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O00468

- AGRIN_HUMAN

UniProt

O00468 - AGRIN_HUMAN

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Protein

Agrin

Gene

AGRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. sialic acid binding Source: UniProtKB
  8. 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
Complete GO annotation...

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.
REACT_267654. Defective EXT2 causes exostoses 2.
REACT_267659. Defective B3GAT3 causes JDSSDHD.
REACT_267674. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_267711. Defective B4GALT7 causes EDS, progeroid type.
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: UniProtKB
  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
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Myasthenic syndrome, congenital, with pre- and postsynaptic defects (CMSPPD) [MIM:615120]: A form of congenital myasthenic syndrome, a group of genetic disorders characterized by failure of neuromuscular transmission, weakness and easy fatigability. CMSPPD is an autosomal recessive disease characterized by prominent defects of both the pre- and postsynaptic regions. Affected individuals have onset of muscle weakness in early childhood; the severity of the weakness and muscles affected is variable.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761G → S in CMSPPD; results in decreased AChR clustering. 1 Publication
VAR_071367
Natural varianti105 – 1051N → I in CMSPPD; results in decreased AChR clustering. 2 Publications
VAR_068726
Natural varianti1709 – 17091G → R in CMSPPD; 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 CMSPPD; 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 varianti1875 – 18751G → R in CMSPPD. 1 Publication
VAR_071369

Keywords - Diseasei

Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

MIMi615120. phenotype.
Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
98914. Presynaptic 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

BgeeiO00468.
CleanExiHS_AGRN.
ExpressionAtlasiO00468. baseline and differential.
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. 9 interactions.
IntActiO00468. 7 interactions.
MINTiMINT-4053526.
STRINGi9606.ENSP00000368678.

Structurei

3D structure databases

ProteinModelPortaliO00468.
SMRiO00468. Positions 36-146, 170-751, 793-921, 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.
GeneTreeiENSGT00530000063501.
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.
IPR013320. ConA-like_dom.
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

        10         20         30         40         50
MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT
60 70 80 90 100
VEEILNVDPV QHTYSCKVRV WRYLKGKDLV ARESLLDGGN KVVISGFGDP
110 120 130 140 150
LICDNQVSTG DTRIFFVNPA PPYLWPAHKN ELMLNSSLMR ITLRNLEEVE
160 170 180 190 200
FCVEDKPGTH FTPVPPTPPD ACRGMLCGFG AVCEPNAEGP GRASCVCKKS
210 220 230 240 250
PCPSVVAPVC GSDASTYSNE CELQRAQCSQ QRRIRLLSRG PCGSRDPCSN
260 270 280 290 300
VTCSFGSTCA RSADGLTASC LCPATCRGAP EGTVCGSDGA DYPGECQLLR
310 320 330 340 350
RACARQENVF KKFDGPCDPC QGALPDPSRS CRVNPRTRRP EMLLRPESCP
360 370 380 390 400
ARQAPVCGDD GVTYENDCVM GRSGAARGLL LQKVRSGQCQ GRDQCPEPCR
410 420 430 440 450
FNAVCLSRRG RPRCSCDRVT CDGAYRPVCA QDGRTYDSDC WRQQAECRQQ
460 470 480 490 500
RAIPSKHQGP CDQAPSPCLG VQCAFGATCA VKNGQAACEC LQACSSLYDP
510 520 530 540 550
VCGSDGVTYG SACELEATAC TLGREIQVAR KGPCDRCGQC RFGALCEAET
560 570 580 590 600
GRCVCPSECV ALAQPVCGSD GHTYPSECML HVHACTHQIS LHVASAGPCE
610 620 630 640 650
TCGDAVCAFG AVCSAGQCVC PRCEHPPPGP VCGSDGVTYG SACELREAAC
660 670 680 690 700
LQQTQIEEAR AGPCEQAECG SGGSGSGEDG DCEQELCRQR GGIWDEDSED
710 720 730 740 750
GPCVCDFSCQ SVPGSPVCGS DGVTYSTECE LKKARCESQR GLYVAAQGAC
760 770 780 790 800
RGPTFAPLPP VAPLHCAQTP YGCCQDNITA ARGVGLAGCP SACQCNPHGS
810 820 830 840 850
YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG RSGCTPCSCD
860 870 880 890 900
PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPAG CEADASAPAT
910 920 930 940 950
CAEMRCEFGA RCVEESGSAH CVCPMLTCPE ANATKVCGSD GVTYGNECQL
960 970 980 990 1000
KTIACRQGLQ ISIQSLGPCQ EAVAPSTHPT SASVTVTTPG LLLSQALPAP
1010 1020 1030 1040 1050
PGALPLAPSS TAHSQTTPPP SSRPRTTASV PRTTVWPVLT VPPTAPSPAP
1060 1070 1080 1090 1100
SLVASAFGES GSTDGSSDEE LSGDQEASGG GSGGLEPLEG SSVATPGPPV
1110 1120 1130 1140 1150
ERASCYNSAL GCCSDGKTPS LDAEGSNCPA TKVFQGVLEL EGVEGQELFY
1160 1170 1180 1190 1200
TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFRSVR LRDLGPGKSV
1210 1220 1230 1240 1250
RAIVDVHFDP TTAFRAPDVA RALLRQIQVS RRRSLGVRRP LQEHVRFMDF
1260 1270 1280 1290 1300
DWFPAFITGA TSGAIAAGAT ARATTASRLP SSAVTPRAPH PSHTSQPVAK
1310 1320 1330 1340 1350
TTAAPTTRRP PTTAPSRVPG RRPPAPQQPP KPCDSQPCFH GGTCQDWALG
1360 1370 1380 1390 1400
GGFTCSCPAG RGGAVCEKVL GAPVPAFEGR SFLAFPTLRA YHTLRLALEF
1410 1420 1430 1440 1450
RALEPQGLLL YNGNARGKDF LALALLDGRV QLRFDTGSGP AVLTSAVPVE
1460 1470 1480 1490 1500
PGQWHRLELS RHWRRGTLSV DGETPVLGES PSGTDGLNLD TDLFVGGVPE
1510 1520 1530 1540 1550
DQAAVALERT FVGAGLRGCI RLLDVNNQRL ELGIGPGAAT RGSGVGECGD
1560 1570 1580 1590 1600
HPCLPNPCHG GAPCQNLEAG RFHCQCPPGR VGPTCADEKS PCQPNPCHGA
1610 1620 1630 1640 1650
APCRVLPEGG AQCECPLGRE GTFCQTASGQ DGSGPFLADF NGFSHLELRG
1660 1670 1680 1690 1700
LHTFARDLGE KMALEVVFLA RGPSGLLLYN GQKTDGKGDF VSLALRDRRL
1710 1720 1730 1740 1750
EFRYDLGKGA AVIRSREPVT LGAWTRVSLE RNGRKGALRV GDGPRVLGES
1760 1770 1780 1790 1800
PKSRKVPHTV LNLKEPLYVG GAPDFSKLAR AAAVSSGFDG AIQLVSLGGR
1810 1820 1830 1840 1850
QLLTPEHVLR QVDVTSFAGH PCTRASGHPC LNGASCVPRE AAYVCLCPGG
1860 1870 1880 1890 1900
FSGPHCEKGL VEKSAGDVDT LAFDGRTFVE YLNAVTESEL ANEIPVPETL
1910 1920 1930 1940 1950
DSGALHEKAL QSNHFELSLR TEATQGLVLW SGKATERADY VALAIVDGHL
1960 1970 1980 1990 2000
QLSYNLGSQP VVLRSTVPVN TNRWLRVVAH REQREGSLQV GNEAPVTGSS
2010 2020 2030 2040 2050
PLGATQLDTD GALWLGGLPE LPVGPALPKA YGTGFVGCLR DVVVGRHPLH
2060
LLEDAVTKPE LRPCPTP
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 varianti76 – 761G → S in CMSPPD; results in decreased AChR clustering. 1 Publication
VAR_071367
Natural varianti105 – 1051N → I in CMSPPD; results in decreased AChR clustering. 2 Publications
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 varianti745 – 7451A → V.1 Publication
VAR_071368
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 CMSPPD; 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 CMSPPD; 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 varianti1875 – 18751G → R in CMSPPD. 1 Publication
VAR_071369
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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, 1320-2067.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 132000. 9 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.
615120. phenotype.
neXtProti NX_O00468.
Orphaneti 98913. Postsynaptic congenital myasthenic syndromes.
98914. Presynaptic congenital myasthenic syndromes.
PharmGKBi PA24626.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312635.
GeneTreei ENSGT00530000063501.
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.
REACT_267654. Defective EXT2 causes exostoses 2.
REACT_267659. Defective B3GAT3 causes JDSSDHD.
REACT_267674. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_267711. Defective B4GALT7 causes EDS, progeroid type.
SignaLinki O00468.

Miscellaneous databases

ChiTaRSi AGRN. human.
GeneWikii Agrin.
GenomeRNAii 375790.
NextBioi 100617.
PROi O00468.
SOURCEi Search...

Gene expression databases

Bgeei O00468.
CleanExi HS_AGRN.
ExpressionAtlasi O00468. baseline and differential.
Genevestigatori O00468.

Family and domain databases

Gene3Di 2.60.120.200. 3 hits.
3.30.70.960. 1 hit.
InterProi IPR004850. Agrin_NtA.
IPR013320. ConA-like_dom.
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

« Hide 'large scale' publications
  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: INVOLVEMENT IN CMSPPD, VARIANT CMSPPD 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 CMSPPD 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 CMSPPD PHE-1727, INTERACTION WITH DAG1, CHARACTERIZATION OF VARIANT CMSPPD PHE-1727.
  15. Cited for: VARIANT VAL-745, VARIANTS CMSPPD SER-76; ILE-105 AND ARG-1875, CHARACTERIZATION OF VARIANTS CMSPPD SER-76 AND ILE-105.

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: November 26, 2014
This is version 141 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