HRAS

Harvey rat sarcoma viral oncogene homolog

PDB rendering based on 1poz.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

121P, 1AA9, 1AGP, 1BKD, 1CLU, 1CRP, 1CRQ, 1CRR, 1CTQ, 1GNP, 1GNQ, 1GNR, 1HE8, 1IAQ, 1IOZ, 1JAH, 1JAI, 1K8R, 1LF0, 1LF5, 1LFD, 1NVU, 1NVV, 1NVW, 1NVX, 1P2S, 1P2T, 1P2U, 1P2V, 1PLJ, 1PLK, 1PLL, 1Q21, 1QRA, 1RVD, 1WQ1, 1XCM, 1XD2, 1XJ0, 1ZVQ, 1ZW6, 221P, 2C5L, 2CE2, 2CL0, 2CL6, 2CL7, 2CLC, 2CLD, 2EVW, 2GDP, 2LCF, 2LWI, 2N42, 2N46, 2Q21, 2QUZ, 2RGA, 2RGB, 2RGC, 2RGD, 2RGE, 2RGG, 2UZI, 2VH5, 2X1V, 3DDC, 3I3S, 3K8Y, 3K9L, 3K9N, 3KKM, 3KKN, 3KUD, 3L8Y, 3L8Z, 3LBH, 3LBI, 3LBN, 3LO5, 3OIU, 3OIV, 3OIW, 3RRY, 3RRZ, 3RS0, 3RS2, 3RS3, 3RS4, 3RS5, 3RS7, 3RSL, 3RSO, 3TGP, 421P, 4DLR, 4DLS, 4DLT, 4DLU, 4DLV, 4DLW, 4DLX, 4DLY, 4DLZ, 4DST, 4DSU, 4EFL, 4EFM, 4EFN, 4G0N, 4G3X, 4K81, 4L9S, 4L9W, 4NYI, 4NYJ, 4NYM, 4Q21, 4RSG, 4URU, 4URV, 4URW, 4URX, 4URY, 4URZ, 4US0, 4US1, 4US2, 4XVQ, 4XVR, 521P, 5P21, 621P, 6Q21, 721P, 821P

Identifiers

Symbols

HRAS ; C-BAS/HAS; C-H-RAS; C-HA-RAS1; CTLO; H-RASIDX; HAMSV; HRAS1; RASH1; p21ras

External IDs

OMIM: 190020 MGI: 88338 HomoloGene: 55890 GeneCards: HRAS Gene

Gene ontology
Molecular function	• GTPase activity • protein binding • GTP binding • protein C-terminus binding
Cellular component	• Golgi membrane • nucleus • cytoplasm • Golgi apparatus • cytosol • plasma membrane • perinuclear region of cytoplasm
Biological process	• MAPK cascade • activation of MAPKK activity • positive regulation of protein phosphorylation • stimulatory C-type lectin receptor signaling pathway • endocytosis • chemotaxis • cell cycle arrest • mitotic cell cycle checkpoint • signal transduction • cell surface receptor signaling pathway • epidermal growth factor receptor signaling pathway • small GTPase mediated signal transduction • Ras protein signal transduction • synaptic transmission • axon guidance • blood coagulation • cell proliferation • positive regulation of cell proliferation • negative regulation of cell proliferation • insulin receptor signaling pathway • fibroblast growth factor receptor signaling pathway • organ morphogenesis • negative regulation of gene expression • positive regulation of cell migration • negative regulation of GTPase activity • social behavior • Fc-epsilon receptor signaling pathway • positive regulation of MAP kinase activity • positive regulation of MAPK cascade • negative regulation of neuron apoptotic process • positive regulation of GTPase activity • innate immune response • positive regulation of DNA replication • positive regulation of transcription from RNA polymerase II promoter • positive regulation of JNK cascade • positive regulation of Ras protein signal transduction • vascular endothelial growth factor receptor signaling pathway • neurotrophin TRK receptor signaling pathway • ephrin receptor signaling pathway • regulation of long-term neuronal synaptic plasticity • positive regulation of epithelial cell proliferation • leukocyte migration • protein heterooligomerization • positive regulation of ERK1 and ERK2 cascade • positive regulation of wound healing • cellular senescence • intrinsic apoptotic signaling pathway • positive regulation of ruffle assembly • positive regulation of actin cytoskeleton reorganization • positive regulation of miRNA metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
0.53 – 0.54 Mb

Chr 7:
141.19 – 141.19 Mb

PubMed search

GTPase HRas also known as transforming protein p21 is an enzyme that in humans is encoded by the HRAS gene.^[1]^[2] The HRAS gene is located on the short (p) arm of chromosome 11 at position 15.5, from base pair 522,241 to base pair 525,549.^[3] HRas is a small G protein in the Ras subfamily of the Ras superfamily of small GTPases. Once bound to Guanosine triphosphate, H-Ras will activate a Raf kinase like c-Raf, the next step in the MAPK/ERK pathway.

Function

GTPase HRas is involved in regulating cell division in response to growth factor stimulation. Growth factors act by binding cell surface receptors that span the cell's plasma membrane. Once activated, receptors stimulate signal transduction events in the cytoplasm, a process by which proteins and second messengers relay signals from outside the cell to the cell nucleus and instructs the cell to grow or divide. The HRAS protein is a GTPase and is an early player in many signal transduction pathways and is usually associated with cell membranes due to the presence of an isoprenyl group on its C-terminus. HRAS acts as a molecular on/off switch, once it is turned on it recruits and activates proteins necessary for the propagation of the receptor's signal, such as c-Raf and PI 3-kinase. HRAS binds to GTP in the active state and possesses an intrinsic enzymatic activity that cleaves the terminal phosphate of this nucleotide converting it to GDP. Upon conversion of GTP to GDP, HRAS is turned off. The rate of conversion is usually slow but can be sped up dramatically by an accessory protein of the GTPase activating protein (GAP) class, for example RasGAP. In turn HRAS can bind to proteins of the Guanine Nucleotide Exchange Factor (GEF) class, for example SOS1, which forces the release of bound nucleotide. Subsequently, GTP present in the cytosol binds and HRAS-GTP dissociates from the GEF, resulting in HRAS activation. HRAS is in the Ras family, which also includes two other proto-oncogenes: KRAS and NRAS. These proteins all are regulated in the same manner and appear to differ largely in their sites of action within the cell.

Clinical significance

Costello syndrome

At least five inherited mutations in the HRAS gene have been identified in people with Costello syndrome. Each of these mutations changes an amino acid in a critical region of the HRAS protein. The most common mutation replaces the amino acid glycine with the amino acid serine at position 12 (written as Gly12Ser or G12S). The mutations responsible for Costello syndrome lead to the production of an HRAS protein that is permanently active. Instead of triggering cell growth in response to particular signals from outside the cell, the overactive protein directs cells to grow and divide constantly. This uncontrolled cell division can result in the formation of noncancerous and cancerous tumors. Researchers are uncertain how mutations in the HRAS gene cause the other features of Costello syndrome (such as mental retardation, distinctive facial features, and heart problems), but many of the signs and symptoms probably result from cell overgrowth and abnormal cell division.

Bladder cancer

HRAS has been shown to be a proto-oncogene. When mutated, proto-oncogenes have the potential to cause normal cells to become cancerous. Some gene mutations are acquired during a person's lifetime and are present only in certain cells. These changes are called somatic mutations and are not inherited. Somatic mutations in the HRAS gene in bladder cells have been associated with bladder cancer. One specific mutation has been identified in a significant percentage of bladder tumors; this mutation substitutes one protein building block (amino acid) for another amino acid in the HRAS protein. Specifically, the mutation replaces the amino acid glycine with the amino acid valine at position 12 (written as Gly12Val or G12V). The altered HRAS protein is permanently activated within the cell. This overactive protein directs the cell to grow and divide in the absence of outside signals, leading to uncontrolled cell division and the formation of a tumor. Mutations in the HRAS gene also have been associated with the progression of bladder cancer and an increased risk of tumor recurrence after treatment.

Other cancers

Somatic mutations in the HRAS gene are probably involved in the development of several other types of cancer. These mutations lead to an HRAS protein that is always active and can direct cells to grow and divide without control. Recent studies suggest that HRAS mutations are common in thyroid, salivary duct carcinoma,^[4] epithelial-myoepithelial carcinoma,^[5] and kidney cancers. The HRAS protein also may be produced at higher levels (overexpressed) in other types of cancer cells.

References

↑ Wong-Staal F, Dalla-Favera R, Franchini G, Gelmann EP, Gallo RC (Jul 1981). "Three distinct genes in human DNA related to the transforming genes of mammalian sarcoma retroviruses". Science 213 (4504): 226–8. doi:10.1126/science.6264598. PMID 6264598.
↑ Russell MW, Munroe DJ, Bric E, Housman DE, Dietz-Band J, Riethman HC, Collins FS, Brody LC (Jul 1996). "A 500-kb physical map and contig from the Harvey ras-1 gene to the 11p telomere". Genomics 35 (2): 353–60. doi:10.1006/geno.1996.0367. PMID 8661149.
↑ "Entrez Gene: v-Ha-ras Harvey rat sarcoma viral oncogene homolog".
↑ Chiosea SI, Williams L, Griffith CC, Thompson LD, Weinreb I, Bauman JE, Luvison A, Roy S, Seethala RR, Nikiforova MN (Jun 2015). "Molecular characterization of apocrine salivary duct carcinoma". The American Journal of Surgical Pathology 39 (6): 744–52. doi:10.1097/PAS.0000000000000410. PMID 25723113.
↑ Chiosea SI, Miller M, Seethala RR (Jun 2014). "HRAS mutations in epithelial-myoepithelial carcinoma". Head and Neck Pathology 8 (2): 146–50. doi:10.1007/s12105-013-0506-4. PMID 24277618.

External links

GeneReviews/NCBI/NIH/UW entry on Costello syndrome
HRAS protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

PDB gallery

121p: STRUKTUR UND GUANOSINTRIPHOSPHAT-HYDROLYSEMECHANISMUS DES C-TERMINAL VERKUERZTEN MENSCHLICHEN KREBSPROTEINS P21-H-RAS

1aa9: HUMAN C-HA-RAS(1-171)(DOT)GDP, NMR, MINIMIZED AVERAGE STRUCTURE

1agp: THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLY-12 MUTANT OF P21-H-RAS

1bkd: COMPLEX OF HUMAN H-RAS WITH HUMAN SOS-1

1clu: H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA,GAMMA-IMIDO-GTP

1crp: THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY

1crq: THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY

1crr: THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY

1ctq: STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K

1gnp: X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP

1gnq: X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP

1gnr: X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP

1he8: RAS G12V - PI 3-KINASE GAMMA COMPLEX

1iaq: C-H-RAS P21 PROTEIN MUTANT WITH THR 35 REPLACED BY SER (T35S) COMPLEXED WITH GUANOSINE-5'-[B,G-IMIDO] TRIPHOSPHATE

1ioz: Crystal Structure of the C-HA-RAS Protein Prepared by the Cell-Free Synthesis

1jah: H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MAGNESIUM

1jai: H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MANGANESE

1k8r: Crystal structure of Ras-Bry2RBD complex

1lf0: Crystal Structure of RasA59G in the GTP-bound form

1lf5: Crystal Structure of RasA59G in the GDP-bound Form

1lfd: CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS

1nvu: Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

1nvv: Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

1nvw: Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

1nvx: Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS

1p2s: H-Ras 166 in 50% 2,2,2 triflouroethanol

1p2t: H-Ras 166 in Aqueous mother liqour, RT

1p2u: H-Ras in 50% isopropanol

1p2v: H-RAS 166 in 60 % 1,6 hexanediol

1plj: CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS

1plk: CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS

1pll: CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS

1q21: CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP

1qra: STRUCTURE OF P21RAS IN COMPLEX WITH GTP AT 100 K

1rvd: H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA,GAMMA-IMIDO-GTP

1wq1: RAS-RASGAP COMPLEX

1xcm: Crystal structure of the GppNHp-bound H-Ras G60A mutant

1xd2: Crystal Structure of a ternary Ras:SOS:Ras*GDP complex

1xj0: Crystal Structure of the GDP-bound form of the RasG60A mutant

1zvq: Structure of the Q61G mutant of Ras in the GDP-bound form

1zw6: Crystal Structure of the GTP-bound form of RasQ61G

221p: THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

2c5l: STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS

2ce2: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP

2cl0: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GPPNHP

2cl6: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH S-CAGED GTP

2cl7: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GTP

2clc: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GTP (2)

2cld: CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP (2)

2evw: Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP

2q21: CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP

421p: THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

4q21: MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS

521p: THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

5p21: REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS

621p: THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

6q21: MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS

721p: THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

821p: THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLYCINE-12 MUTANT OF P21H-RAS

Neoplasm: Tumor suppressor genes/proteins and Oncogenes/Proto-oncogenes

Ligand

Growth factors	ONCO: c-Sis/PDGF HGF

Receptor

Wnt signaling pathway	TSP: CDH1

Hedgehog signaling pathway	TSP: PTCH1

TGF beta signaling pathway	TSP: TGF beta receptor 2

Receptor tyrosine kinase	ONCO: ErbB/c-ErbB HER2/neu Her 3 c-Met c-Ret

JAK-STAT signaling pathway	ONCO: c-Kit Flt3

Intracellular signaling P+Ps

Wnt signaling pathway	ONCO: Beta-catenin TSP: APC

TGF beta signaling pathway	TSP: SMAD2 SMAD4

Akt/PKB signaling pathway	TSP: PTEN ONCO: c-Akt

Hippo signaling pathway	TSP: Neurofibromin 2/Merlin

MAPK/ERK pathway	TSP: Neurofibromin 1 ONCO: c-Ras HRAS c-Raf

Other/unknown	TSP: Maspin ONCO: c-Src

Nucleus

Cell cycle	TSP: p53 pRb WT1 p16/p14arf ONCO: CDK4 Cyclin D Cyclin E

DNA repair/Fanconi	TSP: BRCA1 BRCA2

Ubiquitin ligase	TSP: VHL ONCO: CBL MDM2

Transcription factor	TSP: KLF6 ONCO: AP-1 c-Fos c-Jun c-Myc

Mitochondrion

Other/ungrouped

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

Intracellular signaling peptides and proteins

MAP

see MAP kinase pathway

Calcium

G protein

Heterotrimeric

cAMP:	Heterotrimeric G protein Gs/Gi Adenylate cyclase cAMP 3',5'-cyclic-AMP phosphodiesterase Protein kinase A

cGMP:	Transducin Guanylate cyclase cGMP 3',5'-cyclic-GMP phosphodiesterase Protein kinase G

G alpha subunit G_α GNAO1 GNAI1 GNAI2 GNAI3 GNAT1 GNAT2 GNAT3 GNAZ GNAS GNAL GNAQ GNA11 GNA12 GNA13 GNA14 GNA15/GNA16

G beta-gamma complex G_β GNB1 GNB2 GNB3 GNB4 GNB5 G_γ GNGT1 GNGT2 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNG10 GNG11 GNG12 GNG13 BSCL2

G protein-coupled receptor kinase AMP-activated protein kinase

Monomeric

Cyclin

Lipid

Other protein kinase

Serine/threonine:	Casein kinase 1 2 eIF-2 kinase EIF2AK3 Glycogen synthase kinase GSK1 GSK2 GSK-3 GSK3A GSK3B IκB kinase CHUK IKK2 IKBKG Interleukin-1 receptor-associated kinase IRAK1 IRAK2 IRAK3 IRAK4 Lim kinase LIMK1 LIMK2 p21-activated kinases PAK1 PAK2 PAK3 PAK4 Rho-associated protein kinase ROCK1 ROCK2 Ribosomal s6 kinase RPS6KA1

Tyrosine:	ZAP70 Focal adhesion protein-tyrosine kinase PTK2 PTK2B BTK

both	Dual-specificity kinase

Other protein phosphatase

Serine/threonine:	Protein phosphatase 2

Tyrosine:	protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase Sh2 domain-containing protein tyrosine phosphatase

both:	Dual-specificity phosphatase

Apoptosis

see apoptosis signaling pathway

GTP-binding protein regulators

see GTP-binding protein regulators

Other

see also deficiencies of intracellular signaling peptides and proteins

This article is issued from Wikipedia - version of the Friday, January 08, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.