TEX14_RAT
ID TEX14_RAT Reviewed; 1443 AA.
AC F1M5M3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Inactive serine/threonine-protein kinase TEX14;
DE AltName: Full=Testis-expressed sequence 14;
DE AltName: Full=Testis-expressed sequence 14 protein;
GN Name=Tex14;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-186; SER-561;
RP SER-659; SER-1214; SER-1350; SER-1351 AND SER-1442, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required both for the formation of intercellular bridges
CC during meiosis and for kinetochore-microtubule attachment during
CC mitosis. Intercellular bridges are evolutionarily conserved structures
CC that connect differentiating germ cells and are required for
CC spermatogenesis and male fertility. Acts by promoting the conversion of
CC midbodies into intercellular bridges via its interaction with CEP55:
CC interaction with CEP55 inhibits the interaction between CEP55 and
CC PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to
CC transform midbodies into intercellular bridges. Also plays a role
CC during mitosis: recruited to kinetochores by PLK1 during early mitosis
CC and regulates the maturation of the outer kinetochores and microtubule
CC attachment. Has no protein kinase activity in vitro (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KIF23 and RBM44. Interacts with CEP55;
CC inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the
CC intercellular bridges that connect male germ cell daughter cells after
CC cell division. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DOMAIN: The GPPX3Y motif mediates interaction with CEP55.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Thr residues by CDK1 during early phases of
CC mitosis, promoting the interaction with PLK1 and recruitment to
CC kinetochores. Phosphorylated on Ser-431 by PLK1 during late
CC prometaphase promotes the rapid depletion from kinetochores and its
CC subsequent degradation by the APC/C complex.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-370 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR STRING; 10116.ENSRNOP00000009077; -.
DR iPTMnet; F1M5M3; -.
DR PhosphoSitePlus; F1M5M3; -.
DR PaxDb; F1M5M3; -.
DR PRIDE; F1M5M3; -.
DR RGD; 1305437; Tex14.
DR eggNOG; ENOG502QSZN; Eukaryota.
DR InParanoid; F1M5M3; -.
DR PRO; PR:F1M5M3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0043063; P:intercellular bridge organization; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR039339; Tex14.
DR PANTHER; PTHR23060; PTHR23060; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1443
FT /note="Inactive serine/threonine-protein kinase TEX14"
FT /id="PRO_0000417522"
FT REPEAT 27..54
FT /note="ANK 1"
FT REPEAT 55..84
FT /note="ANK 2"
FT REPEAT 88..117
FT /note="ANK 3"
FT DOMAIN 199..512
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 514..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 788..794
FT /note="GPPX3Y"
FT MOTIF 886..894
FT /note="D-box"
FT COMPBIAS 547..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 431
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1443 AA; 162407 MW; DF65D0C19BB43E0E CRC64;
MSRAVHFPVP CPVLLGTLTD DSLEAQLHEY AKQGNYVKVK KILKKGVCVD AVNTLGQSAL
FVAALLGYVK LVDVLVDYGS DPNHRCFDGS TPVHAAAFSG NQWILSKVLT AGGDLRLHDE
KGRNPQAWAL AAGKDRSTQM VEFMQRCASH MKAVIQGFSY DLLKKIDSPQ RLIGSPPWFG
GLIQGSPNSS PNRQPKPGII SAQNIYSFGF GKFYLTSGMQ LTYPGSLPVI GEKEVIQADD
EPTFSFFSGP YMVMTNLVWN RSRVTVKELN LPTHPHCSRL RLADLLIAEQ EHSSNLRHPS
LLQLMAVCLS RDLEKIRLVY ERITVGTLFS VLHERRSQFP VLHMEMIVHL LLQIADALIY
LHSRGFIHRS LSSYAVHIVS AGEARLTNLE YMMESQDSGA HRDMTRVPLP AQLYNWAAPE
VVLQKTATVK SDIYSFSMII QEILTDNIPW NGLDGSLVKE TIALGNYLEA DVRLPEPYYD
IVKSGIHAKQ KNRTMNLQDI RYILKNDLKE FIGAQKTQTT ESPRGQRYEP HPDINICLGL
TSEYQKDPPD LDIKELKETG SQPHSPTDHS FLTEKTLAPQ TLDSSLSAQE PDNPNVPSAS
RLAEEVRSPT PSEASLYSFE INEIYSGCLT LGTDKEEECP GTASSPEGDK ANQVDELPSL
EEELDKMERE LHCFCEEDKS FSDVDTDLSF EDGDWQSDSL SSLSLPEPTR EAKGKTSSWS
KTDEYVSKCV LNLKISQVMM QQSAEWLRKL EQEVDELEWA QKELDNQCRS LWDASLRFAN
TKFLSAVGPP SLTYLPPVMQ LSEPKQPENG GNWLTLARPP GNERDFQEGN FSKKSEKLSA
CDWNPFTQAS EESRGYCSEP NNQPPTLCGP GKQNTGEQLP STEEAKESLE RNTNQNIRRM
ESVSSEVCDT KSRNNEDAGE ARSKWRLAVK EMAEKAVSGQ LLVPPWNLQS SFESKVENES
TPLPRPPIRG PESTDWQYIL EYQREKDELK GNMKFGKMEN SDCDKNKHSS WTGLQRFTSI
IYPFFRNHEQ PEHNEASQAS CDTXCGEKFY STSSPIEDDF ERIQSSFAQP QGYVEENFQI
REIFGKNAEI LTKPQFQAVQ CAEDEQEETL EETPKELKEK NISLTDIQDL SSITYEQDGC
FKETSCKTPK LKHAPTSAST PLSPESISSA ASHYEDCLEN TFHVKRGSTF CWNGQEAMRT
LSTKFTTVRE RAKSLESLLA SSKTLPAKLT DPKRLCMFGG ACSSNISTAF VTSTHSTKRK
SLPGELAEAT SQHHIDELPP PAQELLDEIE QLKQQQVSSM VSLENTAHDL NVTENDKKHL
EEQETNSSKD SSFLSSREIQ DLEDTERAHS SLDEDLERLL QLPEENMTLL DPTKGSTREK
KTKDQDMVEQ KRKKKEGIKP ERRKSDSFLG TLEEDELKPC FWKRLGWSEP SRIIVLDQSD
LSD
