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LITD1_HUMAN
ID   LITD1_HUMAN             Reviewed;         865 AA.
AC   Q5T7N2; Q8NDA1; Q9NUV8; Q9NV78;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=LINE-1 type transposase domain-containing protein 1;
DE   AltName: Full=ES cell-associated protein 11;
GN   Name=L1TD1; Synonyms=ECAT11;
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 [MRNA], AND VARIANTS ALA-246; MET-309 AND ASN-329.
RA   Yamanaka S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-246 AND MET-309.
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-246; MET-309 AND
RP   ASN-329.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-246; MET-309 AND
RP   ASN-329.
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-2; THR-149; SER-154; SER-472; SER-476; SER-478; SER-518;
RP   SER-561; SER-573; SER-640; SER-648 AND SER-665, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- INTERACTION:
CC       Q5T7N2; P22626: HNRNPA2B1; NbExp=2; IntAct=EBI-7216220, EBI-299649;
CC   -!- SIMILARITY: Belongs to the transposase 22 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91878.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA91878.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB211065; BAD95492.1; -; mRNA.
DR   EMBL; AK001746; BAA91878.1; ALT_SEQ; mRNA.
DR   EMBL; AK001973; BAA92011.1; -; mRNA.
DR   EMBL; AL834314; CAD38984.1; -; mRNA.
DR   EMBL; AL162739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111559; AAI11560.1; -; mRNA.
DR   CCDS; CCDS619.1; -.
DR   RefSeq; NP_001158307.1; NM_001164835.1.
DR   RefSeq; NP_061952.3; NM_019079.4.
DR   PDB; 2LR6; NMR; -; A/B=235-321.
DR   PDB; 3SOO; X-ray; 2.73 A; A/B/C=235-321.
DR   PDBsum; 2LR6; -.
DR   PDBsum; 3SOO; -.
DR   AlphaFoldDB; Q5T7N2; -.
DR   SMR; Q5T7N2; -.
DR   BioGRID; 120072; 26.
DR   IntAct; Q5T7N2; 327.
DR   MINT; Q5T7N2; -.
DR   STRING; 9606.ENSP00000419901; -.
DR   GlyGen; Q5T7N2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5T7N2; -.
DR   PhosphoSitePlus; Q5T7N2; -.
DR   BioMuta; L1TD1; -.
DR   DMDM; 74745406; -.
DR   EPD; Q5T7N2; -.
DR   jPOST; Q5T7N2; -.
DR   MassIVE; Q5T7N2; -.
DR   PaxDb; Q5T7N2; -.
DR   PeptideAtlas; Q5T7N2; -.
DR   PRIDE; Q5T7N2; -.
DR   ProteomicsDB; 64668; -.
DR   Antibodypedia; 33329; 83 antibodies from 23 providers.
DR   DNASU; 54596; -.
DR   Ensembl; ENST00000498273.2; ENSP00000419901.1; ENSG00000240563.2.
DR   GeneID; 54596; -.
DR   KEGG; hsa:54596; -.
DR   MANE-Select; ENST00000498273.2; ENSP00000419901.1; NM_019079.5; NP_061952.3.
DR   UCSC; uc001dae.6; human.
DR   CTD; 54596; -.
DR   DisGeNET; 54596; -.
DR   GeneCards; L1TD1; -.
DR   HGNC; HGNC:25595; L1TD1.
DR   HPA; ENSG00000240563; Group enriched (brain, intestine, lymphoid tissue, placenta, testis).
DR   neXtProt; NX_Q5T7N2; -.
DR   OpenTargets; ENSG00000240563; -.
DR   PharmGKB; PA145008170; -.
DR   VEuPathDB; HostDB:ENSG00000240563; -.
DR   eggNOG; ENOG502SRQ0; Eukaryota.
DR   GeneTree; ENSGT01050000244818; -.
DR   HOGENOM; CLU_336140_0_0_1; -.
DR   InParanoid; Q5T7N2; -.
DR   OMA; FEPKFLC; -.
DR   OrthoDB; 455018at2759; -.
DR   PhylomeDB; Q5T7N2; -.
DR   TreeFam; TF351152; -.
DR   PathwayCommons; Q5T7N2; -.
DR   SignaLink; Q5T7N2; -.
DR   BioGRID-ORCS; 54596; 15 hits in 1041 CRISPR screens.
DR   EvolutionaryTrace; Q5T7N2; -.
DR   GeneWiki; L1TD1; -.
DR   GenomeRNAi; 54596; -.
DR   Pharos; Q5T7N2; Tbio.
DR   PRO; PR:Q5T7N2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5T7N2; protein.
DR   Bgee; ENSG00000240563; Expressed in placenta and 65 other tissues.
DR   Genevisible; Q5T7N2; HS.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0032197; P:transposition, RNA-mediated; IBA:GO_Central.
DR   Gene3D; 3.30.250.20; -; 2.
DR   InterPro; IPR042566; L1_C.
DR   InterPro; IPR035300; L1_dsRBD.
DR   InterPro; IPR043636; L1_RRM_dom.
DR   InterPro; IPR004244; Transposase_22.
DR   PANTHER; PTHR11505; PTHR11505; 1.
DR   Pfam; PF17490; Tnp_22_dsRBD; 2.
DR   Pfam; PF02994; Transposase_22; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CHAIN           2..865
FT                   /note="LINE-1 type transposase domain-containing protein 1"
FT                   /id="PRO_0000307217"
FT   REGION          370..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          642..684
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        379..441
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         149
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         561
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         573
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VARIANT         27
FT                   /note="R -> S (in dbSNP:rs7552335)"
FT                   /id="VAR_035377"
FT   VARIANT         246
FT                   /note="V -> A (in dbSNP:rs7542665)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.1"
FT                   /id="VAR_035378"
FT   VARIANT         309
FT                   /note="V -> M (in dbSNP:rs7533274)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.1"
FT                   /id="VAR_035379"
FT   VARIANT         329
FT                   /note="K -> N (in dbSNP:rs2457828)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1"
FT                   /id="VAR_035380"
FT   VARIANT         549
FT                   /note="P -> T (in dbSNP:rs11207933)"
FT                   /id="VAR_035381"
FT   VARIANT         613
FT                   /note="T -> I (in dbSNP:rs2886644)"
FT                   /id="VAR_035382"
FT   VARIANT         860
FT                   /note="L -> V (in dbSNP:rs11207934)"
FT                   /id="VAR_051094"
FT   CONFLICT        548
FT                   /note="T -> I (in Ref. 2; BAA92011)"
FT                   /evidence="ECO:0000305"
FT   TURN            248..250
FT                   /evidence="ECO:0007829|PDB:2LR6"
FT   HELIX           258..269
FT                   /evidence="ECO:0007829|PDB:3SOO"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:3SOO"
FT   STRAND          287..295
FT                   /evidence="ECO:0007829|PDB:3SOO"
FT   HELIX           296..304
FT                   /evidence="ECO:0007829|PDB:3SOO"
FT   HELIX           307..310
FT                   /evidence="ECO:0007829|PDB:3SOO"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:3SOO"
SQ   SEQUENCE   865 AA;  98850 MW;  C7E33893A1E675CC CRC64;
     MSDVSTSVQS KFARLAKKKE NITYMKREQL TETDKDIAPV LDLKCKDVSA IMNKFKVLME
     IQDLMFEEMR ETLKNDLKAV LGGKATIPEV KNSENSSSRT EFQQIINLAL QKTGMVGKIE
     GENSKIGDDN ENLTFKLEVN ELSGKLDNTN EYNSNDGKKL PQGESRSYEV MGSMEETLCN
     IDDRDGNRNV HLEFTERESR KDGEDEFVKE MREERKFQKL KNKEEVLKAS REEKVLMDEG
     AVLTLVADLS SATLDISKQW SNVFNILREN DFEPKFLCEV KLAFKCDGEI KTFSDLQSLR
     KFASQKSSVK ELLKDVLPQK EEINQGGRKY GIQEKRDKTL IDSKHRAGEI TSDGLSFLFL
     KEVKVAKPEE MKNLETQEEE FSELEELDEE ASGMEDDEDT SGLEEEEEEP SGLEEEEEEE
     ASGLEEDEAS GLEEEEEQTS EQDSTFQGHT LVDAKHEVEI TSDGMETTFI DSVEDSESEE
     EEEGKSSETG KVKTTSLTEK KASRRQKEIP FSYLVGDSGK KKLVKHQVVH KTQEEEETAV
     PTSQGTGTPC LTLCLASPSK SLEMSHDEHK KHSHTNLSIS TGVTKLKKTE EKKHRTLHTE
     ELTSKEADLT EETEENLRSS VINSIREIKE EIGNLKSSHS GVLEIENSVD DLSSRMDILE
     ERIDSLEDQI EEFSKDTMQM TKQIISKERQ RDIEERSRSC NIRLIGIPEK ESYENRAEDI
     IKEIIDENFA ELKKGSSLEI VSACRVPSKI DEKRLTPRHI LVKFWNSSDK EKIIRASRER
     REITYQGTRI RLTADLSLDT LDARSKWSNV FKVLLEKGFN PRILYPAKMA FDFRGKTKVF
     LSIEEFRDYV LHMPTLRELL GNNIP
 
 
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