KASH5_HUMAN
ID KASH5_HUMAN Reviewed; 562 AA.
AC Q8N6L0; Q96MC3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein KASH5 {ECO:0000305};
DE AltName: Full=Coiled-coil domain-containing protein 155;
DE AltName: Full=KASH domain-containing protein 5;
GN Name=KASH5 {ECO:0000312|HGNC:HGNC:26520}; Synonyms=CCDC155;
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=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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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], AND VARIANT GLN-129.
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).
CC -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC Cytoskeleton) complex, involved in the connection between the nuclear
CC lamina and the cytoskeleton. The nucleocytoplasmic interactions
CC established by the LINC complex play an important role in the
CC transmission of mechanical forces across the nuclear envelope and in
CC nuclear movement and positioning. Required for telomere attachment to
CC nuclear envelope in the prophase of meiosis and for rapid telomere
CC prophase movements implicating a SUN1/2:KASH5 LINC complex in which
CC SUN1 and SUN2 seem to act at least partial redundantly. Required for
CC homolog pairing during meiotic prophase in spermatocytes and probably
CC oocytes. Essential for male and female gametogenesis. Recruits
CC cytoplasmic dynein to telomere attachment sites at the nuclear envelope
CC in spermatocytes. In oocytes is involved in meiotic resumption and
CC spindle formation. {ECO:0000250|UniProtKB:Q80VJ8}.
CC -!- SUBUNIT: Core component the LINC complex which is composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC containing proteins seem to bind each other promiscuously; however,
CC differentially expression of LINC complex constituents is giving rise
CC to specific assemblies. At least SUN1/2-containing core LINC complexes
CC are proposed to be hexameric composed of three protomers of each KASH
CC and SUN domain-containing protein. Interacts (via the last 22 AA) with
CC SUN1; this interaction mediates its telomere localization by forming a
CC SUN1:KASH5 LINC complex. Component of a probable SUN2:KASH5 LINC
CC complex. Self-associates. Interacts with DYNC1H1, DCTN1, DYNC1I1/2 and
CC PAFAH1B1; suggesting the association with the dynein-dynactin motor
CC complex. {ECO:0000250|UniProtKB:Q80VJ8}.
CC -!- INTERACTION:
CC Q8N6L0; Q96SE0: ABHD1; NbExp=3; IntAct=EBI-749265, EBI-10293349;
CC Q8N6L0; A8K660: ADIPOQ; NbExp=3; IntAct=EBI-749265, EBI-10174479;
CC Q8N6L0; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-749265, EBI-10827839;
CC Q8N6L0; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-749265, EBI-12109402;
CC Q8N6L0; P17544: ATF7; NbExp=3; IntAct=EBI-749265, EBI-765623;
CC Q8N6L0; Q9UL15: BAG5; NbExp=6; IntAct=EBI-749265, EBI-356517;
CC Q8N6L0; Q92843: BCL2L2; NbExp=8; IntAct=EBI-749265, EBI-707714;
CC Q8N6L0; O15155: BET1; NbExp=3; IntAct=EBI-749265, EBI-749204;
CC Q8N6L0; Q53XK0: BET1; NbExp=3; IntAct=EBI-749265, EBI-10242927;
CC Q8N6L0; D3DR40: C10orf4; NbExp=3; IntAct=EBI-749265, EBI-10176576;
CC Q8N6L0; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-749265, EBI-744556;
CC Q8N6L0; Q6P1J9: CDC73; NbExp=6; IntAct=EBI-749265, EBI-930143;
CC Q8N6L0; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-749265, EBI-3919850;
CC Q8N6L0; Q96Q77: CIB3; NbExp=3; IntAct=EBI-749265, EBI-10292696;
CC Q8N6L0; P56748: CLDN8; NbExp=3; IntAct=EBI-749265, EBI-10215641;
CC Q8N6L0; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-749265, EBI-11522780;
CC Q8N6L0; P29373: CRABP2; NbExp=6; IntAct=EBI-749265, EBI-10204806;
CC Q8N6L0; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-749265, EBI-12019274;
CC Q8N6L0; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-749265, EBI-5453285;
CC Q8N6L0; Q07325: CXCL9; NbExp=3; IntAct=EBI-749265, EBI-3911467;
CC Q8N6L0; Q9BQA9: CYBC1; NbExp=6; IntAct=EBI-749265, EBI-2680384;
CC Q8N6L0; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-749265, EBI-398977;
CC Q8N6L0; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-749265, EBI-8639143;
CC Q8N6L0; P52803: EFNA5; NbExp=3; IntAct=EBI-749265, EBI-1753674;
CC Q8N6L0; P50402: EMD; NbExp=8; IntAct=EBI-749265, EBI-489887;
CC Q8N6L0; Q3B820: FAM161A; NbExp=3; IntAct=EBI-749265, EBI-719941;
CC Q8N6L0; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-749265, EBI-12118888;
CC Q8N6L0; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-749265, EBI-742802;
CC Q8N6L0; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-749265, EBI-6658203;
CC Q8N6L0; Q969F0: FATE1; NbExp=6; IntAct=EBI-749265, EBI-743099;
CC Q8N6L0; Q9Y3D6: FIS1; NbExp=3; IntAct=EBI-749265, EBI-3385283;
CC Q8N6L0; O95954: FTCD; NbExp=3; IntAct=EBI-749265, EBI-10192648;
CC Q8N6L0; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-749265, EBI-12175685;
CC Q8N6L0; P60520: GABARAPL2; NbExp=3; IntAct=EBI-749265, EBI-720116;
CC Q8N6L0; Q10471: GALNT2; NbExp=8; IntAct=EBI-749265, EBI-10226985;
CC Q8N6L0; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-749265, EBI-6166686;
CC Q8N6L0; O14653: GOSR2; NbExp=6; IntAct=EBI-749265, EBI-4401517;
CC Q8N6L0; Q5T3I0: GPATCH4; NbExp=6; IntAct=EBI-749265, EBI-2372076;
CC Q8N6L0; O00155: GPR25; NbExp=6; IntAct=EBI-749265, EBI-10178951;
CC Q8N6L0; Q96DI8: HMOX1; NbExp=3; IntAct=EBI-749265, EBI-10284700;
CC Q8N6L0; P11215: ITGAM; NbExp=3; IntAct=EBI-749265, EBI-2568251;
CC Q8N6L0; Q9Y287: ITM2B; NbExp=3; IntAct=EBI-749265, EBI-2866431;
CC Q8N6L0; Q8N5M9: JAGN1; NbExp=6; IntAct=EBI-749265, EBI-10266796;
CC Q8N6L0; Q6PKG0: LARP1; NbExp=3; IntAct=EBI-749265, EBI-1052114;
CC Q8N6L0; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-749265, EBI-726510;
CC Q8N6L0; Q8TAF8: LHFPL5; NbExp=9; IntAct=EBI-749265, EBI-2820517;
CC Q8N6L0; O75427: LRCH4; NbExp=3; IntAct=EBI-749265, EBI-718707;
CC Q8N6L0; Q13021: MALL; NbExp=3; IntAct=EBI-749265, EBI-750078;
CC Q8N6L0; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-749265, EBI-10317612;
CC Q8N6L0; Q6N075: MFSD5; NbExp=3; IntAct=EBI-749265, EBI-3920969;
CC Q8N6L0; P50281: MMP14; NbExp=3; IntAct=EBI-749265, EBI-992788;
CC Q8N6L0; O75425: MOSPD3; NbExp=3; IntAct=EBI-749265, EBI-12179105;
CC Q8N6L0; P11836: MS4A1; NbExp=3; IntAct=EBI-749265, EBI-2808234;
CC Q8N6L0; O75431: MTX2; NbExp=6; IntAct=EBI-749265, EBI-7415268;
CC Q8N6L0; Q8N912: NRAC; NbExp=3; IntAct=EBI-749265, EBI-12051377;
CC Q8N6L0; Q9NQ35: NRIP3; NbExp=6; IntAct=EBI-749265, EBI-10311735;
CC Q8N6L0; P42857: NSG1; NbExp=6; IntAct=EBI-749265, EBI-6380741;
CC Q8N6L0; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-749265, EBI-2804156;
CC Q8N6L0; P16234: PDGFRA; NbExp=3; IntAct=EBI-749265, EBI-2861522;
CC Q8N6L0; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-749265, EBI-12092917;
CC Q8N6L0; O00264: PGRMC1; NbExp=3; IntAct=EBI-749265, EBI-1045534;
CC Q8N6L0; Q9H490: PIGU; NbExp=3; IntAct=EBI-749265, EBI-11290294;
CC Q8N6L0; Q04941: PLP2; NbExp=3; IntAct=EBI-749265, EBI-608347;
CC Q8N6L0; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-749265, EBI-11721828;
CC Q8N6L0; Q6NYC8: PPP1R18; NbExp=6; IntAct=EBI-749265, EBI-2557469;
CC Q8N6L0; Q5TAB7: RIPPLY2; NbExp=8; IntAct=EBI-749265, EBI-10246897;
CC Q8N6L0; Q9NTX7: RNF146; NbExp=3; IntAct=EBI-749265, EBI-722397;
CC Q8N6L0; Q9NTX7-2: RNF146; NbExp=7; IntAct=EBI-749265, EBI-11750630;
CC Q8N6L0; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-749265, EBI-748350;
CC Q8N6L0; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-749265, EBI-10256202;
CC Q8N6L0; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-749265, EBI-10244780;
CC Q8N6L0; Q9HC62: SENP2; NbExp=6; IntAct=EBI-749265, EBI-714881;
CC Q8N6L0; Q8N6R1: SERP2; NbExp=6; IntAct=EBI-749265, EBI-749270;
CC Q8N6L0; O43765: SGTA; NbExp=8; IntAct=EBI-749265, EBI-347996;
CC Q8N6L0; Q9BRI3: SLC30A2; NbExp=9; IntAct=EBI-749265, EBI-8644112;
CC Q8N6L0; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-749265, EBI-10281213;
CC Q8N6L0; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-749265, EBI-12266234;
CC Q8N6L0; Q96JW4: SLC41A2; NbExp=6; IntAct=EBI-749265, EBI-10290130;
CC Q8N6L0; Q9NY91: SLC5A4; NbExp=3; IntAct=EBI-749265, EBI-12409133;
CC Q8N6L0; O00631: SLN; NbExp=3; IntAct=EBI-749265, EBI-10180786;
CC Q8N6L0; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-749265, EBI-8640191;
CC Q8N6L0; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-749265, EBI-10244848;
CC Q8N6L0; O95210: STBD1; NbExp=3; IntAct=EBI-749265, EBI-2947137;
CC Q8N6L0; Q86Y82: STX12; NbExp=3; IntAct=EBI-749265, EBI-2691717;
CC Q8N6L0; Q13190: STX5; NbExp=6; IntAct=EBI-749265, EBI-714206;
CC Q8N6L0; Q9BQ70: TCF25; NbExp=3; IntAct=EBI-749265, EBI-745182;
CC Q8N6L0; P17152: TMEM11; NbExp=5; IntAct=EBI-749265, EBI-723946;
CC Q8N6L0; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-749265, EBI-348587;
CC Q8N6L0; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-749265, EBI-2339195;
CC Q8N6L0; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-749265, EBI-741829;
CC Q8N6L0; Q8N511: TMEM199; NbExp=3; IntAct=EBI-749265, EBI-10265825;
CC Q8N6L0; Q96HV5: TMEM41A; NbExp=3; IntAct=EBI-749265, EBI-10288884;
CC Q8N6L0; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-749265, EBI-12015604;
CC Q8N6L0; Q9NRS4: TMPRSS4; NbExp=3; IntAct=EBI-749265, EBI-10313040;
CC Q8N6L0; Q9NRS4-3: TMPRSS4; NbExp=3; IntAct=EBI-749265, EBI-10312990;
CC Q8N6L0; P01375: TNF; NbExp=3; IntAct=EBI-749265, EBI-359977;
CC Q8N6L0; Q9Y228: TRAF3IP3; NbExp=6; IntAct=EBI-749265, EBI-765817;
CC Q8N6L0; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-749265, EBI-9053916;
CC Q8N6L0; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-749265, EBI-9090990;
CC Q8N6L0; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-749265, EBI-11988865;
CC Q8N6L0; O75841: UPK1B; NbExp=3; IntAct=EBI-749265, EBI-12237619;
CC Q8N6L0; O00526: UPK2; NbExp=3; IntAct=EBI-749265, EBI-10179682;
CC Q8N6L0; P23763: VAMP1; NbExp=3; IntAct=EBI-749265, EBI-10201335;
CC Q8N6L0; P63027: VAMP2; NbExp=3; IntAct=EBI-749265, EBI-520113;
CC Q8N6L0; O75379: VAMP4; NbExp=3; IntAct=EBI-749265, EBI-744953;
CC Q8N6L0; O75379-2: VAMP4; NbExp=3; IntAct=EBI-749265, EBI-10187996;
CC Q8N6L0; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-749265, EBI-723716;
CC Q8N6L0; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-749265, EBI-14104088;
CC Q8N6L0; O95159: ZFPL1; NbExp=3; IntAct=EBI-749265, EBI-718439;
CC Q8N6L0; P15622-3: ZNF250; NbExp=3; IntAct=EBI-749265, EBI-10177272;
CC Q8N6L0; B2R9H7; NbExp=3; IntAct=EBI-749265, EBI-10175711;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus
CC {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q80VJ8}. Note=Localized exclusively at telomeres
CC from the leptotene to diplotene stages. Colocalizes with SUN2 at sites
CC of telomere attachment in meiocytes. At oocyte MI stage localized
CC around the spindle, at MII stage localized to the spindle poles.
CC {ECO:0000250|UniProtKB:Q80VJ8}.
CC -!- DOMAIN: The C-terminal 22 AA is required and sufficient for
CC localization to telomeres at the nuclear envelope. {ECO:0000250}.
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DR EMBL; AK057220; BAB71384.1; -; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52478.1; -; Genomic_DNA.
DR EMBL; BC029811; AAH29811.1; -; mRNA.
DR CCDS; CCDS46140.1; -.
DR RefSeq; NP_653289.3; NM_144688.4.
DR PDB; 6R2I; X-ray; 1.54 A; B=542-562.
DR PDB; 6WMF; X-ray; 2.60 A; B=542-562.
DR PDBsum; 6R2I; -.
DR PDBsum; 6WMF; -.
DR AlphaFoldDB; Q8N6L0; -.
DR SASBDB; Q8N6L0; -.
DR SMR; Q8N6L0; -.
DR BioGRID; 127094; 155.
DR IntAct; Q8N6L0; 116.
DR MINT; Q8N6L0; -.
DR STRING; 9606.ENSP00000404220; -.
DR GlyGen; Q8N6L0; 1 site, 1 O-linked glycan (1 site).
DR BioMuta; CCDC155; -.
DR DMDM; 187671940; -.
DR MassIVE; Q8N6L0; -.
DR PaxDb; Q8N6L0; -.
DR PeptideAtlas; Q8N6L0; -.
DR PRIDE; Q8N6L0; -.
DR ProteomicsDB; 72187; -.
DR Antibodypedia; 9176; 62 antibodies from 17 providers.
DR DNASU; 147872; -.
DR Ensembl; ENST00000447857.8; ENSP00000404220.2; ENSG00000161609.10.
DR GeneID; 147872; -.
DR KEGG; hsa:147872; -.
DR MANE-Select; ENST00000447857.8; ENSP00000404220.2; NM_144688.5; NP_653289.3.
DR UCSC; uc002pnm.3; human.
DR CTD; 147872; -.
DR DisGeNET; 147872; -.
DR GeneCards; KASH5; -.
DR HGNC; HGNC:26520; KASH5.
DR HPA; ENSG00000161609; Tissue enriched (testis).
DR MIM; 618125; gene.
DR neXtProt; NX_Q8N6L0; -.
DR OpenTargets; ENSG00000161609; -.
DR PharmGKB; PA162381684; -.
DR VEuPathDB; HostDB:ENSG00000161609; -.
DR eggNOG; ENOG502RXNC; Eukaryota.
DR GeneTree; ENSGT00420000029926; -.
DR InParanoid; Q8N6L0; -.
DR OMA; RQLCECE; -.
DR OrthoDB; 335596at2759; -.
DR PhylomeDB; Q8N6L0; -.
DR TreeFam; TF337560; -.
DR PathwayCommons; Q8N6L0; -.
DR SignaLink; Q8N6L0; -.
DR SIGNOR; Q8N6L0; -.
DR BioGRID-ORCS; 147872; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; CCDC155; human.
DR GenomeRNAi; 147872; -.
DR Pharos; Q8N6L0; Tbio.
DR PRO; PR:Q8N6L0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N6L0; protein.
DR Bgee; ENSG00000161609; Expressed in right testis and 92 other tissues.
DR ExpressionAtlas; Q8N6L0; baseline and differential.
DR Genevisible; Q8N6L0; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000800; C:lateral element; IBA:GO_Central.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0090619; C:meiotic spindle pole; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0090220; P:chromosome localization to nuclear envelope involved in homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0090172; P:microtubule cytoskeleton organization involved in homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR GO; GO:0051653; P:spindle localization; IBA:GO_Central.
DR GO; GO:0034397; P:telomere localization; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR028170; KASH5.
DR InterPro; IPR028168; KASH5_coiled-coil.
DR InterPro; IPR039508; KASH5_EF-hand-like_dom.
DR PANTHER; PTHR47300; PTHR47300; 1.
DR Pfam; PF14658; EF-hand_9; 1.
DR Pfam; PF14662; KASH_CCD; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Meiosis; Membrane; Nucleus;
KW Reference proteome; Telomere; Transmembrane; Transmembrane helix.
FT CHAIN 1..562
FT /note="Protein KASH5"
FT /id="PRO_0000331527"
FT TOPO_DOM 1..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..562
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 125..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..349
FT /evidence="ECO:0000255"
FT COMPBIAS 430..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 116
FT /note="L -> P (in dbSNP:rs8102582)"
FT /id="VAR_059597"
FT VARIANT 129
FT /note="R -> Q (in dbSNP:rs10405154)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059598"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:6WMF"
SQ SEQUENCE 562 AA; 62783 MW; 39F47D3F236A9918 CRC64;
MDLPEGPVGG PTAEMYLRER PEEARLGMPV SLEEQILNST FEACDPQRTG TVAVAQVLAY
LEAVTGQGPQ DARLQTLANS LDPNGEGPKA TVDLDTFLVV MRDWIAACQL HGGLELEEET
AFQGALTSRQ LPSGCPEAEE PANLESFGGE DPRPELQATA DLLSSLEDLE LSNRRLVGEN
AKLQRSMETA EEGSARLGEE ILALRKQLHS TQQALQFAKA MDEELEDLKT LARSLEEQNR
SLLAQARQAE KEQQHLVAEM ETLQEENGKL LAERDGVKKR SQELAMEKDT LKRQLFECEH
LICQRDTILS ERTRDVESLA QTLEEYRVTT QELRLEISRL EEQLSQTYEG PDELPEGAQL
RRVGWTELLP PSLGLEIEAI RQKQEVATAD LSNPLCGVWQ WEEVIHETSE ETEFPSEAPA
GGQRNFQGEP AHPEEGRKEP SMWLTRREEE EDAESQVTAD LPVPLGAPRP GDIPENPPER
PARRELQQAL VPVMKKLVPV RRRAWGQLCL PPQRLRVTRH PLIPAPVLGL LLLLLLSVLL
LGPSPPPTWP HLQLCYLQPP PV
