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MTUS1_PONAB
ID   MTUS1_PONAB             Reviewed;        1270 AA.
AC   Q5R9I1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Microtubule-associated tumor suppressor 1 homolog;
DE   AltName: Full=Mitochondrial tumor suppressor 1 homolog;
GN   Name=MTUS1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell
CC       proliferation. May be required for AGTR2 cell surface expression.
CC       Together with PTPN6, induces UBE2V2 expression upon angiotensin-II
CC       stimulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with AGTR2. Interacts with PTPN6.
CC       Associates with microtubules (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=In neurons, translocates into the nucleus after treatment with
CC       angiotensin-II. Localizes with the mitotic spindle during mitosis and
CC       with the intercellular bridge during cytokinesis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
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DR   EMBL; CR859407; CAH91579.1; -; mRNA.
DR   RefSeq; NP_001125928.1; NM_001132456.1.
DR   AlphaFoldDB; Q5R9I1; -.
DR   SMR; Q5R9I1; -.
DR   STRING; 9601.ENSPPYP00000020603; -.
DR   GeneID; 100172862; -.
DR   KEGG; pon:100172862; -.
DR   CTD; 57509; -.
DR   eggNOG; ENOG502QPVG; Eukaryota.
DR   InParanoid; Q5R9I1; -.
DR   OrthoDB; 91479at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR029786; MTUS1.
DR   PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell membrane; Coiled coil; Golgi apparatus; Membrane;
KW   Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1270
FT                   /note="Microtubule-associated tumor suppressor 1 homolog"
FT                   /id="PRO_0000305199"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          940..1231
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        19..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1241..1270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         1203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IMY1"
FT   MOD_RES         1224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         1245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         1255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT   MOD_RES         1259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IMY1"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT   MOD_RES         1264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         1268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
SQ   SEQUENCE   1270 AA;  141576 MW;  59CA71CCE6F4878F CRC64;
     MTDDNSDDKI EDELQTFFTS DKDGNTHAYN PKSPPTQKSS ASSVNWNSAN PDDMVVDYET
     DPAVVTGENI SLSLQGVEVF DHEKSSSDFT SKQVLDMHKD SICQSPALVG TEKPKYLQHS
     CHSLEAVEVQ SVEPSLPFVW KPNDNLNCTG YSDALELNQT FDMTVDKVNC TFISHHAIRK
     SQSFHTAGSL PPTGRRSGNT SSLSYSTWTS SHSDKMHARE TTYDRESFEN PQVTPSEAQD
     TTYTAFSDVV MQSEVFVSDI GNQCPCSSGK VTSEYTDGSQ QRLVGEKETQ ALTPVSDGME
     VPNDSALQEF FCLSHDESNS EPHSQSSYRH KEMGQNLRET VSYCLVDDER PLMVPAFDKS
     EAQVLNPEHK VTETEDTQMV TKGKDSGTQN HTSELILSSP PGQKVGSSFG LTWDANDMVI
     STDNTMCMST PVLEPTKVTF SVSPIEATEK CKKVEKGNRG LKNISNSKEA PVNLCKPSLG
     KSTTKTNTPI GCKVRKTEII SYPRPNFRNV KAKVMSRPVL QSKDAALSKV TPRPQLTSAS
     SPSSAISRQP TVLSRTPRSD LNADKKAEIL INKTHKQQFN KLITSQAVHV TTHSKNASHR
     VPRTTSAVKS NQEDVDKASS SNSACETGSV SALFQKIKGI LPVKMESAEC LEMTYVPNID
     RISPEKKGEK ENGTSMEKQE LKQEIMNETF EYGSLFLGSA SKTTTTSGRN ISKPDSCGLR
     QIAAPKAKVG PPVSCLRRNS DNRNPSADRA VSPQRIRRVS SSGKPTSLKT AQSSWVNLPR
     PLPKSKASLK SPALRRTGST PSIASTHSEL STYSNNSGNA TVIKYEEKPP KPAFQNGSSG
     SFYLKPLVSR AHVHLLKTPP KGPSRKNLFT ALNAVEKSRQ KNPRSLCIQT QTAPDVLPPE
     KTLELTQYKT KCENQSGFIL QLKQLLACGN TKSEALTVVI QHLLSEREEA LKQHKTLSQE
     LVNLRGELVT ASTTCEKLEE ARNELQTAYE AFVQQHQAEK TERENRLKEF YTREYEKLRD
     TYIEEAEKYK MQLQEQFDNL NAAHETSKLE IEASHSEKVE LLKKAYEASL SEIKKGHEME
     KKSLEDLLSE KQESLEKQIS DLKSENDALN EKLKSEEQKR RAREKANLKN PQIMYLEQEL
     ESLKAVLEIK NEKLHQQDIK LMKMEKLVDN NTALVDKLKR FQQENEELKA RMDKHMAISR
     QLSTEQAVLQ ESLEKESKVN KRLSMENEEL LWKLHNGDLC SPKRSPTSSA IPFQSPRNSG
     SFPSPSISPR
 
 
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