Full text data of METAP1
METAP1
(KIAA0094)
[Confidence: low (only semi-automatic identification from reviews)]
Methionine aminopeptidase 1; MAP 1; MetAP 1; 3.4.11.18 (Peptidase M 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Methionine aminopeptidase 1; MAP 1; MetAP 1; 3.4.11.18 (Peptidase M 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53582
ID MAP11_HUMAN Reviewed; 386 AA.
AC P53582; B4E2E6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JUL-2003, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Methionine aminopeptidase 1;
DE Short=MAP 1;
DE Short=MetAP 1;
DE EC=3.4.11.18;
DE AltName: Full=Peptidase M 1;
GN Name=METAP1; Synonyms=KIAA0094;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-386.
RC TISSUE=Placenta;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS, FUNCTION, AND COFACTOR.
RX PubMed=16274222; DOI=10.1021/bi051691k;
RA Addlagatta A., Hu X., Liu J.O., Matthews B.W.;
RT "Structural basis for the functional differences between type I and
RT type II human methionine aminopeptidases.";
RL Biochemistry 44:14741-14749(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND INHIBITORS.
RX PubMed=16724298; DOI=10.1002/anie.200600757;
RA Hu X., Addlagatta A., Matthews B.W., Liu J.O.;
RT "Identification of pyridinylpyrimidines as inhibitors of human
RT methionine aminopeptidases.";
RL Angew. Chem. Int. Ed. 45:3772-3775(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND INHIBITORS, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17114291; DOI=10.1073/pnas.0608389103;
RA Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O.;
RT "Elucidation of the function of type 1 human methionine aminopeptidase
RT during cell cycle progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND THE INHIBITOR OVALICIN.
RX PubMed=16823043; DOI=10.1110/ps.062278006;
RA Addlagatta A., Matthews B.W.;
RT "Structure of the angiogenesis inhibitor ovalicin bound to its
RT noncognate target, human Type 1 methionine aminopeptidase.";
RL Protein Sci. 15:1842-1848(2006).
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when
CC the second residue in the primary sequence is small and uncharged
CC (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal
CC progression through the cell cycle.
CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC preferentially methionine, from peptides and arylamides.
CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. Has a high-
CC affinity and a low affinity metal-binding site. The true nature of
CC the physiological cofactor is under debate. The enzyme is active
CC with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC methionine aminopeptidases function as mononuclear Fe(2+)-
CC metalloproteases under physiological conditions, and the
CC catalytically relevant metal-binding site has been assigned to the
CC histidine-containing high-affinity site (By similarity).
CC -!- COFACTOR: Binds 1 sodium ion per subunit. The sodium ion has a
CC structural role.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S
CC translational complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30054.1; Type=Erroneous initiation;
CC Sequence=BAA07679.1; Type=Erroneous initiation;
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; D42084; BAA07679.1; ALT_INIT; mRNA.
DR EMBL; AK304239; BAG65108.1; -; mRNA.
DR EMBL; CH471057; EAX06083.1; -; Genomic_DNA.
DR EMBL; BC030054; AAH30054.1; ALT_INIT; mRNA.
DR RefSeq; NP_055958.2; NM_015143.2.
DR UniGene; Hs.480364; -.
DR PDB; 2B3H; X-ray; 1.10 A; A=81-384.
DR PDB; 2B3K; X-ray; 1.55 A; A=81-384.
DR PDB; 2B3L; X-ray; 1.50 A; A=81-384.
DR PDB; 2G6P; X-ray; 1.90 A; A=81-384.
DR PDB; 2GZ5; X-ray; 1.10 A; A=81-384.
DR PDB; 2NQ6; X-ray; 1.50 A; A=81-384.
DR PDB; 2NQ7; X-ray; 1.60 A; A=81-384.
DR PDB; 4FLI; X-ray; 1.55 A; A=81-386.
DR PDB; 4FLJ; X-ray; 1.74 A; A=81-386.
DR PDB; 4FLK; X-ray; 1.47 A; A=81-386.
DR PDB; 4FLL; X-ray; 1.50 A; A=81-386.
DR PDB; 4HXX; X-ray; 2.09 A; A=81-384.
DR PDB; 4IU6; X-ray; 1.90 A; A=1-384.
DR PDBsum; 2B3H; -.
DR PDBsum; 2B3K; -.
DR PDBsum; 2B3L; -.
DR PDBsum; 2G6P; -.
DR PDBsum; 2GZ5; -.
DR PDBsum; 2NQ6; -.
DR PDBsum; 2NQ7; -.
DR PDBsum; 4FLI; -.
DR PDBsum; 4FLJ; -.
DR PDBsum; 4FLK; -.
DR PDBsum; 4FLL; -.
DR PDBsum; 4HXX; -.
DR PDBsum; 4IU6; -.
DR ProteinModelPortal; P53582; -.
DR SMR; P53582; 81-384.
DR IntAct; P53582; 1.
DR MINT; MINT-1191219; -.
DR STRING; 9606.ENSP00000296411; -.
DR BindingDB; P53582; -.
DR ChEMBL; CHEMBL2474; -.
DR MEROPS; M24.017; -.
DR PhosphoSite; P53582; -.
DR DMDM; 33302602; -.
DR PaxDb; P53582; -.
DR PeptideAtlas; P53582; -.
DR PRIDE; P53582; -.
DR Ensembl; ENST00000296411; ENSP00000296411; ENSG00000164024.
DR GeneID; 23173; -.
DR KEGG; hsa:23173; -.
DR UCSC; uc003huf.4; human.
DR CTD; 23173; -.
DR GeneCards; GC04P099916; -.
DR HGNC; HGNC:15789; METAP1.
DR HPA; CAB025485; -.
DR MIM; 610151; gene.
DR neXtProt; NX_P53582; -.
DR PharmGKB; PA30764; -.
DR eggNOG; COG0024; -.
DR HOGENOM; HOG000030427; -.
DR HOVERGEN; HBG067178; -.
DR InParanoid; P53582; -.
DR KO; K01265; -.
DR OMA; ECFKRNW; -.
DR OrthoDB; EOG786H38; -.
DR PhylomeDB; P53582; -.
DR BRENDA; 3.4.11.18; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; P53582; -.
DR EvolutionaryTrace; P53582; -.
DR GeneWiki; METAP1; -.
DR GenomeRNAi; 23173; -.
DR NextBio; 44587; -.
DR PRO; PR:P53582; -.
DR ArrayExpress; P53582; -.
DR Bgee; P53582; -.
DR CleanEx; HS_METAP1; -.
DR Genevestigator; P53582; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; TAS:UniProtKB.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:HGNC.
DR GO; GO:0018206; P:peptidyl-methionine modification; TAS:HGNC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006417; P:regulation of translation; TAS:HGNC.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1; -.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR000994; Pept_M24_structural-domain.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 386 Methionine aminopeptidase 1.
FT /FTId=PRO_0000148967.
FT REGION 9 52 Zinc finger-like; important for proper
FT ribosome association (By similarity).
FT METAL 220 220 Divalent metal cation 1.
FT METAL 231 231 Divalent metal cation 1.
FT METAL 231 231 Divalent metal cation 2; catalytic.
FT METAL 294 294 Divalent metal cation 2; catalytic; via
FT tele nitrogen.
FT METAL 327 327 Divalent metal cation 2; catalytic.
FT METAL 358 358 Divalent metal cation 1.
FT METAL 358 358 Divalent metal cation 2; catalytic.
FT BINDING 203 203 Substrate.
FT BINDING 301 301 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT STRAND 84 86
FT HELIX 107 110
FT HELIX 117 121
FT TURN 122 124
FT HELIX 133 155
FT HELIX 163 176
FT TURN 182 185
FT HELIX 186 188
FT STRAND 191 197
FT STRAND 200 202
FT STRAND 216 225
FT STRAND 228 237
FT HELIX 243 261
FT HELIX 271 282
FT STRAND 293 295
FT STRAND 297 306
FT STRAND 309 311
FT STRAND 323 326
FT STRAND 329 333
FT STRAND 337 339
FT STRAND 346 348
FT STRAND 354 356
FT STRAND 358 363
FT STRAND 365 370
FT HELIX 381 383
SQ SEQUENCE 386 AA; 43215 MW; 372879013C2BB01D CRC64;
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT
LLVTDTGCEI LTRRLDSARP HFMSQF
//
ID MAP11_HUMAN Reviewed; 386 AA.
AC P53582; B4E2E6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JUL-2003, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Methionine aminopeptidase 1;
DE Short=MAP 1;
DE Short=MetAP 1;
DE EC=3.4.11.18;
DE AltName: Full=Peptidase M 1;
GN Name=METAP1; Synonyms=KIAA0094;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-386.
RC TISSUE=Placenta;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS, FUNCTION, AND COFACTOR.
RX PubMed=16274222; DOI=10.1021/bi051691k;
RA Addlagatta A., Hu X., Liu J.O., Matthews B.W.;
RT "Structural basis for the functional differences between type I and
RT type II human methionine aminopeptidases.";
RL Biochemistry 44:14741-14749(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND INHIBITORS.
RX PubMed=16724298; DOI=10.1002/anie.200600757;
RA Hu X., Addlagatta A., Matthews B.W., Liu J.O.;
RT "Identification of pyridinylpyrimidines as inhibitors of human
RT methionine aminopeptidases.";
RL Angew. Chem. Int. Ed. 45:3772-3775(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND INHIBITORS, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17114291; DOI=10.1073/pnas.0608389103;
RA Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O.;
RT "Elucidation of the function of type 1 human methionine aminopeptidase
RT during cell cycle progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS AND THE INHIBITOR OVALICIN.
RX PubMed=16823043; DOI=10.1110/ps.062278006;
RA Addlagatta A., Matthews B.W.;
RT "Structure of the angiogenesis inhibitor ovalicin bound to its
RT noncognate target, human Type 1 methionine aminopeptidase.";
RL Protein Sci. 15:1842-1848(2006).
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when
CC the second residue in the primary sequence is small and uncharged
CC (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal
CC progression through the cell cycle.
CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC preferentially methionine, from peptides and arylamides.
CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. Has a high-
CC affinity and a low affinity metal-binding site. The true nature of
CC the physiological cofactor is under debate. The enzyme is active
CC with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC methionine aminopeptidases function as mononuclear Fe(2+)-
CC metalloproteases under physiological conditions, and the
CC catalytically relevant metal-binding site has been assigned to the
CC histidine-containing high-affinity site (By similarity).
CC -!- COFACTOR: Binds 1 sodium ion per subunit. The sodium ion has a
CC structural role.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S
CC translational complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30054.1; Type=Erroneous initiation;
CC Sequence=BAA07679.1; Type=Erroneous initiation;
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; D42084; BAA07679.1; ALT_INIT; mRNA.
DR EMBL; AK304239; BAG65108.1; -; mRNA.
DR EMBL; CH471057; EAX06083.1; -; Genomic_DNA.
DR EMBL; BC030054; AAH30054.1; ALT_INIT; mRNA.
DR RefSeq; NP_055958.2; NM_015143.2.
DR UniGene; Hs.480364; -.
DR PDB; 2B3H; X-ray; 1.10 A; A=81-384.
DR PDB; 2B3K; X-ray; 1.55 A; A=81-384.
DR PDB; 2B3L; X-ray; 1.50 A; A=81-384.
DR PDB; 2G6P; X-ray; 1.90 A; A=81-384.
DR PDB; 2GZ5; X-ray; 1.10 A; A=81-384.
DR PDB; 2NQ6; X-ray; 1.50 A; A=81-384.
DR PDB; 2NQ7; X-ray; 1.60 A; A=81-384.
DR PDB; 4FLI; X-ray; 1.55 A; A=81-386.
DR PDB; 4FLJ; X-ray; 1.74 A; A=81-386.
DR PDB; 4FLK; X-ray; 1.47 A; A=81-386.
DR PDB; 4FLL; X-ray; 1.50 A; A=81-386.
DR PDB; 4HXX; X-ray; 2.09 A; A=81-384.
DR PDB; 4IU6; X-ray; 1.90 A; A=1-384.
DR PDBsum; 2B3H; -.
DR PDBsum; 2B3K; -.
DR PDBsum; 2B3L; -.
DR PDBsum; 2G6P; -.
DR PDBsum; 2GZ5; -.
DR PDBsum; 2NQ6; -.
DR PDBsum; 2NQ7; -.
DR PDBsum; 4FLI; -.
DR PDBsum; 4FLJ; -.
DR PDBsum; 4FLK; -.
DR PDBsum; 4FLL; -.
DR PDBsum; 4HXX; -.
DR PDBsum; 4IU6; -.
DR ProteinModelPortal; P53582; -.
DR SMR; P53582; 81-384.
DR IntAct; P53582; 1.
DR MINT; MINT-1191219; -.
DR STRING; 9606.ENSP00000296411; -.
DR BindingDB; P53582; -.
DR ChEMBL; CHEMBL2474; -.
DR MEROPS; M24.017; -.
DR PhosphoSite; P53582; -.
DR DMDM; 33302602; -.
DR PaxDb; P53582; -.
DR PeptideAtlas; P53582; -.
DR PRIDE; P53582; -.
DR Ensembl; ENST00000296411; ENSP00000296411; ENSG00000164024.
DR GeneID; 23173; -.
DR KEGG; hsa:23173; -.
DR UCSC; uc003huf.4; human.
DR CTD; 23173; -.
DR GeneCards; GC04P099916; -.
DR HGNC; HGNC:15789; METAP1.
DR HPA; CAB025485; -.
DR MIM; 610151; gene.
DR neXtProt; NX_P53582; -.
DR PharmGKB; PA30764; -.
DR eggNOG; COG0024; -.
DR HOGENOM; HOG000030427; -.
DR HOVERGEN; HBG067178; -.
DR InParanoid; P53582; -.
DR KO; K01265; -.
DR OMA; ECFKRNW; -.
DR OrthoDB; EOG786H38; -.
DR PhylomeDB; P53582; -.
DR BRENDA; 3.4.11.18; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; P53582; -.
DR EvolutionaryTrace; P53582; -.
DR GeneWiki; METAP1; -.
DR GenomeRNAi; 23173; -.
DR NextBio; 44587; -.
DR PRO; PR:P53582; -.
DR ArrayExpress; P53582; -.
DR Bgee; P53582; -.
DR CleanEx; HS_METAP1; -.
DR Genevestigator; P53582; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; TAS:UniProtKB.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:HGNC.
DR GO; GO:0018206; P:peptidyl-methionine modification; TAS:HGNC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006417; P:regulation of translation; TAS:HGNC.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1; -.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR000994; Pept_M24_structural-domain.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 386 Methionine aminopeptidase 1.
FT /FTId=PRO_0000148967.
FT REGION 9 52 Zinc finger-like; important for proper
FT ribosome association (By similarity).
FT METAL 220 220 Divalent metal cation 1.
FT METAL 231 231 Divalent metal cation 1.
FT METAL 231 231 Divalent metal cation 2; catalytic.
FT METAL 294 294 Divalent metal cation 2; catalytic; via
FT tele nitrogen.
FT METAL 327 327 Divalent metal cation 2; catalytic.
FT METAL 358 358 Divalent metal cation 1.
FT METAL 358 358 Divalent metal cation 2; catalytic.
FT BINDING 203 203 Substrate.
FT BINDING 301 301 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT STRAND 84 86
FT HELIX 107 110
FT HELIX 117 121
FT TURN 122 124
FT HELIX 133 155
FT HELIX 163 176
FT TURN 182 185
FT HELIX 186 188
FT STRAND 191 197
FT STRAND 200 202
FT STRAND 216 225
FT STRAND 228 237
FT HELIX 243 261
FT HELIX 271 282
FT STRAND 293 295
FT STRAND 297 306
FT STRAND 309 311
FT STRAND 323 326
FT STRAND 329 333
FT STRAND 337 339
FT STRAND 346 348
FT STRAND 354 356
FT STRAND 358 363
FT STRAND 365 370
FT HELIX 381 383
SQ SEQUENCE 386 AA; 43215 MW; 372879013C2BB01D CRC64;
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT
LLVTDTGCEI LTRRLDSARP HFMSQF
//
MIM
610151
*RECORD*
*FIELD* NO
610151
*FIELD* TI
*610151 METHIONYL AMINOPEPTIDASE 1; METAP1
;;KIAA0094
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human myeloid
read moreleukemia cell line cDNA library, Nagase et al. (1995) cloned METAP1,
which they designated KIAA0094. The deduced 394-amino acid protein
shares 51.8% amino acid identity with S. cerevisiae Metap1. Northern
blot analysis detected intermediate expression of Metap1 in skeletal
muscle and low expression in all other tissues and cell lines examined.
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1995) mapped
the METAP1 gene to chromosome 4.
*FIELD* RF
1. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CD
Patricia A. Hartz: 5/30/2006
*FIELD* ED
mgross: 06/02/2006
mgross: 5/30/2006
*RECORD*
*FIELD* NO
610151
*FIELD* TI
*610151 METHIONYL AMINOPEPTIDASE 1; METAP1
;;KIAA0094
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human myeloid
read moreleukemia cell line cDNA library, Nagase et al. (1995) cloned METAP1,
which they designated KIAA0094. The deduced 394-amino acid protein
shares 51.8% amino acid identity with S. cerevisiae Metap1. Northern
blot analysis detected intermediate expression of Metap1 in skeletal
muscle and low expression in all other tissues and cell lines examined.
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1995) mapped
the METAP1 gene to chromosome 4.
*FIELD* RF
1. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CD
Patricia A. Hartz: 5/30/2006
*FIELD* ED
mgross: 06/02/2006
mgross: 5/30/2006