(data stored in ACNUC6163 zone)

HOVERGEN: AT11C_HUMAN

ID   AT11C_HUMAN             Reviewed;        1132 AA.
AC   Q8NB49; Q5JT69; Q5JT70; Q5JT71; Q5JT72; Q5JT73; Q6ZND5; Q6ZU50;
AC   Q6ZUP7; Q70IJ9; Q70IK0; Q8WX24;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 3.
DT   03-NOV-2009, entry version 74.
DE   RecName: Full=Probable phospholipid-transporting ATPase IG;
DE            EC=3.6.3.1;
DE   AltName: Full=ATPase class VI type 11C;
DE   AltName: Full=ATPase IG;
DE   AltName: Full=ATPase IQ;
GN   Name=ATP11C; Synonyms=ATPIG, ATPIQ;
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP   VARIANT TRP-114.
RC   TISSUE=Liver;
RX   PubMed=15533723; DOI=10.1016/j.ygeno.2004.08.003;
RA   Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P.,
RA   Thakker R.V.;
RT   "X-linked hypoparathyroidism region on Xq27 is evolutionarily
RT   conserved with regions on 3q26 and 13q34 and contains a novel P-type
RT   ATPase.";
RL   Genomics 84:1060-1070(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1132 (ISOFORM 4),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-1132 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1132 (ISOFORM 2).
RC   TISSUE=Brain, Fetal brain, Testis, and Thalamus;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-261, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18187866; DOI=10.2116/analsci.24.161;
RA   Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
RT   "Automated phosphoproteome analysis for cultured cancer cells by two-
RT   dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
RL   Anal. Sci. 24:161-166(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP   SPECTROMETRY.
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   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8NB49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NB49-2; Sequence=VSP_007309;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8NB49-3; Sequence=VSP_013373;
CC       Name=4;
CC         IsoId=Q8NB49-4; Sequence=VSP_013374;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family. Type IV subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI39713.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI39714.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI39716.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI40418.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI41444.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI41445.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI41446.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI41447.1; Type=Erroneous gene model prediction;
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CC   -!- GENE_FAMILY: HBG050601 [ FAMILY / ALN / TREE ]
DR   EMBL; AJ580093; CAE30472.1; -; mRNA.
DR   EMBL; AJ580094; CAE30473.1; -; mRNA.
DR   EMBL; AL161777; CAI39713.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356785; CAI39713.1; JOINED; Genomic_DNA.
DR   EMBL; AL161777; CAI39714.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356785; CAI39714.1; JOINED; Genomic_DNA.
DR   EMBL; AL161777; CAI39716.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356785; CAI39716.1; JOINED; Genomic_DNA.
DR   EMBL; AL590077; CAI39716.1; JOINED; Genomic_DNA.
DR   EMBL; AL356785; CAI41444.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161777; CAI41444.1; JOINED; Genomic_DNA.
DR   EMBL; AL356785; CAI41445.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161777; CAI41445.1; JOINED; Genomic_DNA.
DR   EMBL; AL356785; CAI41446.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161777; CAI41446.1; JOINED; Genomic_DNA.
DR   EMBL; AL590077; CAI41446.1; JOINED; Genomic_DNA.
DR   EMBL; AL356785; CAI41447.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL590077; CAI40418.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL356785; CAI40418.1; JOINED; Genomic_DNA.
DR   EMBL; AL161777; CAI40418.1; JOINED; Genomic_DNA.
DR   EMBL; AK091552; BAC03692.1; ALT_INIT; mRNA.
DR   EMBL; AK125474; BAC86172.1; ALT_INIT; mRNA.
DR   EMBL; AK125986; BAC86377.1; ALT_INIT; mRNA.
DR   EMBL; AK131262; BAD18440.1; ALT_INIT; mRNA.
DR   IPI; IPI00237446; -.
DR   IPI; IPI00396234; -.
DR   IPI; IPI00552319; -.
DR   IPI; IPI00555989; -.
DR   RefSeq; NP_001010986.1; -.
DR   RefSeq; NP_775965.2; -.
DR   UniGene; Hs.88252; -.
DR   STRING; Q8NB49; -.
DR   PhosphoSite; Q8NB49; -.
DR   PRIDE; Q8NB49; -.
DR   Ensembl; ENST00000327569; ENSP00000332756; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000359686; ENSP00000352715; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000361648; ENSP00000355165; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000370543; ENSP00000359574; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000370557; ENSP00000359588; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000422228; ENSP00000394573; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000433868; ENSP00000397923; ENSG00000101974; Homo sapiens.
DR   Ensembl; ENST00000450801; ENSP00000391259; ENSG00000101974; Homo sapiens.
DR   GeneID; 286410; -.
DR   KEGG; hsa:286410; -.
DR   UCSC; uc004faz.1; human.
DR   UCSC; uc004fba.1; human.
DR   CTD; 286410; -.
DR   GeneCards; GC0XM138636; -.
DR   HGNC; HGNC:13554; ATP11C.
DR   MIM; 300516; gene.
DR   PharmGKB; PA25103; -.
DR   HOVERGEN; Q8NB49; -.
DR   OMA; ECCIDGH; -.
DR   BRENDA; 3.6.3.1; 247.
DR   NextBio; 96190; -.
DR   ArrayExpress; Q8NB49; -.
DR   Bgee; Q8NB49; -.
DR   Genevestigator; Q8NB49; -.
DR   GermOnline; ENSG00000101974; Homo sapiens.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane m...; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-reg.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   PANTHER; PTHR11939; ATPase_P; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q6ZUP7.
DR   SWISS-2DPAGE; Q6ZUP7.
KW   Alternative splicing; ATP-binding; Complete proteome; Hydrolase;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Transmembrane.
FT   DOMAIN       46     77       PRODOM:2005.1:PD584476  133
FT   DOMAIN       80    164       PRODOM:2005.1:PD583714  159
FT   DOMAIN      165    215       PRODOM:2005.1:PD111436  109
FT   DOMAIN      221    272       PRODOM:2005.1:PD004982  138
FT   DOMAIN      273    363       PRODOM:2005.1:PD006317  109
FT   DOMAIN      396    434       PRODOM:2005.1:PD864285  143
FT   DOMAIN      465    528       PRODOM:2005.1:PD003346  121
FT   DOMAIN      550    593       PRODOM:2005.1:PD461286  88
FT   DOMAIN      594    640       PRODOM:2005.1:PD250570  129
FT   DOMAIN      642    673       PRODOM:2005.1:PD336512  128
FT   DOMAIN      674    714       PRODOM:2005.1:PD030421  130
FT   DOMAIN      750    792       PRODOM:2005.1:PD004657  92
FT   DOMAIN      813    850       PRODOM:2005.1:PD005736  137
FT   DOMAIN      851    892       PRODOM:2005.1:PD435496  137
FT   DOMAIN      893    993       PRODOM:2005.1:PD304524  143
FT   DOMAIN      994   1055       PRODOM:2005.1:PDA1E1E9  67
FT   DOMAIN     1056   1090       PRODOM:2005.1:PD412927  11
FT   DOMAIN     1091   1132       PRODOM:2005.1:PD898636  2
FT   CHAIN         1   1132       Probable phospholipid-transporting ATPase
FT                                IG.
FT                                /FTId=PRO_0000046373.
FT   TOPO_DOM      1     66       Cytoplasmic (Potential).
FT   TRANSMEM     67     85       Potential.
FT   TOPO_DOM     86     86       Extracellular (Potential).
FT   TRANSMEM     87    107       Potential.
FT   TOPO_DOM    108    290       Cytoplasmic (Potential).
FT   TRANSMEM    291    311       Potential.
FT   TOPO_DOM    312    346       Extracellular (Potential).
FT   TRANSMEM    347    367       Potential.
FT   TOPO_DOM    368    879       Cytoplasmic (Potential).
FT   TRANSMEM    880    900       Potential.
FT   TOPO_DOM    901    908       Extracellular (Potential).
FT   TRANSMEM    909    929       Potential.
FT   TOPO_DOM    930    955       Cytoplasmic (Potential).
FT   TRANSMEM    956    976       Potential.
FT   TOPO_DOM    977    995       Extracellular (Potential).
FT   TRANSMEM    996   1016       Potential.
FT   TOPO_DOM   1017   1026       Cytoplasmic (Potential).
FT   TRANSMEM   1027   1047       Potential.
FT   TOPO_DOM   1048   1069       Extracellular (Potential).
FT   TRANSMEM   1070   1090       Potential.
FT   TOPO_DOM   1091   1132       Cytoplasmic (Potential).
FT   ACT_SITE    412    412       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       819    819       Magnesium (By similarity).
FT   METAL       823    823       Magnesium (By similarity).
FT   MOD_RES     261    261       Phosphotyrosine.
FT   MOD_RES     445    445       Phosphoserine.
FT   MOD_RES    1108   1108       Phosphoserine (By similarity).
FT   VAR_SEQ    1100   1132       RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VHHL
FT                                ISSSA (in isoform 2).
FT                                /FTId=VSP_007309.
FT   VAR_SEQ    1100   1132       RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> NPNL
FT                                ELPMLLSYKHTDSGYS (in isoform 3).
FT                                /FTId=VSP_013373.
FT   VAR_SEQ    1100   1132       RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VTKR
FT                                LPSSGTSAIFMLSQTSSNHSFSWSE (in isoform 4).
FT                                /FTId=VSP_013374.
FT   VARIANT     114    114       C -> W (in dbSNP:rs2491014).
FT                                /FTId=VAR_021827.
FT   VARIANT     157    157       T -> I (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036501.
FT   VARIANT     522    522       Y -> C (in dbSNP:rs17281983).
FT                                /FTId=VAR_055546.
FT   VARIANT     931    931       Q -> P (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036502.
FT   CONFLICT    537    537       L -> P (in Ref. 3; BAC86377).
FT   CONFLICT    873    873       I -> V (in Ref. 3; BAC86377).
SQ   SEQUENCE   1132 AA;  129477 MW;  74B63B20A5C6E49D CRC64;
     MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP
     KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD
     NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS
     LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR
     SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF
     ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV
     SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN
     SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN
     DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT
     LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC
     VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA
     ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE
     LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ
     ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE
     GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF
     SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL
     YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF
     WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS
     LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL
//

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