SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P50579

- MAP2_HUMAN

UniProt

P50579 - MAP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methionine aminopeptidase 2
Gene
METAP2, MNPEP, P67EIF2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.4 Publications
Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.4 Publications

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 Publication

Cofactori

Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity. Also manganese has been proposed to be the physiological cofactor for human METAP2.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311Substrate
Metal bindingi251 – 2511Divalent metal cation 1
Metal bindingi262 – 2621Divalent metal cation 1
Metal bindingi262 – 2621Divalent metal cation 2; catalytic
Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogen
Binding sitei339 – 3391Substrate
Metal bindingi364 – 3641Divalent metal cation 2; catalytic
Metal bindingi459 – 4591Divalent metal cation 1
Metal bindingi459 – 4591Divalent metal cation 2; catalytic

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-HAMAP
  3. metalloaminopeptidase activity Source: UniProtKB-HAMAP
  4. metalloexopeptidase activity Source: UniProtKB
  5. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. N-terminal protein amino acid modification Source: HGNC
  2. peptidyl-methionine modification Source: HGNC
  3. phototransduction, visible light Source: Reactome
  4. protein initiator methionine removal Source: UniProtKB-HAMAP
  5. protein processing Source: HGNC
  6. regulation of rhodopsin mediated signaling pathway Source: Reactome
  7. rhodopsin mediated signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.18. 2681.
ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Initiation factor 2-associated 67 kDa glycoprotein
Short name:
p67
Short name:
p67eIF2
Peptidase M
Gene namesi
Name:METAP2
Synonyms:MNPEP, P67EIF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16672. METAP2.

Subcellular locationi

Cytoplasm
Note: About 30% of expressed METAP2 associates with polysomes.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. cytosol Source: Reactome
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30765.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 478477Methionine aminopeptidase 2UniRule annotation
PRO_0000148982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei45 – 451Phosphoserine2 Publications
Modified residuei60 – 601Phosphoserine; alternate1 Publication
Glycosylationi60 – 601O-linked (GlcNAc); alternate By similarity
Modified residuei63 – 631Phosphoserine; alternate1 Publication
Glycosylationi63 – 631O-linked (GlcNAc); alternate By similarity
Modified residuei74 – 741Phosphoserine2 Publications

Post-translational modificationi

Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP50579.
PaxDbiP50579.
PeptideAtlasiP50579.
PRIDEiP50579.

2D gel databases

REPRODUCTION-2DPAGEIPI00033036.

PTM databases

PhosphoSiteiP50579.

Expressioni

Gene expression databases

ArrayExpressiP50579.
BgeeiP50579.
CleanExiHS_METAP2.
GenevestigatoriP50579.

Organism-specific databases

HPAiCAB013025.
HPA019095.

Interactioni

Subunit structurei

Interacts strongly with the eIF-2 gamma-subunit EIF2S3 By similarity. Binds EIF2S1 at low magnesium concentrations.

Protein-protein interaction databases

BioGridi116184. 12 interactions.
IntActiP50579. 2 interactions.
MINTiMINT-2803706.
STRINGi9606.ENSP00000325312.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi120 – 1234
Beta strandi133 – 1353
Beta strandi141 – 1433
Helixi149 – 1513
Helixi154 – 1618
Helixi163 – 18624
Helixi193 – 20816
Turni212 – 2143
Beta strandi215 – 22511
Beta strandi228 – 2303
Beta strandi248 – 2569
Beta strandi259 – 2679
Helixi271 – 2733
Helixi274 – 29017
Helixi297 – 30913
Beta strandi312 – 3154
Beta strandi318 – 3214
Beta strandi329 – 3346
Beta strandi337 – 3393
Beta strandi343 – 3497
Beta strandi360 – 37011
Beta strandi382 – 3854
Helixi397 – 40913
Turni410 – 4123
Helixi417 – 4226
Helixi429 – 4379
Beta strandi440 – 4445
Beta strandi455 – 46410
Beta strandi469 – 4713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B59X-ray1.80A109-478[»]
1B6AX-ray1.60A1-478[»]
1BN5X-ray1.80A1-478[»]
1BOAX-ray1.80A1-478[»]
1KQ0X-ray2.00A1-478[»]
1KQ9X-ray1.90A1-478[»]
1QZYX-ray1.60A1-478[»]
1R58X-ray1.90A110-478[»]
1R5GX-ray2.00A110-478[»]
1R5HX-ray2.40A110-478[»]
1YW7X-ray1.85A110-478[»]
1YW8X-ray2.65A110-478[»]
1YW9X-ray1.64A110-478[»]
2ADUX-ray1.90A110-478[»]
2EA2X-ray2.50A110-478[»]
2EA4X-ray2.35A110-478[»]
2GA2X-ray1.95A110-478[»]
2OAZX-ray1.90A110-478[»]
ProteinModelPortaliP50579.
SMRiP50579. Positions 110-478.

Miscellaneous databases

EvolutionaryTraceiP50579.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 466Poly-LysUniRule annotation
Compositional biasi98 – 1069Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
HOVERGENiHBG050495.
InParanoidiP50579.
KOiK01265.
OMAiIQICEEL.
PhylomeDBiP50579.
TreeFamiTF300426.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50579-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA    50
AGEQEPDKES GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK 100
KKKKKKRGPK VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT 150
TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL 200
EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI 250
DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV 300
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG 350
EATRMEEGEV YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK 400
HLLNVINENF GTLAFCRRWL DRLGESKYLM ALKNLCDLGI VDPYPPLCDI 450
KGSYTAQFEH TILLRPTCKE VVSRGDDY 478
Length:478
Mass (Da):52,892
Last modified:October 1, 1996 - v1
Checksum:i5788E4BB83E48F9A
GO
Isoform 2 (identifier: P50579-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: Missing.
     87-109: DGDGDGDGATGKKKKKKKKKRGP → A

Note: No experimental confirmation available.

Show »
Length:455
Mass (Da):50,510
Checksum:i6B2C99F5B40B951F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei50 – 501Missing in isoform 2.
VSP_055467
Alternative sequencei87 – 10923DGDGD…KKRGP → A in isoform 2.
VSP_055468Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti434 – 4341N → D in BAC03733. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29607 mRNA. Translation: AAA82930.1.
U13261 mRNA. Translation: AAC63402.1.
AK091730 mRNA. Translation: BAC03733.1.
AK315559 mRNA. Translation: BAG37935.1.
AC018475 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97537.1.
CH471054 Genomic DNA. Translation: EAW97538.1.
BC013782 mRNA. Translation: AAH13782.1.
CCDSiCCDS9052.1.
PIRiS52112. DPHUM2.
RefSeqiNP_006829.1. NM_006838.3.
UniGeneiHs.444986.

Genome annotation databases

EnsembliENST00000261220; ENSP00000261220; ENSG00000111142.
ENST00000323666; ENSP00000325312; ENSG00000111142.
GeneIDi10988.
KEGGihsa:10988.
UCSCiuc001tec.3. human.

Polymorphism databases

DMDMi1703273.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29607 mRNA. Translation: AAA82930.1 .
U13261 mRNA. Translation: AAC63402.1 .
AK091730 mRNA. Translation: BAC03733.1 .
AK315559 mRNA. Translation: BAG37935.1 .
AC018475 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97537.1 .
CH471054 Genomic DNA. Translation: EAW97538.1 .
BC013782 mRNA. Translation: AAH13782.1 .
CCDSi CCDS9052.1.
PIRi S52112. DPHUM2.
RefSeqi NP_006829.1. NM_006838.3.
UniGenei Hs.444986.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B59 X-ray 1.80 A 109-478 [» ]
1B6A X-ray 1.60 A 1-478 [» ]
1BN5 X-ray 1.80 A 1-478 [» ]
1BOA X-ray 1.80 A 1-478 [» ]
1KQ0 X-ray 2.00 A 1-478 [» ]
1KQ9 X-ray 1.90 A 1-478 [» ]
1QZY X-ray 1.60 A 1-478 [» ]
1R58 X-ray 1.90 A 110-478 [» ]
1R5G X-ray 2.00 A 110-478 [» ]
1R5H X-ray 2.40 A 110-478 [» ]
1YW7 X-ray 1.85 A 110-478 [» ]
1YW8 X-ray 2.65 A 110-478 [» ]
1YW9 X-ray 1.64 A 110-478 [» ]
2ADU X-ray 1.90 A 110-478 [» ]
2EA2 X-ray 2.50 A 110-478 [» ]
2EA4 X-ray 2.35 A 110-478 [» ]
2GA2 X-ray 1.95 A 110-478 [» ]
2OAZ X-ray 1.90 A 110-478 [» ]
ProteinModelPortali P50579.
SMRi P50579. Positions 110-478.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116184. 12 interactions.
IntActi P50579. 2 interactions.
MINTi MINT-2803706.
STRINGi 9606.ENSP00000325312.

Chemistry

BindingDBi P50579.
ChEMBLi CHEMBL3922.
DrugBanki DB00134. L-Methionine.
GuidetoPHARMACOLOGYi 1573.

Protein family/group databases

MEROPSi M24.002.

PTM databases

PhosphoSitei P50579.

Polymorphism databases

DMDMi 1703273.

2D gel databases

REPRODUCTION-2DPAGE IPI00033036.

Proteomic databases

MaxQBi P50579.
PaxDbi P50579.
PeptideAtlasi P50579.
PRIDEi P50579.

Protocols and materials databases

DNASUi 10988.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261220 ; ENSP00000261220 ; ENSG00000111142 .
ENST00000323666 ; ENSP00000325312 ; ENSG00000111142 .
GeneIDi 10988.
KEGGi hsa:10988.
UCSCi uc001tec.3. human.

Organism-specific databases

CTDi 10988.
GeneCardsi GC12P095800.
HGNCi HGNC:16672. METAP2.
HPAi CAB013025.
HPA019095.
MIMi 601870. gene.
neXtProti NX_P50579.
PharmGKBi PA30765.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
HOVERGENi HBG050495.
InParanoidi P50579.
KOi K01265.
OMAi IQICEEL.
PhylomeDBi P50579.
TreeFami TF300426.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 2681.
Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSi METAP2. human.
EvolutionaryTracei P50579.
GeneWikii METAP2.
GenomeRNAii 10988.
NextBioi 41747.
PROi P50579.
SOURCEi Search...

Gene expression databases

ArrayExpressi P50579.
Bgeei P50579.
CleanExi HS_METAP2.
Genevestigatori P50579.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes."
    Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67)."
    Li X., Chang Y.
    Biochim. Biophys. Acta 1260:333-336(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Heart and Placenta.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  7. "Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit."
    Datta B., Ray M.K., Chakrabarti D., Wylie D.E., Gupta N.K.
    J. Biol. Chem. 264:20620-20624(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EIF2S1 PROTECTION, GLYCOSYLATION.
  8. "Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese."
    Wang J., Sheppard G.S., Lou P., Kawai M., Park C., Egan D.A., Schneider A., Bouska J., Lesniewski R., Henkin J.
    Biochemistry 42:5035-5042(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases."
    Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.
    Biochemistry 49:5588-5599(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Localization and function of a eukaryotic-initiation-factor-2-associated 67-kDa glycoprotein."
    Wu S.
    World J. Biol. Chem. 1:313-320(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structure of human methionine aminopeptidase-2 complexed with fumagillin."
    Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J.
    Science 282:1324-1327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FUMAGILLIN, COFACTOR.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALT IONS AND BENGAMIDE, FUNCTION.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH INHIBITOR A-357300.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH 4-ARYL-1,2,3-TRIAZOLE AND COBALT IONS.
  19. "Human methionine aminopeptidase type 2 in complex with L- and D-methionine."
    Nonato M.C., Widom J., Clardy J.
    Bioorg. Med. Chem. Lett. 16:2580-2583(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND METHIONINE, PARTIAL PROTEIN SEQUENCE.
  20. "Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids."
    Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J., Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A., Lesniewski R., Sheppard G.S., Bell R.L.
    Bioorg. Med. Chem. Lett. 17:2817-2822(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 110-478 IN COMPLEX WITH MANGANESE AND INHIBITOR.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH COBALT IONS AND INHIBITOR, COFACTOR, FUNCTION.

Entry informationi

Entry nameiMAP2_HUMAN
AccessioniPrimary (citable) accession number: P50579
Secondary accession number(s): B2RDI8, G3XA91, Q8NB11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi