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AMOL2_HUMAN
ID   AMOL2_HUMAN             Reviewed;         779 AA.
AC   Q9Y2J4; A8K6F1; B7Z5Q1; E9PHW3; Q53EP1; Q96F99; Q9UKB4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Angiomotin-like protein 2;
DE   AltName: Full=Leman coiled-coil protein;
DE            Short=LCCP;
GN   Name=AMOTL2; Synonyms=KIAA0989;
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] (ISOFORM 2), AND VARIANT ASP-731.
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
RP   ASP-731.
RC   TISSUE=Placenta, and Teratocarcinoma;
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] (ISOFORM 3), AND VARIANT ASP-731.
RC   TISSUE=Kidney;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 211-779 (ISOFORM 1), AND VARIANT ASP-731.
RC   TISSUE=Glioblastoma;
RX   PubMed=12406577; DOI=10.1016/s0378-1119(02)00928-9;
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA   Holmgren L.;
RT   "Angiomotin belongs to a novel protein family with conserved coiled-coil
RT   and PDZ binding domains.";
RL   Gene 298:69-77(2002).
RN   [5]
RP   ERRATUM OF PUBMED:12406577.
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA   Holmgren L.;
RL   Gene 310:231-231(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-779 (ISOFORM 1).
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).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH SRC.
RX   PubMed=17293535; DOI=10.1242/dev.02782;
RA   Huang H., Lu F.I., Jia S., Meng S., Cao Y., Wang Y., Ma W., Yin K., Wen Z.,
RA   Peng J., Thisse C., Thisse B., Meng A.;
RT   "Amotl2 is essential for cell movements in zebrafish embryo and regulates
RT   c-Src translocation.";
RL   Development 134:979-988(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   FUNCTION.
RX   PubMed=21937427; DOI=10.1074/jbc.m111.296806;
RA   Wang Y., Li Z., Xu P., Huang L., Tong J., Huang H., Meng A.;
RT   "Angiomotin-like2 gene (amotl2) is required for migration and proliferation
RT   of endothelial cells during angiogenesis.";
RL   J. Biol. Chem. 286:41095-41104(2011).
RN   [11]
RP   FUNCTION.
RX   PubMed=22362771; DOI=10.1074/jbc.m112.347419;
RA   Li Z., Wang Y., Zhang M., Xu P., Huang H., Wu D., Meng A.;
RT   "The Amotl2 gene inhibits Wnt/beta-catenin signaling and regulates
RT   embryonic development in zebrafish.";
RL   J. Biol. Chem. 287:13005-13015(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Regulates the translocation of phosphorylated SRC to
CC       peripheral cell-matrix adhesion sites. Required for proper architecture
CC       of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway,
CC       probably by recruiting CTNNB1 to recycling endosomes and hence
CC       preventing its translocation to the nucleus. Participates in
CC       angiogenesis. May play a role in the polarity, proliferation and
CC       migration of endothelial cells. Selectively promotes FGF-induced MAPK
CC       activation through SRC. {ECO:0000269|PubMed:17293535,
CC       ECO:0000269|PubMed:21937427, ECO:0000269|PubMed:22362771}.
CC   -!- SUBUNIT: Interacts with SRC. {ECO:0000269|PubMed:17293535}.
CC   -!- INTERACTION:
CC       Q9Y2J4; A2BDD9: AMOT; NbExp=3; IntAct=EBI-746752, EBI-17286414;
CC       Q9Y2J4; Q13515: BFSP2; NbExp=3; IntAct=EBI-746752, EBI-10229433;
CC       Q9Y2J4; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-746752, EBI-5666615;
CC       Q9Y2J4; Q13895: BYSL; NbExp=3; IntAct=EBI-746752, EBI-358049;
CC       Q9Y2J4; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-746752, EBI-11530605;
CC       Q9Y2J4; Q8N715: CCDC185; NbExp=3; IntAct=EBI-746752, EBI-740814;
CC       Q9Y2J4; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-746752, EBI-10181422;
CC       Q9Y2J4; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-746752, EBI-10961624;
CC       Q9Y2J4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-746752, EBI-10175300;
CC       Q9Y2J4; Q16543: CDC37; NbExp=3; IntAct=EBI-746752, EBI-295634;
CC       Q9Y2J4; Q9BW66: CINP; NbExp=3; IntAct=EBI-746752, EBI-739784;
CC       Q9Y2J4; Q9UER7: DAXX; NbExp=3; IntAct=EBI-746752, EBI-77321;
CC       Q9Y2J4; O60941-5: DTNB; NbExp=3; IntAct=EBI-746752, EBI-11984733;
CC       Q9Y2J4; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-746752, EBI-10264440;
CC       Q9Y2J4; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-746752, EBI-6658203;
CC       Q9Y2J4; Q96RD9: FCRL5; NbExp=3; IntAct=EBI-746752, EBI-12091825;
CC       Q9Y2J4; P46439: GSTM5; NbExp=4; IntAct=EBI-746752, EBI-4312072;
CC       Q9Y2J4; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-746752, EBI-8472129;
CC       Q9Y2J4; P04264: KRT1; NbExp=3; IntAct=EBI-746752, EBI-298429;
CC       Q9Y2J4; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-746752, EBI-739909;
CC       Q9Y2J4; Q03252: LMNB2; NbExp=3; IntAct=EBI-746752, EBI-2830427;
CC       Q9Y2J4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-746752, EBI-11742507;
CC       Q9Y2J4; Q96A72: MAGOHB; NbExp=4; IntAct=EBI-746752, EBI-746778;
CC       Q9Y2J4; P55081: MFAP1; NbExp=3; IntAct=EBI-746752, EBI-1048159;
CC       Q9Y2J4; Q15014: MORF4L2; NbExp=3; IntAct=EBI-746752, EBI-399257;
CC       Q9Y2J4; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-746752, EBI-14093244;
CC       Q9Y2J4; O14777: NDC80; NbExp=3; IntAct=EBI-746752, EBI-715849;
CC       Q9Y2J4; P35240-4: NF2; NbExp=3; IntAct=EBI-746752, EBI-1014514;
CC       Q9Y2J4; Q16649: NFIL3; NbExp=4; IntAct=EBI-746752, EBI-3951858;
CC       Q9Y2J4; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-746752, EBI-744782;
CC       Q9Y2J4; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746752, EBI-14066006;
CC       Q9Y2J4; P54646: PRKAA2; NbExp=3; IntAct=EBI-746752, EBI-1383852;
CC       Q9Y2J4; Q99633: PRPF18; NbExp=3; IntAct=EBI-746752, EBI-2798416;
CC       Q9Y2J4; P17980: PSMC3; NbExp=5; IntAct=EBI-746752, EBI-359720;
CC       Q9Y2J4; O75771: RAD51D; NbExp=8; IntAct=EBI-746752, EBI-1055693;
CC       Q9Y2J4; Q15311: RALBP1; NbExp=3; IntAct=EBI-746752, EBI-749285;
CC       Q9Y2J4; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-746752, EBI-3437896;
CC       Q9Y2J4; Q5VTR2: RNF20; NbExp=4; IntAct=EBI-746752, EBI-2372238;
CC       Q9Y2J4; O75150: RNF40; NbExp=3; IntAct=EBI-746752, EBI-744408;
CC       Q9Y2J4; O76064: RNF8; NbExp=3; IntAct=EBI-746752, EBI-373337;
CC       Q9Y2J4; Q8TEC5: SH3RF2; NbExp=4; IntAct=EBI-746752, EBI-2130111;
CC       Q9Y2J4; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-746752, EBI-455078;
CC       Q9Y2J4; O94964-4: SOGA1; NbExp=3; IntAct=EBI-746752, EBI-14083835;
CC       Q9Y2J4; Q15560: TCEA2; NbExp=3; IntAct=EBI-746752, EBI-710310;
CC       Q9Y2J4; P10827: THRA; NbExp=3; IntAct=EBI-746752, EBI-286285;
CC       Q9Y2J4; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-746752, EBI-10241197;
CC       Q9Y2J4; P07947: YES1; NbExp=3; IntAct=EBI-746752, EBI-515331;
CC       Q9Y2J4; Q05516: ZBTB16; NbExp=3; IntAct=EBI-746752, EBI-711925;
CC       Q9Y2J4; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-746752, EBI-16428984;
CC       Q9Y2J4; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-746752, EBI-10183064;
CC       Q9Y2J4-4; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-10187270, EBI-2548012;
CC       Q9Y2J4-4; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-10187270, EBI-5666615;
CC       Q9Y2J4-4; Q9H257: CARD9; NbExp=5; IntAct=EBI-10187270, EBI-751319;
CC       Q9Y2J4-4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-10187270, EBI-10175300;
CC       Q9Y2J4-4; Q01850: CDR2; NbExp=3; IntAct=EBI-10187270, EBI-1181367;
CC       Q9Y2J4-4; Q8WWE8: CYTH4; NbExp=3; IntAct=EBI-10187270, EBI-10277443;
CC       Q9Y2J4-4; P35638-2: DDIT3; NbExp=3; IntAct=EBI-10187270, EBI-10173632;
CC       Q9Y2J4-4; P63167: DYNLL1; NbExp=3; IntAct=EBI-10187270, EBI-349105;
CC       Q9Y2J4-4; O60573: EIF4E2; NbExp=3; IntAct=EBI-10187270, EBI-398610;
CC       Q9Y2J4-4; Q6P9G8: FAM184A; NbExp=3; IntAct=EBI-10187270, EBI-10253239;
CC       Q9Y2J4-4; P63218: GNG5; NbExp=3; IntAct=EBI-10187270, EBI-10220734;
CC       Q9Y2J4-4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10187270, EBI-618309;
CC       Q9Y2J4-4; P46439: GSTM5; NbExp=3; IntAct=EBI-10187270, EBI-4312072;
CC       Q9Y2J4-4; A1A4E9: KRT13; NbExp=3; IntAct=EBI-10187270, EBI-10171552;
CC       Q9Y2J4-4; P19012: KRT15; NbExp=3; IntAct=EBI-10187270, EBI-739566;
CC       Q9Y2J4-4; P08727: KRT19; NbExp=3; IntAct=EBI-10187270, EBI-742756;
CC       Q9Y2J4-4; P35900: KRT20; NbExp=3; IntAct=EBI-10187270, EBI-742094;
CC       Q9Y2J4-4; Q15323: KRT31; NbExp=3; IntAct=EBI-10187270, EBI-948001;
CC       Q9Y2J4-4; O76015: KRT38; NbExp=3; IntAct=EBI-10187270, EBI-1047263;
CC       Q9Y2J4-4; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10187270, EBI-10172150;
CC       Q9Y2J4-4; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-10187270, EBI-10172511;
CC       Q9Y2J4-4; P61968: LMO4; NbExp=3; IntAct=EBI-10187270, EBI-2798728;
CC       Q9Y2J4-4; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-10187270, EBI-10194128;
CC       Q9Y2J4-4; P55081: MFAP1; NbExp=3; IntAct=EBI-10187270, EBI-1048159;
CC       Q9Y2J4-4; Q9Y217: MTMR6; NbExp=3; IntAct=EBI-10187270, EBI-766064;
CC       Q9Y2J4-4; Q9ULV0: MYO5B; NbExp=3; IntAct=EBI-10187270, EBI-311356;
CC       Q9Y2J4-4; Q16649: NFIL3; NbExp=3; IntAct=EBI-10187270, EBI-3951858;
CC       Q9Y2J4-4; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10187270, EBI-741158;
CC       Q9Y2J4-4; P17980: PSMC3; NbExp=5; IntAct=EBI-10187270, EBI-359720;
CC       Q9Y2J4-4; O75771: RAD51D; NbExp=3; IntAct=EBI-10187270, EBI-1055693;
CC       Q9Y2J4-4; Q15311: RALBP1; NbExp=3; IntAct=EBI-10187270, EBI-749285;
CC       Q9Y2J4-4; Q8WWW0: RASSF5; NbExp=3; IntAct=EBI-10187270, EBI-367390;
CC       Q9Y2J4-4; Q5VTR2: RNF20; NbExp=3; IntAct=EBI-10187270, EBI-2372238;
CC       Q9Y2J4-4; O75150: RNF40; NbExp=3; IntAct=EBI-10187270, EBI-744408;
CC       Q9Y2J4-4; Q08AM8: SH3RF2; NbExp=3; IntAct=EBI-10187270, EBI-10225873;
CC       Q9Y2J4-4; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-10187270, EBI-455078;
CC       Q9Y2J4-4; P23497: SP100; NbExp=3; IntAct=EBI-10187270, EBI-751145;
CC       Q9Y2J4-4; Q96R06: SPAG5; NbExp=3; IntAct=EBI-10187270, EBI-413317;
CC       Q9Y2J4-4; P10827: THRA; NbExp=3; IntAct=EBI-10187270, EBI-286285;
CC       Q9Y2J4-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-10187270, EBI-355744;
CC       Q9Y2J4-4; P14373: TRIM27; NbExp=3; IntAct=EBI-10187270, EBI-719493;
CC       Q9Y2J4-4; O96006: ZBED1; NbExp=3; IntAct=EBI-10187270, EBI-740037;
CC       Q9Y2J4-4; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-10187270, EBI-3439227;
CC       Q9Y2J4-4; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-10187270, EBI-10183064;
CC   -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9Y2J4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2J4-2; Sequence=VSP_015711;
CC       Name=3;
CC         IsoId=Q9Y2J4-3; Sequence=VSP_037826;
CC       Name=4;
CC         IsoId=Q9Y2J4-4; Sequence=VSP_044081;
CC   -!- PTM: Phosphorylation at Tyr-107 is necessary for efficient binding to
CC       SRC and synergistically functioning with SRC to activate the downstream
CC       MAPK pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA76833.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD97318.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB023206; BAA76833.1; ALT_INIT; mRNA.
DR   EMBL; AK291616; BAF84305.1; -; mRNA.
DR   EMBL; AK299270; BAH12987.1; -; mRNA.
DR   EMBL; AK223598; BAD97318.1; ALT_INIT; mRNA.
DR   EMBL; AF175966; AAD56361.2; -; mRNA.
DR   EMBL; AC010207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011454; AAH11454.1; ALT_INIT; mRNA.
DR   CCDS; CCDS33860.1; -. [Q9Y2J4-2]
DR   CCDS; CCDS63783.1; -. [Q9Y2J4-3]
DR   CCDS; CCDS63784.1; -. [Q9Y2J4-4]
DR   CCDS; CCDS87138.1; -. [Q9Y2J4-1]
DR   RefSeq; NP_001265612.1; NM_001278683.1. [Q9Y2J4-4]
DR   RefSeq; NP_001265614.1; NM_001278685.1. [Q9Y2J4-3]
DR   RefSeq; NP_057285.3; NM_016201.3. [Q9Y2J4-2]
DR   RefSeq; XP_006713717.1; XM_006713654.2. [Q9Y2J4-1]
DR   RefSeq; XP_011511183.1; XM_011512881.1.
DR   RefSeq; XP_016862069.1; XM_017006580.1. [Q9Y2J4-2]
DR   RefSeq; XP_016862070.1; XM_017006581.1. [Q9Y2J4-2]
DR   RefSeq; XP_016862071.1; XM_017006582.1. [Q9Y2J4-2]
DR   AlphaFoldDB; Q9Y2J4; -.
DR   SMR; Q9Y2J4; -.
DR   BioGRID; 119530; 154.
DR   CORUM; Q9Y2J4; -.
DR   DIP; DIP-57510N; -.
DR   IntAct; Q9Y2J4; 117.
DR   MINT; Q9Y2J4; -.
DR   STRING; 9606.ENSP00000424765; -.
DR   GlyGen; Q9Y2J4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y2J4; -.
DR   PhosphoSitePlus; Q9Y2J4; -.
DR   BioMuta; AMOTL2; -.
DR   DMDM; 308153633; -.
DR   EPD; Q9Y2J4; -.
DR   jPOST; Q9Y2J4; -.
DR   MassIVE; Q9Y2J4; -.
DR   MaxQB; Q9Y2J4; -.
DR   PaxDb; Q9Y2J4; -.
DR   PeptideAtlas; Q9Y2J4; -.
DR   PRIDE; Q9Y2J4; -.
DR   ProteomicsDB; 20614; -.
DR   ProteomicsDB; 85814; -. [Q9Y2J4-1]
DR   ProteomicsDB; 85815; -. [Q9Y2J4-2]
DR   ProteomicsDB; 85816; -. [Q9Y2J4-3]
DR   Antibodypedia; 33394; 108 antibodies from 22 providers.
DR   DNASU; 51421; -.
DR   Ensembl; ENST00000249883.10; ENSP00000249883.5; ENSG00000114019.15. [Q9Y2J4-2]
DR   Ensembl; ENST00000422605.6; ENSP00000409999.2; ENSG00000114019.15. [Q9Y2J4-1]
DR   Ensembl; ENST00000513145.1; ENSP00000425475.1; ENSG00000114019.15. [Q9Y2J4-3]
DR   Ensembl; ENST00000514516.5; ENSP00000424765.1; ENSG00000114019.15. [Q9Y2J4-4]
DR   GeneID; 51421; -.
DR   KEGG; hsa:51421; -.
DR   MANE-Select; ENST00000249883.10; ENSP00000249883.5; NM_016201.4; NP_057285.3. [Q9Y2J4-2]
DR   UCSC; uc003eqf.4; human. [Q9Y2J4-1]
DR   CTD; 51421; -.
DR   DisGeNET; 51421; -.
DR   GeneCards; AMOTL2; -.
DR   HGNC; HGNC:17812; AMOTL2.
DR   HPA; ENSG00000114019; Low tissue specificity.
DR   MIM; 614658; gene.
DR   neXtProt; NX_Q9Y2J4; -.
DR   OpenTargets; ENSG00000114019; -.
DR   PharmGKB; PA24775; -.
DR   VEuPathDB; HostDB:ENSG00000114019; -.
DR   eggNOG; ENOG502QR7W; Eukaryota.
DR   GeneTree; ENSGT00940000156577; -.
DR   HOGENOM; CLU_009937_2_0_1; -.
DR   InParanoid; Q9Y2J4; -.
DR   OMA; YRFYQPQ; -.
DR   OrthoDB; 369983at2759; -.
DR   PhylomeDB; Q9Y2J4; -.
DR   TreeFam; TF333368; -.
DR   PathwayCommons; Q9Y2J4; -.
DR   Reactome; R-HSA-2028269; Signaling by Hippo.
DR   SignaLink; Q9Y2J4; -.
DR   BioGRID-ORCS; 51421; 26 hits in 1080 CRISPR screens.
DR   ChiTaRS; AMOTL2; human.
DR   GeneWiki; AMOTL2; -.
DR   GenomeRNAi; 51421; -.
DR   Pharos; Q9Y2J4; Tbio.
DR   PRO; PR:Q9Y2J4; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9Y2J4; protein.
DR   Bgee; ENSG00000114019; Expressed in amniotic fluid and 202 other tissues.
DR   ExpressionAtlas; Q9Y2J4; baseline and differential.
DR   Genevisible; Q9Y2J4; HS.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR   GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IBA:GO_Central.
DR   GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR009114; Angiomotin.
DR   InterPro; IPR024646; Angiomotin_C.
DR   Pfam; PF12240; Angiomotin_C; 1.
DR   PRINTS; PR01807; ANGIOMOTIN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Endosome; Phosphoprotein;
KW   Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..779
FT                   /note="Angiomotin-like protein 2"
FT                   /id="PRO_0000190672"
FT   REGION          41..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          308..581
FT                   /evidence="ECO:0000255"
FT   MOTIF           776..779
FT                   /note="PDZ-binding"
FT   COMPBIAS        61..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         107
FT                   /note="Phosphotyrosine; by FGFR1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         759
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         762
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K371"
FT   VAR_SEQ         1
FT                   /note="M -> MTGRKASGGTPCTLRKGAPIITLGKNWTERLAAGDSVGCSGARCHRP
FT                   LSRQLCASQRSM (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044081"
FT   VAR_SEQ         525..526
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_037826"
FT   VAR_SEQ         701
FT                   /note="T -> TA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10231032,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015711"
FT   VARIANT         227
FT                   /note="T -> I (in dbSNP:rs35377537)"
FT                   /id="VAR_055497"
FT   VARIANT         342
FT                   /note="A -> P (in dbSNP:rs2303635)"
FT                   /id="VAR_055498"
FT   VARIANT         415
FT                   /note="G -> S (in dbSNP:rs2241559)"
FT                   /id="VAR_055499"
FT   VARIANT         731
FT                   /note="E -> D (in dbSNP:rs1353776)"
FT                   /evidence="ECO:0000269|PubMed:10231032,
FT                   ECO:0000269|PubMed:12406577, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_023535"
FT   CONFLICT        666
FT                   /note="K -> E (in Ref. 2; BAH12987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        680
FT                   /note="Q -> K (in Ref. 4; AAD56361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   779 AA;  85764 MW;  665BE69FD7757CEF CRC64;
     MRTLEDSSGT VLHRLIQEQL RYGNLTETRT LLAIQQQALR GGAGTGGTGS PQASLEILAP
     EDSQVLQQAT RQEPQGQEHQ GGENHLAENT LYRLCPQPSK GEELPTYEEA KAHSQYYAAQ
     QAGTRPHAGD RDPRGAPGGS RRQDEALREL RHGHVRSLSE RLLQLSLERN GARAPSHMSS
     SHSFPQLARN QQGPPLRGPP AEGPESRGPP PQYPHVVLAH ETTTAVTDPR YRARGSPHFQ
     HAEVRILQAQ VPPVFLQQQQ QYQYLQQSQE HPPPPHPAAL GHGPLSSLSP PAVEGPVSAQ
     ASSATSGSAH LAQMEAVLRE NARLQRDNER LQRELESSAE KAGRIEKLES EIQRLSEAHE
     SLTRASSKRE ALEKTMRNKM DSEMRRLQDF NRDLRERLES ANRRLASKTQ EAQAGSQDMV
     AKLLAQSYEQ QQEQEKLERE MALLRGAIED QRRRAELLEQ ALGNAQGRAA RAEEELRKKQ
     AYVEKVERLQ QALGQLQAAC EKREQLELRL RTRLEQELKA LRAQQRQAGA PGGSSGSGGS
     PELSALRLSE QLREKEEQIL ALEADMTKWE QKYLEERAMR QFAMDAAATA AAQRDTTLIR
     HSPQPSPSSS FNEGLLTGGH RHQEMESRLK VLHAQILEKD AVIKVLQQRS RRDPGKAIQG
     SLRPAKSVPS VFAAAAAGTQ GWQGLSSSER QTADAPARLT TDRAPTEEPV VTAPPAAHAK
     HGSRDGSTQT EGPPDSTSTC LPPEPDSLLG CSSSQRAASL DSVATSRVQD LSDMVEILI
 
 
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