WordNet

relating to or occurring in a term or fixed period of time; "terminal examinations"; "terminal payments"
a contact on an electrical device (such as a battery) at which electric current enters or leaves (同)pole
station where transport vehicles load or unload passengers or goods (同)terminus, depot
electronic equipment consisting of a device providing access to a computer; has a keyboard and display
being or situated at an end; "the endmost pillar"; "terminal buds on a branch"; "a terminal station"; "the terminal syllable"
causing or ending in or approaching death; "a terminal patient"; "terminal cancer"
of or relating to or situated at the ends of a delivery route; "freight pickup is a terminal service"; "terminal charges"
pertaining to or containing any of a group of organic compounds of nitrogen derived from ammonia (同)aminic
the radical -NH2 (同)amino_group

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『終りの』,末端の / 毎期の,定期の;学期末の / 『死に至る』, / 末端 / (電池の)端子 / (町の中心に近い)空港バス発着場;(一般に,鉄道・バスの)終点,終着駅

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/22 17:09:59」(JST)

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"N-term" redirects here. For the divergence test, see Term test.

A tetrapeptide (example: Val-Gly-Ser-Ala) with green highlighted N-terminal α-amino acid (example: L-valine) and blue marked C-terminal α-amino acid (example: L-alanine). This tetrapeptide could be encoded by the mRNA sequence 5'-GUUGGUAGUGCU-3'.

The N-terminus (also known as the amino-terminus, NH₂-terminus, N-terminal end or amine-terminus) refers to the start of a protein or polypeptide terminated by an amino acid with a free amine group (-NH₂). The convention for writing peptide sequences is to put the N-terminus on the left and write the sequence from N- to C-terminus. When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus.

Chemistry[edit]

Each amino acid has a carboxyl group and an amine group, and amino acids link to one another to form a chain by a dehydration reaction by joining the carboxyl group of one amino acid to the amine group of the next. Thus, polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an amine group, the N-terminus.

When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The amino end of an amino acid (on a charged tRNA) during the elongation stage of translation, attaches to the carboxyl end of the growing or nascent chain. Since the start codon of the genetic code codes for the amino acid methionine, most protein sequences start with a methionine (or, in bacteria, mitochondria and chloroplasts, the modified version N-formylmethionine, fMet). However, some proteins are modified posttranslationally, for example by cleavage from a protein precursor, and therefore may have different amino acids at their N-terminus.

Function[edit]

N-terminal targeting signals[edit]

The N-terminus is the first part of the protein that exits the ribosome during protein biosynthesis. It often contains signal peptide sequences, "intracellular postal codes" that direct delivery of the protein to the proper organelle. The signal peptide is typically removed at the destination by a signal peptidase. The N-terminal amino acid of a protein is an important determinant of its half-life (likelihood of being degraded). This is called the N-end rule.

Signal peptide[edit]

Main article: Signal peptide

The N-terminal signal peptide is recognized by the signal recognition particle (SRP) and results in the targeting of the protein to the secretory pathway. In eukaryotic cells, these proteins are synthesized at the rough endoplasmic reticulum. In prokaryotic cells, the proteins are exported across the cell membrane. In chloroplasts, signal peptides target proteins to the thylakoids.

Mitochondrial targeting peptide[edit]

The N-terminal mitochondrial targeting peptide (mtTP) allows for the protein to be imported into the mitochondrion.

Chloroplast targeting peptide[edit]

The N-terminal chloroplast targeting peptide (cpTP) allows for the protein to be imported into the chloroplast.

N-terminal modifications[edit]

Some proteins are modified posttranslationally by the addition of membrane anchors that allow the protein to associate with membrane without having a transmembrane domain. The N-terminus (as well as the C-terminus) of a protein can be modified this way.

N-Myristoylation[edit]

Main article: Myristoylation

The N-terminus can be modified by the addition of a myristoyl anchor. Proteins that are modified this way contain a consensus motif at their N-terminus as a modification signal.

N-Acylation[edit]

Main article: Palmitoylation

The N-terminus can also be modified by the addition of a fatty acid anchor to form N-acylated proteins. The most common form of such modification is the addition of a palmitoyl group.

References[edit]

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English Journal

Circulating concentrations of vitamin E isomers: Association with bone turnover and arterial stiffness in post-menopausal women.

Hampson G1, Edwards S2, Sankaralingam A3, Harrington DJ4, Voong K4, Fogelman I2, Frost ML2.
Bone.Bone.2015 Dec;81:407-12. doi: 10.1016/j.bone.2015.08.010. Epub 2015 Aug 11.
The effects of vitamin E on cardiovascular and bone health are conflicting with beneficial and detrimental findings reported. To investigate this further, we carried out a cross-sectional study to determine the relationship between circulating concentrations of the 2 vitamin E isomers, α- and γ-to
PMID 26271527

Signaling pathway of MAPK/ERK in cell proliferation, differentiation, migration, senescence and apoptosis.

Sun Y1, Liu WZ1, Liu T1, Feng X1, Yang N1, Zhou HF1.
Journal of receptor and signal transduction research.J Recept Signal Transduct Res.2015 Dec;35(6):600-4. doi: 10.3109/10799893.2015.1030412. Epub 2015 Jun 22.
The generic mitogen-activated protein kinases (MAPK) signaling pathway is shared by four distinct cascades, including the extracellular signal-related kinases (ERK1/2), Jun amino-terminal kinases (JNK1/2/3), p38-MAPK and ERK5. Mitogen-activated protein kinases/extracellular signal-regulated kinase (
PMID 26096166

High CO2 Leads to Na,K-ATPase Endocytosis via c-Jun Amino-Terminal Kinase-Induced LMO7b Phosphorylation.

Dada LA1, Trejo Bittar HE2, Welch LC2, Vagin O3, Deiss-Yehiely N2, Kelly AM2, Baker MR2, Capri J4, Cohn W4, Whitelegge JP4, Vadász I5, Gruenbaum Y6, Sznajder JI2.
Molecular and cellular biology.Mol Cell Biol.2015 Dec 1;35(23):3962-73. doi: 10.1128/MCB.00813-15. Epub 2015 Sep 14.
The c-Jun amino-terminal kinase (JNK) plays a role in inflammation, proliferation, apoptosis, and cell adhesion and cell migration by phosphorylating paxillin and β-catenin. JNK phosphorylation downstream of AMP-activated protein kinase (AMPK) activation is required for high CO2 (hypercapnia)-induc
PMID 26370512

Japanese Journal

Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA

Shaik Syed Ali P.,John Jasmine,Selvaraj Manikandan [他]
Microbiology and immunology 59(5), 299-304, 2015-05
NAID 40020479147

Preparation and Characterization of Liquid Rubber-modified Polybenzoxazine

Suwitaningsih Dwi Ngesti,Katsuta Seizaburo,Kawauchi Takehiro,Furukawa Nobuyuki,Takeichi Tsutomu
Journal of Photopolymer Science and Technology 28(2), 137-143, 2015
… We used three kinds of liquid rubber having different functional groups at the chain-end, which are amino, carboxyl and methoxyl groups, namely ATBN, CTBN and ETBN, respectively, to examine the effect of liquid rubber terminal groups on the polymerization of a typical benzoxazine monomer, F-a, and the compatibility with the polybenzoxazine, PF-a. …
NAID 130005093836

N-Linked Glycosylation at an Appropriate Position in the Pre-S2 Domain Is Critical for Cellular and Humoral Immunity against Middle HBV Surface Antigen

Liu Hao,Wang Shixia,Jia Yiqiong,Li Jun,Huang Zuhu,Lu Shan,Xing Yiping
The Tohoku Journal of Experimental Medicine 236(2), 131-138, 2015
… Among these envelope proteins, the middle HBV surface antigen (MHBs) contains a constitutive N-linked glycosylation site at position 4 (Asn4) in the amino-terminal portion (MQWNSTTFHQ) of pre-S2 domain. … Here, we constructed four MHBs genes carrying mutations, underlined, in the amino-terminal portion of pre-S2 domain. …
NAID 130005075697