Full text data of TOM1L2
TOM1L2
[Confidence: low (only semi-automatic identification from reviews)]
TOM1-like protein 2 (Target of Myb-like protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TOM1-like protein 2 (Target of Myb-like protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6ZVM7
ID TM1L2_HUMAN Reviewed; 507 AA.
AC Q6ZVM7; B7Z7F4; Q86V61; Q8TDE7; Q96M88;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=TOM1-like protein 2;
DE AltName: Full=Target of Myb-like protein 2;
GN Name=TOM1L2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=11997338; DOI=10.1101/gr.73702;
RA Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA Lupski J.R.;
RT "Genes in a refined Smith-Magenis syndrome critical deletion interval
RT on chromosome 17p11.2 and the syntenic region of the mouse.";
RL Genome Res. 12:713-728(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Testis, and Uterus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH CLATHRIN AND TOLLIP.
RX PubMed=16412388; DOI=10.1016/j.bbrc.2005.12.156;
RA Katoh Y., Imakagura H., Futatsumori M., Nakayama K.;
RT "Recruitment of clathrin onto endosomes by the Tom1-Tollip complex.";
RL Biochem. Biophys. Res. Commun. 341:143-149(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH SRC.
RX PubMed=16479011; DOI=10.1128/MCB.26.5.1932-1947.2006;
RA Franco M., Furstoss O., Simon V., Benistant C., Hong W.J., Roche S.;
RT "The adaptor protein Tom1L1 is a negative regulator of Src mitogenic
RT signaling induced by growth factors.";
RL Mol. Cell. Biol. 26:1932-1947(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND THR-164, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Probable role in protein transport. May regulate growth
CC factor-induced mitogenic signaling.
CC -!- SUBUNIT: Interacts with clathrin, SRC and TOLLIP.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZVM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZVM7-2; Sequence=VSP_023391;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6ZVM7-3; Sequence=VSP_023392;
CC Name=4;
CC IsoId=Q6ZVM7-4; Sequence=VSP_023390;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
CC in heart and skeletal muscle.
CC -!- DOMAIN: The GAT domain mediates interaction with TOLLIP.
CC -!- SIMILARITY: Belongs to the TOM1 family.
CC -!- SIMILARITY: Contains 1 GAT domain.
CC -!- SIMILARITY: Contains 1 VHS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL78338.1; Type=Frameshift; Positions=101, 121, 170;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF467441; AAL78338.1; ALT_SEQ; mRNA.
DR EMBL; AK057308; BAB71421.1; -; mRNA.
DR EMBL; AK124331; BAC85834.1; -; mRNA.
DR EMBL; AK301944; BAH13590.1; -; mRNA.
DR EMBL; AC122129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051650; AAH51650.1; -; mRNA.
DR RefSeq; NP_001028723.1; NM_001033551.2.
DR RefSeq; NP_001076437.1; NM_001082968.1.
DR RefSeq; XP_005256522.1; XM_005256465.1.
DR RefSeq; XP_005256526.1; XM_005256469.1.
DR UniGene; Hs.462379; -.
DR ProteinModelPortal; Q6ZVM7; -.
DR SMR; Q6ZVM7; 2-153, 212-311.
DR IntAct; Q6ZVM7; 3.
DR MINT; MINT-1180181; -.
DR STRING; 9606.ENSP00000368818; -.
DR PhosphoSite; Q6ZVM7; -.
DR DMDM; 74712301; -.
DR PaxDb; Q6ZVM7; -.
DR PRIDE; Q6ZVM7; -.
DR Ensembl; ENST00000318094; ENSP00000312860; ENSG00000175662.
DR Ensembl; ENST00000379504; ENSP00000368818; ENSG00000175662.
DR Ensembl; ENST00000395739; ENSP00000379088; ENSG00000175662.
DR Ensembl; ENST00000478943; ENSP00000463313; ENSG00000175662.
DR Ensembl; ENST00000581396; ENSP00000464297; ENSG00000175662.
DR GeneID; 146691; -.
DR KEGG; hsa:146691; -.
DR UCSC; uc002grz.4; human.
DR CTD; 146691; -.
DR GeneCards; GC17M017746; -.
DR HGNC; HGNC:11984; TOM1L2.
DR HPA; HPA022541; -.
DR HPA; HPA023304; -.
DR neXtProt; NX_Q6ZVM7; -.
DR PharmGKB; PA36668; -.
DR eggNOG; NOG118960; -.
DR HOGENOM; HOG000285970; -.
DR HOVERGEN; HBG025068; -.
DR OMA; SLQHCNP; -.
DR OrthoDB; EOG75B859; -.
DR GeneWiki; TOM1L2; -.
DR GenomeRNAi; 146691; -.
DR NextBio; 85414; -.
DR PMAP-CutDB; Q6ZVM7; -.
DR PRO; PR:Q6ZVM7; -.
DR ArrayExpress; Q6ZVM7; -.
DR Bgee; Q6ZVM7; -.
DR CleanEx; HS_TOM1L2; -.
DR Genevestigator; Q6ZVM7; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR027429; TOM1L2.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
DR PANTHER; PTHR13856:SF31; PTHR13856:SF31; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036948; TOM1; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 507 TOM1-like protein 2.
FT /FTId=PRO_0000278790.
FT DOMAIN 20 152 VHS.
FT DOMAIN 219 307 GAT.
FT MOTIF 329 334 Clathrin-binding.
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 164 164 Phosphothreonine.
FT VAR_SEQ 1 267 Missing (in isoform 4).
FT /FTId=VSP_023390.
FT VAR_SEQ 73 122 Missing (in isoform 2).
FT /FTId=VSP_023391.
FT VAR_SEQ 123 167 Missing (in isoform 3).
FT /FTId=VSP_023392.
FT CONFLICT 12 12 P -> A (in Ref. 1; AAL78338).
FT CONFLICT 177 177 T -> S (in Ref. 1; AAL78338).
FT CONFLICT 323 323 N -> S (in Ref. 1; AAL78338).
FT CONFLICT 331 331 I -> L (in Ref. 1; AAL78338).
FT CONFLICT 347 347 N -> S (in Ref. 1; AAL78338).
FT CONFLICT 400 400 K -> Q (in Ref. 1; AAL78338).
FT CONFLICT 466 466 E -> V (in Ref. 1; AAL78338).
FT CONFLICT 475 475 P -> H (in Ref. 1; AAL78338).
SQ SEQUENCE 507 AA; 55556 MW; 6CB4B4433076D8D0 CRC64;
MEFLLGNPFS TPVGQCLEKA TDGSLQSEDW TLNMEICDII NETEEGPKDA IRALKKRLNG
NRNYREVMLA LTVLETCVKN CGHRFHILVA NRDFIDSVLV KIISPKNNPP TIVQDKVLAL
IQAWADAFRS SPDLTGVVHI YEELKRKGVE FPMADLDALS PIHTPQRSVP EVDPAATMPR
SQSQQRTSAG SYSSPPPAPY SAPQAPALSV TGPITANSEQ IARLRSELDV VRGNTKVMSE
MLTEMVPGQE DSSDLELLQE LNRTCRAMQQ RIVELISRVS NEEVTEELLH VNDDLNNVFL
RYERFERYRS GRSVQNASNG VLNEVTEDNL IDLGPGSPAV VSPMVGNTAP PSSLSSQLAG
LDLGTESVSG TLSSLQQCNP RDGFDMFAQT RGNSLAEQRK TVTYEDPQAV GGLASALDNR
KQSSEGIPVA QPSVMDDIEV WLRTDLKGDD LEEGVTSEEF DKFLEERAKA AEMVPDLPSP
PMEAPAPASN PSGRKKPERS EDALFAL
//
ID TM1L2_HUMAN Reviewed; 507 AA.
AC Q6ZVM7; B7Z7F4; Q86V61; Q8TDE7; Q96M88;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=TOM1-like protein 2;
DE AltName: Full=Target of Myb-like protein 2;
GN Name=TOM1L2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=11997338; DOI=10.1101/gr.73702;
RA Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA Lupski J.R.;
RT "Genes in a refined Smith-Magenis syndrome critical deletion interval
RT on chromosome 17p11.2 and the syntenic region of the mouse.";
RL Genome Res. 12:713-728(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Testis, and Uterus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH CLATHRIN AND TOLLIP.
RX PubMed=16412388; DOI=10.1016/j.bbrc.2005.12.156;
RA Katoh Y., Imakagura H., Futatsumori M., Nakayama K.;
RT "Recruitment of clathrin onto endosomes by the Tom1-Tollip complex.";
RL Biochem. Biophys. Res. Commun. 341:143-149(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH SRC.
RX PubMed=16479011; DOI=10.1128/MCB.26.5.1932-1947.2006;
RA Franco M., Furstoss O., Simon V., Benistant C., Hong W.J., Roche S.;
RT "The adaptor protein Tom1L1 is a negative regulator of Src mitogenic
RT signaling induced by growth factors.";
RL Mol. Cell. Biol. 26:1932-1947(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND THR-164, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Probable role in protein transport. May regulate growth
CC factor-induced mitogenic signaling.
CC -!- SUBUNIT: Interacts with clathrin, SRC and TOLLIP.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZVM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZVM7-2; Sequence=VSP_023391;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6ZVM7-3; Sequence=VSP_023392;
CC Name=4;
CC IsoId=Q6ZVM7-4; Sequence=VSP_023390;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
CC in heart and skeletal muscle.
CC -!- DOMAIN: The GAT domain mediates interaction with TOLLIP.
CC -!- SIMILARITY: Belongs to the TOM1 family.
CC -!- SIMILARITY: Contains 1 GAT domain.
CC -!- SIMILARITY: Contains 1 VHS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL78338.1; Type=Frameshift; Positions=101, 121, 170;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF467441; AAL78338.1; ALT_SEQ; mRNA.
DR EMBL; AK057308; BAB71421.1; -; mRNA.
DR EMBL; AK124331; BAC85834.1; -; mRNA.
DR EMBL; AK301944; BAH13590.1; -; mRNA.
DR EMBL; AC122129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051650; AAH51650.1; -; mRNA.
DR RefSeq; NP_001028723.1; NM_001033551.2.
DR RefSeq; NP_001076437.1; NM_001082968.1.
DR RefSeq; XP_005256522.1; XM_005256465.1.
DR RefSeq; XP_005256526.1; XM_005256469.1.
DR UniGene; Hs.462379; -.
DR ProteinModelPortal; Q6ZVM7; -.
DR SMR; Q6ZVM7; 2-153, 212-311.
DR IntAct; Q6ZVM7; 3.
DR MINT; MINT-1180181; -.
DR STRING; 9606.ENSP00000368818; -.
DR PhosphoSite; Q6ZVM7; -.
DR DMDM; 74712301; -.
DR PaxDb; Q6ZVM7; -.
DR PRIDE; Q6ZVM7; -.
DR Ensembl; ENST00000318094; ENSP00000312860; ENSG00000175662.
DR Ensembl; ENST00000379504; ENSP00000368818; ENSG00000175662.
DR Ensembl; ENST00000395739; ENSP00000379088; ENSG00000175662.
DR Ensembl; ENST00000478943; ENSP00000463313; ENSG00000175662.
DR Ensembl; ENST00000581396; ENSP00000464297; ENSG00000175662.
DR GeneID; 146691; -.
DR KEGG; hsa:146691; -.
DR UCSC; uc002grz.4; human.
DR CTD; 146691; -.
DR GeneCards; GC17M017746; -.
DR HGNC; HGNC:11984; TOM1L2.
DR HPA; HPA022541; -.
DR HPA; HPA023304; -.
DR neXtProt; NX_Q6ZVM7; -.
DR PharmGKB; PA36668; -.
DR eggNOG; NOG118960; -.
DR HOGENOM; HOG000285970; -.
DR HOVERGEN; HBG025068; -.
DR OMA; SLQHCNP; -.
DR OrthoDB; EOG75B859; -.
DR GeneWiki; TOM1L2; -.
DR GenomeRNAi; 146691; -.
DR NextBio; 85414; -.
DR PMAP-CutDB; Q6ZVM7; -.
DR PRO; PR:Q6ZVM7; -.
DR ArrayExpress; Q6ZVM7; -.
DR Bgee; Q6ZVM7; -.
DR CleanEx; HS_TOM1L2; -.
DR Genevestigator; Q6ZVM7; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR027429; TOM1L2.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
DR PANTHER; PTHR13856:SF31; PTHR13856:SF31; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036948; TOM1; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 507 TOM1-like protein 2.
FT /FTId=PRO_0000278790.
FT DOMAIN 20 152 VHS.
FT DOMAIN 219 307 GAT.
FT MOTIF 329 334 Clathrin-binding.
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 164 164 Phosphothreonine.
FT VAR_SEQ 1 267 Missing (in isoform 4).
FT /FTId=VSP_023390.
FT VAR_SEQ 73 122 Missing (in isoform 2).
FT /FTId=VSP_023391.
FT VAR_SEQ 123 167 Missing (in isoform 3).
FT /FTId=VSP_023392.
FT CONFLICT 12 12 P -> A (in Ref. 1; AAL78338).
FT CONFLICT 177 177 T -> S (in Ref. 1; AAL78338).
FT CONFLICT 323 323 N -> S (in Ref. 1; AAL78338).
FT CONFLICT 331 331 I -> L (in Ref. 1; AAL78338).
FT CONFLICT 347 347 N -> S (in Ref. 1; AAL78338).
FT CONFLICT 400 400 K -> Q (in Ref. 1; AAL78338).
FT CONFLICT 466 466 E -> V (in Ref. 1; AAL78338).
FT CONFLICT 475 475 P -> H (in Ref. 1; AAL78338).
SQ SEQUENCE 507 AA; 55556 MW; 6CB4B4433076D8D0 CRC64;
MEFLLGNPFS TPVGQCLEKA TDGSLQSEDW TLNMEICDII NETEEGPKDA IRALKKRLNG
NRNYREVMLA LTVLETCVKN CGHRFHILVA NRDFIDSVLV KIISPKNNPP TIVQDKVLAL
IQAWADAFRS SPDLTGVVHI YEELKRKGVE FPMADLDALS PIHTPQRSVP EVDPAATMPR
SQSQQRTSAG SYSSPPPAPY SAPQAPALSV TGPITANSEQ IARLRSELDV VRGNTKVMSE
MLTEMVPGQE DSSDLELLQE LNRTCRAMQQ RIVELISRVS NEEVTEELLH VNDDLNNVFL
RYERFERYRS GRSVQNASNG VLNEVTEDNL IDLGPGSPAV VSPMVGNTAP PSSLSSQLAG
LDLGTESVSG TLSSLQQCNP RDGFDMFAQT RGNSLAEQRK TVTYEDPQAV GGLASALDNR
KQSSEGIPVA QPSVMDDIEV WLRTDLKGDD LEEGVTSEEF DKFLEERAKA AEMVPDLPSP
PMEAPAPASN PSGRKKPERS EDALFAL
//