[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CBL. DOI=10.1006/bbrc.2000.2147; PubMed=10679202 [NCBI, ExPASy, EBI, Israel, Japan] Take H., Watanabe S., Takeda K., Yu Z.-X., Iwata N., Kajigaya S.; "Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl."; Biochem. Biophys. Res. Commun. 268:321-328(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=T-cell; DOI=10.1093/intimm/dxg032; PubMed=12618476 [NCBI, ExPASy, EBI, Israel, Japan] Tibaldi E.V., Reinherz E.L.; "CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the same CD2 cytoplasmic segment but elicit divergent functional activities."; Int. Immunol. 15:313-329(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Adrenal cortex, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, AND VARIANT LEU-382. PubMed=11474197 [NCBI, ExPASy, EBI, Israel, Japan] Narita T., Amano F., Yoshizaki K., Nishimoto N., Nishimura T., Tajima T., Namiki H., Taniyama T.; "Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in situ hybridization."; Cytogenet. Cell Genet. 93:133-134(2001).
[5]	INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, AND SELF-ASSOCIATION. DOI=10.1006/bbrc.2000.3760; PubMed=11071869 [NCBI, ExPASy, EBI, Israel, Japan] Watanabe S., Take H., Takeda K., Yu Z.X., Iwata N., Kajigaya S.; "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes."; Biochem. Biophys. Res. Commun. 278:167-174(2000).
[6]	INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC, FUNCTION IN RECEPTOR INTERNALIZATION, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M205535200; PubMed=12177062 [NCBI, ExPASy, EBI, Israel, Japan] Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S., Dikic I.; "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases."; J. Biol. Chem. 277:39666-39672(2002).
[7]	FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1; SH3GL2; SH3GL3 AND CBL, AND SUBCELLULAR LOCATZION. DOI=10.1038/416183a; PubMed=11894095 [NCBI, ExPASy, EBI, Israel, Japan] Soubeyran P., Kowanetz K., Szymkiewicz I., Langdon W.Y., Dikic I.; "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors."; Nature 416:183-187(2002).
[8]	FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH SH3GL1; SH3GL2; SH3GL3; CBL AND MET. DOI=10.1038/416187a; PubMed=11894096 [NCBI, ExPASy, EBI, Israel, Japan] Petrelli A., Gilestro G.F., Lanzardo S., Comoglio P.M., Migone N., Giordano S.; "The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met."; Nature 416:187-190(2002).
[9]	UBIQUITINATION BY CBL AND CBLB. DOI=10.1073/pnas.192462299; PubMed=12218189 [NCBI, ExPASy, EBI, Israel, Japan] Haglund K., Shimokawa N., Szymkiewicz I., Dikic I.; "Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors."; Proc. Natl. Acad. Sci. U.S.A. 99:12191-12196(2002).
[10]	INTERACTION WITH DAB2, AND IDENTIFICATION IN A COMPLEX WITH DAB2 AND CLATHRIN. DOI=10.1016/S0014-5793(03)01111-6; PubMed=14596919 [NCBI, ExPASy, EBI, Israel, Japan] Kowanetz K., Terzic J., Dikic I.; "Dab2 links CIN85 with clathrin-mediated receptor internalization."; FEBS Lett. 554:81-87(2003).
[11]	FUNCTION IN CELL ADHESION, AND INTERACTION WITH PDCD6IP; PTK2 AND PTK2B. DOI=10.1242/jcs.00522; PubMed=12771190 [NCBI, ExPASy, EBI, Israel, Japan] Schmidt M.H., Chen B., Randazzo L.M., Boegler O.; "SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion."; J. Cell Sci. 116:2845-2855(2003).
[12]	INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN. DOI=10.1074/jbc.M302540200; PubMed=12690097 [NCBI, ExPASy, EBI, Israel, Japan] Hutchings N.J., Clarkson N., Chalkley R., Barclay A.N., Brown M.H.; "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85."; J. Biol. Chem. 278:22396-22403(2003).
[13]	FUNCTION IN RECEPTOR INTERNALIZATION. DOI=10.1073/pnas.1031790100; PubMed=12734385 [NCBI, ExPASy, EBI, Israel, Japan] Schmidt M.H., Furnari F.B., Cavenee W.K., Bogler O.; "Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization."; Proc. Natl. Acad. Sci. U.S.A. 100:6505-6510(2003).
[14]	FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH DDEF1; CENTD3; HIP1R; SYNJ2; INPP5D; STAP1 AND EGFR, IDENTIFICATION IN A COMPLEX WITH DDEF1 AND CENTD3, AND SUBCELLULAR LOCATION. DOI=10.1091/mbc.E03-09-0683; PubMed=15090612 [NCBI, ExPASy, EBI, Israel, Japan] Kowanetz K., Husnjak K., Holler D., Kowanetz M., Soubeyran P., Hirsch D., Schmidt M.H., Pavelic K., De Camilli P., Randazzo P.A., Dikic I.; "CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors."; Mol. Biol. Cell 15:3155-3166(2004).
[15]	INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB. DOI=10.1128/MCB.24.20.8981-8993.2004; PubMed=15456872 [NCBI, ExPASy, EBI, Israel, Japan] Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I., Bogler O.; "Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex."; Mol. Cell. Biol. 24:8981-8993(2004).
[16]	FUNCTION, AND INTERACTION WITH MAP3K4. DOI=10.1016/j.bbrc.2005.10.032; PubMed=16256071 [NCBI, ExPASy, EBI, Israel, Japan] Aissouni Y., Zapart G., Iovanna J.L., Dikic I., Soubeyran P.; "CIN85 regulates the ability of MEKK4 to activate the p38 MAP kinase pathway."; Biochem. Biophys. Res. Commun. 338:808-814(2005).
[17]	INTERACTION WITH SPRY2. DOI=10.1038/sj.embor.7400453; PubMed=15962011 [NCBI, ExPASy, EBI, Israel, Japan] Haglund K., Schmidt M.H., Wong E.S., Guy G.R., Dikic I.; "Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation."; EMBO Rep. 6:635-641(2005).
[18]	FUNCTION IN APOPTOSIS, AND INTERACTION WITH SRC; LCK; LYN; FGR; FYN; HCK; TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1. DOI=10.1016/j.yexcr.2004.11.005; PubMed=15707590 [NCBI, ExPASy, EBI, Israel, Japan] Narita T., Nishimura T., Yoshizaki K., Taniyama T.; "CIN85 associates with TNF receptor 1 via Src and modulates TNF-alpha-induced apoptosis."; Exp. Cell Res. 304:256-264(2005).
[19]	FUNCTION IN RECEPTOR INTERNALIZATION. PubMed=16177060 [NCBI, ExPASy, EBI, Israel, Japan] Molfetta R., Belleudi F., Peruzzi G., Morrone S., Leone L., Dikic I., Piccoli M., Frati L., Torrisi M.R., Santoni A., Paolini R.; "CIN85 regulates the ligand-dependent endocytosis of the IgE receptor: a new molecular mechanism to dampen mast cell function."; J. Immunol. 175:4208-4216(2005).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASS SPECTROMETRY. DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.-E., Tannenbaum S.R., White F.M.; "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; J. Proteome Res. 4:1339-1346(2005).
[21]	INTERACTION WITH ARHGAP17. DOI=10.1016/j.cell.2006.02.045; PubMed=16678097 [NCBI, ExPASy, EBI, Israel, Japan] Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.; "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."; Cell 125:535-548(2006).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-509 AND SER-511, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[23]	INTERACTION WITH DDN AND MAGI2, AND SUBCELLULAR LOCATION. DOI=10.1093/jb/mvj105; PubMed=16751601 [NCBI, ExPASy, EBI, Israel, Japan] Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.; "CIN85 is localized at synapses and forms a complex with S-SCAM via dendrin."; J. Biochem. 139:931-939(2006).
[24]	INTERACTION WITH FAM125A. DOI=10.1074/jbc.M605693200; PubMed=16895919 [NCBI, ExPASy, EBI, Israel, Japan] Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H.; "CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."; J. Biol. Chem. 281:28919-28931(2006).
[25]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB. DOI=10.1038/nsmb1000; PubMed=16228008 [NCBI, ExPASy, EBI, Israel, Japan] Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D., Groemping Y., Dikic I., Rittinger K., Bravo J.; "Cbl promotes clustering of endocytic adaptor proteins."; Nat. Struct. Mol. Biol. 12:972-979(2005).

Comments

FUNCTION: Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis.
SUBUNIT: Can self-associate and form homotetramers. Interacts with CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, MAGI2, CRK, BCAR1, SOS1, DDEF1, CENTD3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with CBL and CBLB, but does not interact with CBLC. Two molecules of SH3KBP1 seem to bind through their respective SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is increased upon EGF stimulation. The interaction with CBL is attenuated by PDCD6IP. Interacts through its proline-rich region with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex seems to associate with a complex containing the phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably associates with DDEF1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, DDEF1 and CENTD3. Interacts with focal adhesion kinases PTK2 AND PTK2B, probably as a dimer. Interacts with DAB2 and probably associates with chathrin through its interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1 following growth factor treatment, enabling interaction with CBL. Interacts with DDN and probably associates with MAGI2 through its interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-associated complex upon stimulation with TNF-alpha seems to be mediated by SRC. Probably interacts with SH3KBP1.
INTERACTION:
P08631:HCK; NbExp=1; IntAct=EBI-346595, EBI-346340;
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junction, synapse, synaptosome. Cell junction, focal adhesion (By similarity). Note=Localized in endocytic vesicles containing clustered receptors. Colocalizes with DDEF1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions (By similarity). Colocalized with MAGI2 in synaptosomes (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q96B97-1
Note: Interacts with CBL.
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q96B97-2
Note: Interacts with CD2 cytoplasmic tail and does not interact with F-actin.
Features which should be applied to build the isoform sequence: VSP_007504.

TISSUE SPECIFICITY: Ubiquitously expressed. Also expressed in some cancer cell lines.
DOMAIN: The SH3 domains mediate interaction with SHKBP1 (By similarity).
PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus.
SIMILARITY: Contains 3 SH3 domains.
SEQUENCE CAUTION:
- Sequence=AAH50663.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF230904; AAF37854.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF542051; AAN77231.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015806; AAH15806.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050663; AAH50663.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF329267; AAK95587.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF329268; AAO13348.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC7191; JC7191.

RefSeq

NP_001019837.1; -.
NP_114098.1; -.

UniGene

Hs.444770

3D structure databases

PDB

2BZ8; X-ray; 2.00 A; A/B=1-58.	[ExPASy / RCSB / EBI]
2O2O; NMR; -; A=92-168.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

2BZ8; -.
2O2O; -.

Q96B97; 264-326.

Protein-protein interaction databases

IntAct

Q96B97; -.

PTM databases

PhosphoSite

Q96B97; -.

Organism-specific databases

HIX0021848; -.

HGNC:13867; SH3KBP1.

HPA003351; -.
HPA003355; -.

MIM

300374; gene. [NCBI / EBI]

PharmGKB

PA37822; -.

GeneCards

Q96B97.

Gene expression databases

ArrayExpress

Q96B97; -.

CleanEx

HS_SH3KBP1; -.

GermOnline

ENSG00000147010; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007267;	Biological process: cell-cell signaling (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000108; Neu_cyt_fact_2.
IPR001452; SH3.
Graphical view of domain structure.

Pfam

PF00018; SH3_1; 3.
Pfam graphical view of domain structure.

PRINTS

PR00499; P67PHOX.
PR00452; SH3DOMAIN.

ProDom

PD000066; SH3; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00326; SH3; 3.
SMART graphical view of domain structure.

PROSITE

PS50002; SH3; 3.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q96B97.

Genome annotation databases

Ensembl

ENSG00000147010; Homo sapiens. [Contig view]

GeneID

30011; -.

KEGG

hsa:30011; -.

NMPDR

fig|9606.3.peg.32531; -.

Phylogenomic databases

HOGENOM

Q96B97; -.

HOVERGEN

Q96B97; -.

Other

SOURCE

SH3KBP1; Homo sapiens.

ProtoNet

Q96B97.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Apoptosis; Cell junction; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Membrane; Phosphoprotein; Polymorphism; Repeat; SH3 domain; SH3-binding; Synapse; Synaptosome; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 665`	`665`	`SH3 domain-containing kinase-binding protein 1.`	`PRO_0000097728`
`DOMAIN`	`1 58`	`58`	`SH3 1.`
`DOMAIN`	`98 157`	`60`	`SH3 2.`
`DOMAIN`	`267 328`	`62`	`SH3 3.`
`COILED`	`602 664`	`63`	`Potential.`
`COMPBIAS`	`327 428`	`102`	`Pro-rich.`
`MOD_RES`	`156 156`		`Phosphoserine (By similarity).`
`MOD_RES`	`230 230`		`Phosphoserine.`
`MOD_RES`	`509 509`		`Phosphoserine.`
`MOD_RES`	`511 511`		`Phosphoserine.`
`MOD_RES`	`587 587`		`Phosphoserine.`
`VAR_SEQ`	`1 54`		`MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQ` `INGRRGLFPDNFVR -> MEVSAAKAPSAADLSEI (in isoform 2).`	`VSP_007504`
`VARIANT`	`382 382`	`1`	`P -> L.`	`VAR_015667`
`CONFLICT`	`570 570`		`A -> V (in Ref. 3; AAH15806).`
`STRAND`	`4 8`	`5`
`STRAND`	`25 30`	`6`
`TURN`	`33 35`	`3`
`STRAND`	`36 41`	`6`
`STRAND`	`44 49`	`6`
`HELIX`	`50 52`	`3`
`STRAND`	`53 55`	`3`
`STRAND`	`102 105`	`4`
`STRAND`	`113 115`	`3`
`STRAND`	`124 126`	`3`
`HELIX`	`130 132`	`3`
`STRAND`	`149 153`	`5`
`TURN`	`161 164`	`4`

Sequence information

Length: 665 AA [This is the length of the unprocessed precursor]

Molecular weight: 73126 Da [This is the MW of the unprocessed precursor]

CRC64: 3BD350FCDB14BD4C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEAIVEFDY QAQHDDELTI SVGEIITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKEM 

        70         80         90        100        110        120 
KKDPLTNKAP EKPLHEVPSG NSLLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK 

       130        140        150        160        170        180 
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSSLRETTG 

       190        200        210        220        230        240 
SESDGGDSSS TKSEGANGTV ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV 

       250        260        270        280        290        300 
EKTIGKKLPA TTATPDSSKT EMDSRTKSKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD 

       310        320        330        340        350        360 
CIDVGWWEGE LNGRRGVFPD NFVKLLPPDF EKEGNRPKKP PPPSAPVIKQ GAGTTERKHE 

       370        380        390        400        410        420 
IKKIPPERPE MLPNRTEEKE RPEREPKLDL QKPSVPAIPP KKPRPPKTNS LSRPGALPPR 

       430        440        450        460        470        480 
RPERPVGPLT HTRGDSPKID LAGSSLSGIL DKDLSDRSND IDLEGFDSVV SSTEKLSHPT 

       490        500        510        520        530        540 
TSRPKATGRR PPSQSLTSSS LSSPDIFDSP SPEEDKEEHI SLAHRGVDAS KKTSKTVTIS 

       550        560        570        580        590        600 
QVSDNKASLP PKPGTMAAGG GGPAPLSSAA PSPLSSSLGT AGHRANSPSL FGTEGKPKME 

       610        620        630        640        650        660 
PAASSQAAVE ELRTQVRELR SIIETMKDQQ KREIKQLLSE LDEEKKIRLR LQMEVNDIKK 


ALQSK

Q96B97 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools