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O00468

- AGRIN_HUMAN

UniProt

O00468 - AGRIN_HUMAN

Protein

Agrin

Gene

AGRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 5 (06 Mar 2013)
      Previous versions | rss
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    Functioni

    Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.
    Isoform 2: transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.
    Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.
    Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.
    Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling By similarity.By similarity
    Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1102 – 11032Cleavage, alpha site; by neurotrypsinBy similarity
    Sitei1250 – 12501Alternative splice site to produce 'x' isoformsBy similarity
    Sitei1751 – 17511Alternative splice site to produce 'y' isoformsBy similarity
    Sitei1862 – 18621Critical for cleavage by neurotrypsinBy similarity
    Sitei1863 – 18642Cleavage, beta site; by neurotrypsinBy similarity
    Sitei1888 – 18881Alternative splice site to produce 'z' isoformsBy similarity
    Sitei1892 – 18921Highly important for the agrin receptor complex activity of the 'z(8)' insertBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1940 – 200869By similarityAdd
    BLAST

    GO - Molecular functioni

    1. acetylcholine receptor regulator activity Source: Ensembl
    2. calcium ion binding Source: UniProtKB
    3. chondroitin sulfate binding Source: UniProtKB
    4. dystroglycan binding Source: UniProtKB
    5. heparan sulfate proteoglycan binding Source: UniProtKB
    6. laminin binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. sialic acid binding Source: UniProtKB
    9. structural constituent of cytoskeleton Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. carbohydrate metabolic process Source: Reactome
    3. chondroitin sulfate metabolic process Source: Reactome
    4. clustering of voltage-gated sodium channels Source: UniProtKB
    5. extracellular matrix organization Source: Reactome
    6. glycosaminoglycan biosynthetic process Source: Reactome
    7. glycosaminoglycan catabolic process Source: Reactome
    8. glycosaminoglycan metabolic process Source: Reactome
    9. G-protein coupled acetylcholine receptor signaling pathway Source: UniProtKB
    10. neuromuscular junction development Source: Ensembl
    11. neurotransmitter receptor metabolic process Source: Ensembl
    12. phototransduction, visible light Source: Reactome
    13. plasma membrane organization Source: Ensembl
    14. positive regulation of filopodium assembly Source: UniProtKB
    15. positive regulation of neuron apoptotic process Source: Ensembl
    16. positive regulation of Rho GTPase activity Source: UniProtKB
    17. positive regulation of synaptic growth at neuromuscular junction Source: UniProtKB
    18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. receptor clustering Source: UniProtKB
    20. retinoid metabolic process Source: Reactome
    21. signal transduction Source: UniProtKB
    22. small molecule metabolic process Source: Reactome
    23. synapse organization Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_120752. HS-GAG degradation.
    REACT_121248. HS-GAG biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_13552. Integrin cell surface interactions.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_18312. NCAM1 interactions.
    REACT_24968. Retinoid metabolism and transport.
    SignaLinkiO00468.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agrin
    Cleaved into the following 4 chains:
    Gene namesi
    Name:AGRN
    Synonyms:AGRIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:329. AGRN.

    Subcellular locationi

    Isoform 1 : Secretedextracellular spaceextracellular matrix
    Note: Synaptic basal lamina at the neuromuscular junction.By similarity

    GO - Cellular componenti

    1. basal lamina Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. cell surface Source: Ensembl
    4. cytoplasm Source: HPA
    5. extracellular matrix Source: UniProtKB
    6. extracellular region Source: Reactome
    7. extracellular space Source: Ensembl
    8. extracellular vesicular exosome Source: UniProt
    9. Golgi lumen Source: Reactome
    10. integral component of membrane Source: UniProtKB-KW
    11. lysosomal lumen Source: Reactome
    12. plasma membrane Source: HPA
    13. synapse Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Extracellular matrix, Membrane, Secreted, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Myasthenia, limb-girdle, familial (LGM) [MIM:254300]: A congenital myasthenic syndrome characterized by a typical 'limb girdle' pattern of muscle weakness with small, simplified neuromuscular junctions but normal acetylcholine receptor and acetylcholinesterase function.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1709 – 17091G → R in LGM; results in disruption of the neuromuscular junction architecture; does not affect phosphorylation of MUSK; does not affect AChR clustering. 1 Publication
    VAR_068742
    Natural varianti1727 – 17271V → F in LGM; decreased AGRN-induced clustering of AChR by >100-fold and decreased phosphorylation of the MUSK receptor and AChR beta subunit by about 10-fold. Increased binding to alpha-dystroglycan. 1 Publication
    VAR_069066

    Keywords - Diseasei

    Congenital myasthenic syndrome, Disease mutation

    Organism-specific databases

    MIMi254300. phenotype.
    Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBiPA24626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 20672038AgrinPRO_0000007471Add
    BLAST
    Chaini30 – 11021073Agrin N-terminal 110 kDa subunitBy similarityPRO_0000421613Add
    BLAST
    Chaini1103 – 2067965Agrin C-terminal 110 kDa subunitBy similarityPRO_0000421614Add
    BLAST
    Chaini1103 – 1863761Agrin C-terminal 90 kDa fragmentBy similarityPRO_0000421615Add
    BLAST
    Chaini1864 – 2067204Agrin C-terminal 22 kDa fragmentBy similarityPRO_0000421616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 103By similarity
    Glycosylationi135 – 1351N-linked (GlcNAc...)1 Publication
    Disulfide bondi152 ↔ 177Or C-152 with C-183PROSITE-ProRule annotation
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi777 – 7771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi793 ↔ 805By similarity
    Disulfide bondi795 ↔ 812By similarity
    Disulfide bondi814 ↔ 823By similarity
    Disulfide bondi826 ↔ 844By similarity
    Disulfide bondi847 ↔ 859By similarity
    Disulfide bondi849 ↔ 866By similarity
    Disulfide bondi868 ↔ 877By similarity
    Disulfide bondi880 ↔ 891By similarity
    Glycosylationi932 – 9321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1333 ↔ 1344By similarity
    Disulfide bondi1338 ↔ 1355By similarity
    Disulfide bondi1357 ↔ 1366By similarity
    Disulfide bondi1519 ↔ 1548By similarity
    Disulfide bondi1553 ↔ 1564By similarity
    Disulfide bondi1558 ↔ 1574By similarity
    Disulfide bondi1576 ↔ 1585By similarity
    Disulfide bondi1592 ↔ 1603By similarity
    Disulfide bondi1597 ↔ 1613By similarity
    Disulfide bondi1615 ↔ 1624By similarity
    Disulfide bondi1822 ↔ 1836By similarity
    Disulfide bondi1830 ↔ 1845By similarity
    Glycosylationi1835 – 18351O-linked (Fuc...)By similarity
    Disulfide bondi1847 ↔ 1856By similarity
    Disulfide bondi2038 ↔ 2064By similarity

    Post-translational modificationi

    Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions By similarity.By similarity
    At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ).

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Heparan sulfate, Proteoglycan

    Proteomic databases

    MaxQBiO00468.
    PaxDbiO00468.
    PRIDEiO00468.

    PTM databases

    PhosphoSiteiO00468.

    Expressioni

    Tissue specificityi

    Expressed in basement membranes of lung and kidney. Muscle- and neuron-specific isoforms are found. Isoforms (y+) with the 4 AA insert and (z+8) isoforms with the 8 AA insert are all neuron-specific. Isoforms (z+11) are found in both neuronal and non-neuronal tissues.3 Publications

    Gene expression databases

    ArrayExpressiO00468.
    BgeeiO00468.
    CleanExiHS_AGRN.
    GenevestigatoriO00468.

    Organism-specific databases

    HPAiHPA040090.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1 By similarity. Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN7O152652EBI-947482,EBI-708350

    Protein-protein interaction databases

    BioGridi132000. 7 interactions.
    IntActiO00468. 7 interactions.
    MINTiMINT-4053526.
    STRINGi9606.ENSP00000368678.

    Structurei

    3D structure databases

    ProteinModelPortaliO00468.
    SMRiO00468. Positions 36-146, 170-751, 793-921, 934-969, 1320-2067.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 157128NtAPROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 24454Kazal-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 31956Kazal-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini337 – 39155Kazal-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini408 – 46356Kazal-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini484 – 53653Kazal-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini540 – 60162Kazal-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini607 – 66660Kazal-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini699 – 75254Kazal-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini793 – 84654Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini847 – 89347Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 97155Kazal-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1130 – 1252123SEAPROSITE-ProRule annotationAdd
    BLAST
    Domaini1329 – 136739EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1372 – 1548177Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1549 – 158638EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1588 – 162538EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1635 – 1822188Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1818 – 185740EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1868 – 2064197Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi671 – 6777Gly/Ser-rich
    Compositional biasi974 – 1099126Ser/Thr-richAdd
    BLAST
    Compositional biasi1058 – 109740Gly/Ser-richAdd
    BLAST
    Compositional biasi1254 – 132471Ser/Thr-richAdd
    BLAST

    Domaini

    The NtA domain, absent in TM-agrin, is required for binding laminin and connecting to basal lamina.
    Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan/DAG1 binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding By similarity.By similarity

    Sequence similaritiesi

    Contains 4 EGF-like domains.PROSITE-ProRule annotation
    Contains 9 Kazal-like domains.PROSITE-ProRule annotation
    Contains 2 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 3 laminin G-like domains.PROSITE-ProRule annotation
    Contains 1 NtA (N-terminal agrin) domain.PROSITE-ProRule annotation
    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Laminin EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG312635.
    HOGENOMiHOG000033860.
    HOVERGENiHBG080471.
    InParanoidiO00468.
    KOiK06254.
    OMAiPRCSCDR.
    OrthoDBiEOG7BGHJZ.
    TreeFamiTF326548.

    Family and domain databases

    Gene3Di2.60.120.200. 3 hits.
    3.30.70.960. 1 hit.
    InterProiIPR004850. Agrin_NtA.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR003645. Fol_N.
    IPR002350. Kazal_dom.
    IPR001791. Laminin_G.
    IPR000082. SEA_dom.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view]
    PfamiPF00008. EGF. 3 hits.
    PF00050. Kazal_1. 3 hits.
    PF07648. Kazal_2. 6 hits.
    PF00053. Laminin_EGF. 2 hits.
    PF00054. Laminin_G_1. 3 hits.
    PF03146. NtA. 1 hit.
    PF01390. SEA. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 4 hits.
    SM00180. EGF_Lam. 2 hits.
    SM00274. FOLN. 5 hits.
    SM00280. KAZAL. 9 hits.
    SM00282. LamG. 3 hits.
    SM00200. SEA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 4 hits.
    SSF50242. SSF50242. 1 hit.
    SSF82671. SSF82671. 1 hit.
    PROSITEiPS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 1 hit.
    PS50027. EGF_LAM_2. 2 hits.
    PS51465. KAZAL_2. 9 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51121. NTA. 1 hit.
    PS50024. SEA. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Many isoforms may exist depending on the occurrence and length of inserts at the x, y or z splice site. Four 'z' isoforms can be produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity.

    Isoform 1 (identifier: O00468-1) [UniParc]FASTAAdd to Basket

    Also known as: Secreted agrin, LN-agrin

    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

    MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT     50
    VEEILNVDPV QHTYSCKVRV WRYLKGKDLV ARESLLDGGN KVVISGFGDP 100
    LICDNQVSTG DTRIFFVNPA PPYLWPAHKN ELMLNSSLMR ITLRNLEEVE 150
    FCVEDKPGTH FTPVPPTPPD ACRGMLCGFG AVCEPNAEGP GRASCVCKKS 200
    PCPSVVAPVC GSDASTYSNE CELQRAQCSQ QRRIRLLSRG PCGSRDPCSN 250
    VTCSFGSTCA RSADGLTASC LCPATCRGAP EGTVCGSDGA DYPGECQLLR 300
    RACARQENVF KKFDGPCDPC QGALPDPSRS CRVNPRTRRP EMLLRPESCP 350
    ARQAPVCGDD GVTYENDCVM GRSGAARGLL LQKVRSGQCQ GRDQCPEPCR 400
    FNAVCLSRRG RPRCSCDRVT CDGAYRPVCA QDGRTYDSDC WRQQAECRQQ 450
    RAIPSKHQGP CDQAPSPCLG VQCAFGATCA VKNGQAACEC LQACSSLYDP 500
    VCGSDGVTYG SACELEATAC TLGREIQVAR KGPCDRCGQC RFGALCEAET 550
    GRCVCPSECV ALAQPVCGSD GHTYPSECML HVHACTHQIS LHVASAGPCE 600
    TCGDAVCAFG AVCSAGQCVC PRCEHPPPGP VCGSDGVTYG SACELREAAC 650
    LQQTQIEEAR AGPCEQAECG SGGSGSGEDG DCEQELCRQR GGIWDEDSED 700
    GPCVCDFSCQ SVPGSPVCGS DGVTYSTECE LKKARCESQR GLYVAAQGAC 750
    RGPTFAPLPP VAPLHCAQTP YGCCQDNITA ARGVGLAGCP SACQCNPHGS 800
    YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG RSGCTPCSCD 850
    PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPAG CEADASAPAT 900
    CAEMRCEFGA RCVEESGSAH CVCPMLTCPE ANATKVCGSD GVTYGNECQL 950
    KTIACRQGLQ ISIQSLGPCQ EAVAPSTHPT SASVTVTTPG LLLSQALPAP 1000
    PGALPLAPSS TAHSQTTPPP SSRPRTTASV PRTTVWPVLT VPPTAPSPAP 1050
    SLVASAFGES GSTDGSSDEE LSGDQEASGG GSGGLEPLEG SSVATPGPPV 1100
    ERASCYNSAL GCCSDGKTPS LDAEGSNCPA TKVFQGVLEL EGVEGQELFY 1150
    TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFRSVR LRDLGPGKSV 1200
    RAIVDVHFDP TTAFRAPDVA RALLRQIQVS RRRSLGVRRP LQEHVRFMDF 1250
    DWFPAFITGA TSGAIAAGAT ARATTASRLP SSAVTPRAPH PSHTSQPVAK 1300
    TTAAPTTRRP PTTAPSRVPG RRPPAPQQPP KPCDSQPCFH GGTCQDWALG 1350
    GGFTCSCPAG RGGAVCEKVL GAPVPAFEGR SFLAFPTLRA YHTLRLALEF 1400
    RALEPQGLLL YNGNARGKDF LALALLDGRV QLRFDTGSGP AVLTSAVPVE 1450
    PGQWHRLELS RHWRRGTLSV DGETPVLGES PSGTDGLNLD TDLFVGGVPE 1500
    DQAAVALERT FVGAGLRGCI RLLDVNNQRL ELGIGPGAAT RGSGVGECGD 1550
    HPCLPNPCHG GAPCQNLEAG RFHCQCPPGR VGPTCADEKS PCQPNPCHGA 1600
    APCRVLPEGG AQCECPLGRE GTFCQTASGQ DGSGPFLADF NGFSHLELRG 1650
    LHTFARDLGE KMALEVVFLA RGPSGLLLYN GQKTDGKGDF VSLALRDRRL 1700
    EFRYDLGKGA AVIRSREPVT LGAWTRVSLE RNGRKGALRV GDGPRVLGES 1750
    PKSRKVPHTV LNLKEPLYVG GAPDFSKLAR AAAVSSGFDG AIQLVSLGGR 1800
    QLLTPEHVLR QVDVTSFAGH PCTRASGHPC LNGASCVPRE AAYVCLCPGG 1850
    FSGPHCEKGL VEKSAGDVDT LAFDGRTFVE YLNAVTESEL ANEIPVPETL 1900
    DSGALHEKAL QSNHFELSLR TEATQGLVLW SGKATERADY VALAIVDGHL 1950
    QLSYNLGSQP VVLRSTVPVN TNRWLRVVAH REQREGSLQV GNEAPVTGSS 2000
    PLGATQLDTD GALWLGGLPE LPVGPALPKA YGTGFVGCLR DVVVGRHPLH 2050
    LLEDAVTKPE LRPCPTP 2067
    Length:2,067
    Mass (Da):217,232
    Last modified:March 6, 2013 - v5
    Checksum:iE7FAAB9AFB7B8039
    GO
    Isoform 2 (identifier: O00468-2) [UniParc]FASTAAdd to Basket

    Also known as: Transmembrane agrin, TM-agrin

    The sequence of this isoform differs from the canonical sequence as follows:
         1-104: Missing.
         105-154: NQVSTGDTRI...NLEEVEFCVE → MPXLAVARDT...FAVLLFLNNY

    Note: Produced by usage of an alternative first exon.

    Show »
    Length:1,963
    Mass (Da):205,544
    Checksum:i8E904C7A584AE78F
    GO
    Isoform 3 (identifier: O00468-3) [UniParc]FASTAAdd to Basket

    Also known as: Agrin z(0)

    The sequence of this isoform differs from the canonical sequence as follows:
         1889-1906: Missing.

    Show »
    Length:2,049
    Mass (Da):215,345
    Checksum:iC6CC67CA63060E92
    GO
    Isoform 4 (identifier: O00468-4) [UniParc]FASTAAdd to Basket

    Also known as: Agrin z(+11)

    The sequence of this isoform differs from the canonical sequence as follows:
         1889-1896: Missing.

    Show »
    Length:2,059
    Mass (Da):216,366
    Checksum:i45560978CFB636D3
    GO
    Isoform 5 (identifier: O00468-5) [UniParc]FASTAAdd to Basket

    Also known as: Agrin z(+8)

    The sequence of this isoform differs from the canonical sequence as follows:
         1897-1906: Missing.

    Show »
    Length:2,057
    Mass (Da):216,211
    Checksum:i099A9FB384BDE301
    GO
    Isoform 6 (identifier: O00468-6) [UniParc]FASTAAdd to Basket

    Also known as: Agrin y(0)z(0)

    The sequence of this isoform differs from the canonical sequence as follows:
         1752-1755: Missing.
         1889-1906: Missing.

    Show »
    Length:2,045
    Mass (Da):214,846
    Checksum:i108BDA7146ECB94D
    GO
    Isoform 7 (identifier: O00468-7) [UniParc]FASTAAdd to Basket

    Also known as: y(0)

    The sequence of this isoform differs from the canonical sequence as follows:
         1752-1755: Missing.

    Show »
    Length:2,063
    Mass (Da):216,733
    Checksum:i9E761313F0E53B1B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti343 – 3431L → R in AAB52917. (PubMed:9652404)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231V → L.1 Publication
    VAR_068724
    Natural varianti58 – 581D → N.1 Publication
    VAR_068725
    Natural varianti105 – 1051N → I.1 Publication
    VAR_068726
    Natural varianti267 – 2671T → M.1 Publication
    VAR_068727
    Natural varianti375 – 3751A → S.1 Publication
    Corresponds to variant rs138031468 [ dbSNP | Ensembl ].
    VAR_068728
    Natural varianti728 – 7281E → V.1 Publication
    Corresponds to variant rs113288277 [ dbSNP | Ensembl ].
    VAR_068729
    Natural varianti852 – 8521Q → R.1 Publication
    Corresponds to variant rs9697293 [ dbSNP | Ensembl ].
    VAR_068730
    Natural varianti984 – 9841V → M.1 Publication
    VAR_068731
    Natural varianti1088 – 10881L → F.1 Publication
    Corresponds to variant rs150132566 [ dbSNP | Ensembl ].
    VAR_068732
    Natural varianti1118 – 11181T → K.1 Publication
    Corresponds to variant rs149159118 [ dbSNP | Ensembl ].
    VAR_068733
    Natural varianti1135 – 11351Q → R.1 Publication
    Corresponds to variant rs142416636 [ dbSNP | Ensembl ].
    VAR_068734
    Natural varianti1240 – 12401P → L.1 Publication
    Corresponds to variant rs142620337 [ dbSNP | Ensembl ].
    VAR_068735
    Natural varianti1341 – 13411G → R.1 Publication
    VAR_068736
    Natural varianti1451 – 14511P → L.1 Publication
    VAR_068737
    Natural varianti1514 – 15141A → T.1 Publication
    Corresponds to variant rs111818381 [ dbSNP | Ensembl ].
    VAR_068738
    Natural varianti1565 – 15651Q → H.1 Publication
    Corresponds to variant rs199876002 [ dbSNP | Ensembl ].
    VAR_068739
    Natural varianti1666 – 16661V → I.1 Publication
    Corresponds to variant rs17160775 [ dbSNP | Ensembl ].
    VAR_048966
    Natural varianti1671 – 16711R → Q.1 Publication
    VAR_068740
    Natural varianti1698 – 16981R → P.1 Publication
    VAR_068741
    Natural varianti1709 – 17091G → R in LGM; results in disruption of the neuromuscular junction architecture; does not affect phosphorylation of MUSK; does not affect AChR clustering. 1 Publication
    VAR_068742
    Natural varianti1727 – 17271V → F in LGM; decreased AGRN-induced clustering of AChR by >100-fold and decreased phosphorylation of the MUSK receptor and AChR beta subunit by about 10-fold. Increased binding to alpha-dystroglycan. 1 Publication
    VAR_069066
    Natural varianti1734 – 17341R → H.1 Publication
    Corresponds to variant rs145444272 [ dbSNP | Ensembl ].
    VAR_068743
    Natural varianti1789 – 17891D → N.1 Publication
    VAR_068744
    Natural varianti2045 – 20451G → V.1 Publication
    VAR_068745

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 104104Missing in isoform 2. CuratedVSP_045753Add
    BLAST
    Alternative sequencei105 – 15450NQVST…EFCVE → MPXLAVARDTRQPAGASLLV RGFMVPCNACLILLATATLG FAVLLFLNNY in isoform 2. CuratedVSP_045754Add
    BLAST
    Alternative sequencei1752 – 17554Missing in isoform 6 and isoform 7. CuratedVSP_045755
    Alternative sequencei1889 – 190618Missing in isoform 3 and isoform 6. 2 PublicationsVSP_045756Add
    BLAST
    Alternative sequencei1889 – 18968Missing in isoform 4. CuratedVSP_045757
    Alternative sequencei1897 – 190610Missing in isoform 5. CuratedVSP_045758

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U84406 mRNA. Translation: AAB52917.1.
    AB191264 mRNA. Translation: BAD52440.1.
    AL645608 Genomic DNA. Translation: CAI15575.2.
    AL645608 Genomic DNA. Translation: CAI15576.1.
    AF016903 mRNA. Translation: AAC39776.1.
    BC004220 mRNA. Translation: AAH04220.2.
    BC007649 mRNA. Translation: AAH07649.1.
    BC034009 mRNA. Translation: AAH34009.1.
    BC063620 mRNA. Translation: AAH63620.1.
    CCDSiCCDS30551.1. [O00468-6]
    RefSeqiNP_940978.2. NM_198576.3. [O00468-6]
    XP_005244806.1. XM_005244749.1. [O00468-3]
    XP_006710696.1. XM_006710633.1. [O00468-5]
    UniGeneiHs.273330.
    Hs.602356.

    Genome annotation databases

    EnsembliENST00000379370; ENSP00000368678; ENSG00000188157. [O00468-6]
    GeneIDi375790.
    KEGGihsa:375790.
    UCSCiuc001ack.2. human. [O00468-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    The Leiden Muscular Dystrophy pages, Agrin (AGRN)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U84406 mRNA. Translation: AAB52917.1 .
    AB191264 mRNA. Translation: BAD52440.1 .
    AL645608 Genomic DNA. Translation: CAI15575.2 .
    AL645608 Genomic DNA. Translation: CAI15576.1 .
    AF016903 mRNA. Translation: AAC39776.1 .
    BC004220 mRNA. Translation: AAH04220.2 .
    BC007649 mRNA. Translation: AAH07649.1 .
    BC034009 mRNA. Translation: AAH34009.1 .
    BC063620 mRNA. Translation: AAH63620.1 .
    CCDSi CCDS30551.1. [O00468-6 ]
    RefSeqi NP_940978.2. NM_198576.3. [O00468-6 ]
    XP_005244806.1. XM_005244749.1. [O00468-3 ]
    XP_006710696.1. XM_006710633.1. [O00468-5 ]
    UniGenei Hs.273330.
    Hs.602356.

    3D structure databases

    ProteinModelPortali O00468.
    SMRi O00468. Positions 36-146, 170-751, 793-921, 934-969, 1320-2067.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 132000. 7 interactions.
    IntActi O00468. 7 interactions.
    MINTi MINT-4053526.
    STRINGi 9606.ENSP00000368678.

    PTM databases

    PhosphoSitei O00468.

    Proteomic databases

    MaxQBi O00468.
    PaxDbi O00468.
    PRIDEi O00468.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379370 ; ENSP00000368678 ; ENSG00000188157 . [O00468-6 ]
    GeneIDi 375790.
    KEGGi hsa:375790.
    UCSCi uc001ack.2. human. [O00468-1 ]

    Organism-specific databases

    CTDi 375790.
    GeneCardsi GC01P000946.
    GeneReviewsi AGRN.
    HGNCi HGNC:329. AGRN.
    HPAi HPA040090.
    MIMi 103320. gene.
    254300. phenotype.
    neXtProti NX_O00468.
    Orphaneti 98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBi PA24626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312635.
    HOGENOMi HOG000033860.
    HOVERGENi HBG080471.
    InParanoidi O00468.
    KOi K06254.
    OMAi PRCSCDR.
    OrthoDBi EOG7BGHJZ.
    TreeFami TF326548.

    Enzyme and pathway databases

    Reactomei REACT_120752. HS-GAG degradation.
    REACT_121248. HS-GAG biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_13552. Integrin cell surface interactions.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_18312. NCAM1 interactions.
    REACT_24968. Retinoid metabolism and transport.
    SignaLinki O00468.

    Miscellaneous databases

    GeneWikii Agrin.
    GenomeRNAii 375790.
    NextBioi 100617.
    PROi O00468.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00468.
    Bgeei O00468.
    CleanExi HS_AGRN.
    Genevestigatori O00468.

    Family and domain databases

    Gene3Di 2.60.120.200. 3 hits.
    3.30.70.960. 1 hit.
    InterProi IPR004850. Agrin_NtA.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR003645. Fol_N.
    IPR002350. Kazal_dom.
    IPR001791. Laminin_G.
    IPR000082. SEA_dom.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view ]
    Pfami PF00008. EGF. 3 hits.
    PF00050. Kazal_1. 3 hits.
    PF07648. Kazal_2. 6 hits.
    PF00053. Laminin_EGF. 2 hits.
    PF00054. Laminin_G_1. 3 hits.
    PF03146. NtA. 1 hit.
    PF01390. SEA. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 4 hits.
    SM00180. EGF_Lam. 2 hits.
    SM00274. FOLN. 5 hits.
    SM00280. KAZAL. 9 hits.
    SM00282. LamG. 3 hits.
    SM00200. SEA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 4 hits.
    SSF50242. SSF50242. 1 hit.
    SSF82671. SSF82671. 1 hit.
    PROSITEi PS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 1 hit.
    PS50027. EGF_LAM_2. 2 hits.
    PS51465. KAZAL_2. 9 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51121. NTA. 1 hit.
    PS50024. SEA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and high expression of human agrin in basement membranes of adult lung and kidney."
      Groffen A.J.A., Buskens C.A.F., Van Kuppevelt T.H., Veerkamp J.H., Monnens L.A.H., Van den Heuvel L.P.W.J.
      Eur. J. Biochem. 254:123-128(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    2. Kato S.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Retinal pigment epithelium.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1703-1949 (ISOFORM 6).
    4. "Agrin binds to the nerve-muscle basal lamina via laminin."
      Denzer A.J., Brandenberger R., Gesemann M., Chiquet M., Ruegg M.A.
      J. Cell Biol. 137:671-683(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-172, INTERACTION WITH LAMININ.
    5. "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] OF 1558-2045.
      Tissue: Brain, Colon and Kidney.
    6. "An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein."
      Neumann F.R., Bittcher G., Annies M., Schumacher B., Kroger S., Ruegg M.A.
      Mol. Cell. Neurosci. 17:208-225(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2).
    7. "Identification of agrinSN isoform and muscle-specific receptor tyrosine kinase (MuSK) in sperm."
      Kumar P., Ferns M.J., Meizel S.
      Biochem. Biophys. Res. Commun. 342:522-528(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    8. Erratum
      Kumar P., Ferns M.J., Meizel S.
      Biochem. Biophys. Res. Commun. 344:453-453(2006)
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135.
      Tissue: Liver.
    10. "Proteomics characterization of extracellular space components in the human aorta."
      Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.
      Mol. Cell. Proteomics 9:2048-2062(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    11. "Agrin binds to the N-terminal region of Lrp4 protein and stimulates association between Lrp4 and the first immunoglobulin-like domain in muscle-specific kinase (MuSK)."
      Zhang W., Coldefy A.S., Hubbard S.R., Burden S.J.
      J. Biol. Chem. 286:40624-40630(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP4, FUNCTION.
    12. "C-terminal Agrin Fragment as a potential marker for sarcopenia caused by degeneration of the neuromuscular junction."
      Drey M., Sieber C.C., Bauer J.M., Uter W., Dahinden P., Fariello R.G., Vrijbloed J.W.
      Exp. Gerontol. 48:76-80(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: POTENTIAL USAGE AS A BIOMARKER FOR SARCOPENIA.
    13. Cited for: VARIANT LGM ARG-1709, VARIANTS LEU-23; ASN-58; ILE-105; MET-267; SER-375; VAL-728; ARG-852; MET-984; PHE-1088; LYS-1118; ARG-1135; LEU-1240; ARG-1341; LEU-1451; THR-1514; HIS-1565; ILE-1666; GLN-1671; PRO-1698; HIS-1734; ASN-1789 AND VAL-2045, FUNCTION, CHARACTERIZATION OF VARIANT LGM ARG-1709.
    14. "LG2 agrin mutation causing severe congenital myasthenic syndrome mimics functional characteristics of non-neural (z-) agrin."
      Maselli R.A., Fernandez J.M., Arredondo J., Navarro C., Ngo M., Beeson D., Cagney O., Williams D.C., Wollmann R.L., Yarov-Yarovoy V., Ferns M.J.
      Hum. Genet. 131:1123-1135(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LGM PHE-1727, INTERACTION WITH DAG1, CHARACTERIZATION OF PHE-1727.

    Entry informationi

    Entry nameiAGRIN_HUMAN
    AccessioniPrimary (citable) accession number: O00468
    Secondary accession number(s): Q5SVA1
    , Q5SVA2, Q60FE1, Q7KYS8, Q8N4J5, Q96IC1, Q9BTD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2004
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 139 of the entry and version 5 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

    Miscellaneous

    Cleaved C-terminal fragments may be used as a biomarker for sarcopenia, age-related progressive loss of skeletal muscle.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3