomeRNAi; 145645; -.
DR Pharos; Q8NHR7; Tdark.
DR PRO; PR:Q8NHR7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8NHR7; protein.
DR Bgee; ENSG00000167014; Expressed in right testis and 27 other tissues.
DR ExpressionAtlas; Q8NHR7; baseline and differential.
DR Genevisible; Q8NHR7; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
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 InterPro; IPR028065; TERB2.
DR PANTHER; PTHR35345; PTHR35345; 1.
DR Pfam; PF15101; TERB2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Membrane; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..220
FT /note="Telomere repeats-binding bouquet formation protein
FT 2"
FT /id="PRO_0000263717"
FT VARIANT 31
FT /note="P -> R (in dbSNP:rs11638723)"
FT /id="VAR_029614"
FT VARIANT 103
FT /note="S -> R"
FT /evidence="ECO:0000269|PubMed:26063658"
FT /id="VAR_076385"
FT VARIANT 190
FT /note="H -> N (in dbSNP:rs1248475666)"
FT /evidence="ECO:0000269|PubMed:26063658"
FT /id="VAR_076386"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:6J07"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:6J07"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6J07"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6GNY"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6GNX"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6GNY"
SQ SEQUENCE 220 AA; 25316 MW; 539EC536A27A0DE1 CRC64;
MFQGQRGWFC GSVSQDLRQF WVAEGGTISD PRAADFLFSC DASHPDTLRI YQSLDYIEDN
ATVFHAYYLS AVANAKIKNS VALGHFILPP ACLQKEIRRK IGSFIWEQDQ HFLIEKHDEV
TPNEIKTLRE NSELATEHKK ELSKSPEKHF IRTPVVEKQM YFPLQNYPVN NMVTGYISID
AMKKFLGELH DFIPGTSGYL AYHVQNEINM SAIKNKLKRK
