Insulin-like growth factor 1 receptor precursor

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Q60751 (IGF1R_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Insulin-like growth factor 1 receptor
EC=2.7.10.1

Alternative name(s):
Insulin-like growth factor I receptor
Short name=IGF-I receptor
CD_antigen=CD221

Cleaved into the following 2 chains:

Insulin-like growth factor 1 receptor alpha chain
Insulin-like growth factor 1 receptor beta chain

Gene names

Name:

Igf1r

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R By similarity. When present in a hybrid receptor with INSR, binds IGF1 By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Activated by autophosphorylation at Tyr-1163, Tyr-1167 and Tyr-1168 on the kinase activation loop; phosphorylation at all three tyrosine residues is required for optimal kinase activity. Inhibited by MSC1609119A-1, BMS-754807, PQIP, benzimidazole pyridinone, isoquinolinedione, bis-azaindole, 3-cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine, pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin (PPP), tyrphostin derivatives. While most inhibitors bind to the ATP binding pocket, MSC1609119A-1 functions as allosteric inhibitor and binds close to the DFG motif and the activation loop By similarity. Ref.5
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1167 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1163 and Tyr-1168. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1163, Tyr-1167 and Tyr-1168) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is required for IRS1- and SHC1-binding By similarity. Dephosphorylated by PTPN1. Polyubiquitinated at Lys-1170 and Lys-1173 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation By similarity.
Disruption phenotype	Deficient mice are 45% of the size of wild-type littermates at birth, and die shortly due to severe organ hypoplasia. Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 3 fibronectin type-III domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from electronic annotation. Source: Compara brain development Inferred from mutant phenotype PubMed 12904469. Source: MGI establishment of cell polarity Inferred from electronic annotation. Source: Compara exocrine pancreas development Inferred from mutant phenotype PubMed 12101187. Source: MGI immune response Inferred from electronic annotation. Source: Compara inactivation of MAPKK activity Inferred from electronic annotation. Source: Compara male sex determination Inferred from mutant phenotype PubMed 14628051. Source: MGI mammary gland development Inferred from mutant phenotype PubMed 17662267. Source: MGI negative regulation of MAPK cascade Inferred from mutant phenotype PubMed 18451178. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 18451178. Source: MGI phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from mutant phenotype PubMed 18451178. Source: MGI positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cytokinesis Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 18451178. Source: MGI positive regulation of steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara prostate gland epithelium morphogenesis Inferred from mutant phenotype PubMed 18451178. Source: MGI protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from sequence or structural similarity. Source: UniProtKB regulation of JNK cascade Inferred from electronic annotation. Source: Compara response to vitamin E Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 18451178. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW insulin binding Inferred from electronic annotation. Source: Compara insulin receptor substrate binding Inferred from sequence or structural similarity. Source: UniProtKB insulin-like growth factor binding Inferred from sequence or structural similarity. Source: UniProtKB insulin-like growth factor-activated receptor activity Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol 3-kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

Potential

Chain

31 – 737

707

Insulin-like growth factor 1 receptor alpha chain

PRO_0000016683

Chain

742 – 1373

632

Insulin-like growth factor 1 receptor beta chain

PRO_0000016684

Regions

Topological domain

742 – 936

195

Extracellular Potential

Transmembrane

937 – 960

Helical; Potential

Topological domain

961 – 1373

413

Cytoplasmic By similarity

Domain

489 – 607

119

Fibronectin type-III 1

Domain

612 – 690

Fibronectin type-III 2

Domain

832 – 927

Fibronectin type-III 3

Domain

1000 – 1276

277

Protein kinase

Nucleotide binding

1006 – 1014

ATP By similarity

Motif

978 – 981

IRS1- and SHC1-binding By similarity

Sites

Active site

1137

Proton acceptor By similarity

Binding site

1034

ATP By similarity

Amino acid modifications

Modified residue

981

Phosphotyrosine By similarity

Modified residue

1163

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1167

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1168

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1345

Phosphoserine By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

102

N-linked (GlcNAc...) Potential

Glycosylation

135

N-linked (GlcNAc...) Potential

Glycosylation

245

N-linked (GlcNAc...) Potential

Glycosylation

314

N-linked (GlcNAc...) Potential

Glycosylation

418

N-linked (GlcNAc...) Potential

Glycosylation

439

N-linked (GlcNAc...) Potential

Glycosylation

535

N-linked (GlcNAc...) Potential

Glycosylation

608

N-linked (GlcNAc...) Potential

Glycosylation

623

N-linked (GlcNAc...) Potential

Glycosylation

639

N-linked (GlcNAc...) Ref.7

Glycosylation

641

N-linked (GlcNAc...) Ref.7

Glycosylation

748

N-linked (GlcNAc...) Ref.6

Glycosylation

757

N-linked (GlcNAc...) Ref.7

Glycosylation

765

N-linked (GlcNAc...) Ref.7

Glycosylation

901

N-linked (GlcNAc...) Ref.6

Glycosylation

914

N-linked (GlcNAc...) Potential

Disulfide bond

33 ↔ 52

By similarity

Disulfide bond

150 ↔ 178

By similarity

Disulfide bond

182 ↔ 205

By similarity

Disulfide bond

192 ↔ 211

By similarity

Disulfide bond

215 ↔ 224

By similarity

Disulfide bond

219 ↔ 230

By similarity

Disulfide bond

231 ↔ 239

By similarity

Disulfide bond

235 ↔ 248

By similarity

Disulfide bond

251 ↔ 260

By similarity

Disulfide bond

264 ↔ 276

By similarity

Disulfide bond

282 ↔ 303

By similarity

Disulfide bond

307 ↔ 321

By similarity

Disulfide bond

324 ↔ 328

By similarity

Disulfide bond

332 ↔ 354

By similarity

Disulfide bond

456 ↔ 489

By similarity

Cross-link

1170

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

1173

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict

58 – 59

FL → LV in AAC52123. Ref.2

Sequence conflict

260

C → S in AAC52123. Ref.2

Sequence conflict

301

D → G in AAC52123. Ref.2

Sequence conflict

306

E → V in AAC52123. Ref.2

Sequence conflict

324

C → S in AAC52123. Ref.2

Sequence conflict

1134

V → I in AAA40013. Ref.3

Sequence conflict

1145

V → D in AAA40013. Ref.3

Sequence conflict

1202

V → I in AAA40013. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q60751 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 5EE3B72EF101E379
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FASTA

1,373

155,788

        10         20         30         40         50         60 
MKSGSGGGSP TSLWGLVFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGFLH 

        70         80         90        100        110        120 
ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVIF 

       130        140        150        160        170        180 
EMTNLKDIGL YNLRNITRGA IRIEKNADLC YLSTIDWSLI LDAVSNNYIV GNKPPKECGD 

       190        200        210        220        230        240 
LCPGTLEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSVCG KRACTENNEC CHPECLGSCH 

       250        260        270        280        290        300 
TPDDNTTCVA CRHYYYKGVC VPACPPGTYR FEGWRCVDRD FCANIPNAES SDSDGFVIHD 

       310        320        330        340        350        360 
DECMQECPSG FIRNSTQSMY CIPCEGPCPK VCGDEEKKTK TIDSVTSAQM LQGCTILKGN 

       370        380        390        400        410        420 
LLINIRRGNN IASELENFMG LIEVVTGYVK IRHSHALVSL SFLKNLRLIL GEEQLEGNYS 

       430        440        450        460        470        480 
FYVLDNQNLQ QLWDWNHRNL TVRSGKMYFA FNPKLCVSEI YRMEEVTGTK GRQSKGDINT 

       490        500        510        520        530        540 
RNNGERASCE SDVLRFTSTT TWKNRIIITW HRYRPPDYRD LISFTVYYKE APFKNVTEYD 

       550        560        570        580        590        600 
GQDACGSNSW NMVDVDLPPN KEGEPGILLH GLKPWTQYAV YVKAVTLTMV ENDHIRGAKS 

       610        620        630        640        650        660 
EILYIRTNAS VPSIPLDVLS ASNSSSQLIV KWNPPTLPNG NLSYYIVRWQ RQPQDGYLYR 

       670        680        690        700        710        720 
HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC CACPKTEAEK QAEKEEAEYR 

       730        740        750        760        770        780 
KVFENFLHNS IFVPRPERRR RDVMQVANTT MSSRSRNTTV ADTYNITDPE EFETEYPFFE 

       790        800        810        820        830        840 
SRVDNKERTV ISNLRPFTLY RIDIHSCNHE AEKLGCSASN FVFARTMPAE GADDIPGPVT 

       850        860        870        880        890        900 
WEPRPENSIF LKWPEPENPN GLILMYEIKY GSQVEDQREC VSRQEYRKYG GAKLNRLNPG 

       910        920        930        940        950        960 
NYTARIQATS LSGNGSWTDP VFFYVPAKTT YENFMHLIIA LPVAILLIVG GLVIMLYVFH 

       970        980        990       1000       1010       1020 
RKRNNSRLGN GVLYASVNPE YFSAADVYVP DEWEVAREKI TMNRELGQGS FGMVYEGVAK 

      1030       1040       1050       1060       1070       1080 
GVVKDEPETR VAIKTVNEAA SMRERIEFLN EASVMKEFNC HHVVRLLGVV SQGQPTLVIM 

      1090       1100       1110       1120       1130       1140 
ELMTRGDLKS YLRSLRPEVE QNNLVLIPPS LSKMIQMAGE IADGMAYLNA NKFVHRDLAA 

      1150       1160       1170       1180       1190       1200 
RNCMVAEDFT VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MSPESLKDGV FTTHSDVWSF 

      1210       1220       1230       1240       1250       1260 
GVVLWEIATL AEQPYQGLSN EQVLRFVMEG GLLDKPDNCP DMLFELMRMC WQYNPKMRPS 

      1270       1280       1290       1300       1310       1320 
FLEIIGSIKD EMEPSFQEVS FYYSEENKPP EPEELEMELE MEPENMESVP LDPSASSASL 

      1330       1340       1350       1360       1370 
PLPERHSGHK AENGPGPGVL VLRASFDERQ PYAHMNGGRA NERALPLPQS STC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA for the mouse insulin-like growth factor I receptor." Navarro M., Garandel V., Barenton B., Bernardi H. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of cDNA for the alpha subunit of mouse insulin-like growth factor I receptor and the role of the receptor in metanephric development." Wada J., Liu Z.Z., Alvares K., Kumar A., Wallner E.I., Makino H., Kanwar Y.S. Proc. Natl. Acad. Sci. U.S.A. 90:10360-10364(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-329. Strain: CD-1. Tissue: Kidney.
[3]	"The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family." Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J. Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1134-1203.
[4]	"Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)." Liu J.P., Baker J., Perkins A.S., Robertson E.J., Efstratiadis A. Cell 75:59-72(1993) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[5]	"Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts." Buckley D.A., Cheng A., Kiely P.A., Tremblay M.L., O'Connor R. Mol. Cell. Biol. 22:1998-2010(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[6]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-748 AND ASN-901, MASS SPECTROMETRY. Tissue: Myoblast.
[7]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-639; ASN-641; ASN-757 AND ASN-765, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF056187 mRNA. Translation: AAC12782.1. U00182 mRNA. Translation: AAC52123.1. M33422 mRNA. Translation: AAA40013.1.
IPI	IPI00120225.
PIR	A48805. JH0113.
RefSeq	NP_034643.2. NM_010513.2.
UniGene	Mm.275742.
3D structure databases
ProteinModelPortal	Q60751.
SMR	Q60751. Positions 30-652, 785-828, 848-1288.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-219894.
PTM databases
PhosphoSite	Q60751.
Proteomic databases
PaxDb	Q60751.
PRIDE	Q60751.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	16001.
KEGG	mmu:16001.
UCSC	uc009hja.1. mouse.
Organism-specific databases
CTD	3480.
MGI	MGI:96433. Igf1r.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000038045.
HOVERGEN	HBG006134.
InParanoid	Q60751.
KO	K05087.
OrthoDB	EOG4Z62MR.
Enzyme and pathway databases
BRENDA	2.7.10.1. 3474.
Gene expression databases
ArrayExpress	Q60751.
Bgee	Q60751.
CleanEx	MM_IGF1R.
Genevestigator	Q60751.
GermOnline	ENSMUSG00000005533. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 4 hits.
InterPro	IPR000494. EGF_rcpt_L. IPR003961. Fibronectin_type3. IPR006211. Furin-like_Cys-rich_dom. IPR006212. Furin_repeat. IPR009030. Growth_fac_rcpt. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016246. Tyr_kinase_insulin-like_rcpt. IPR002011. Tyr_kinase_rcpt_2_CS. [Graphical view]
Pfam	PF00041. fn3. 1 hit. PF00757. Furin-like. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF01030. Recep_L_domain. 2 hits. [Graphical view]
PIRSF	PIRSF000620. Insulin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00060. FN3. 3 hits. SM00261. FU. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 3 hits. SSF57184. Grow_fac_recept. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS50853. FN3. 3 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS00239. RECEPTOR_TYR_KIN_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q60751.
ChEMBL	CHEMBL5381.
ChiTaRS	IGF1R. mouse.
NextBio	288790.
SOURCE	Search...

Entry information

Entry name

IGF1R_MOUSE

Accession

Primary (citable) accession number: Q60751
Secondary accession number(s): O70438, Q62123

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 11, 2001
Last modified:	May 1, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents