Reviewed,
UniProtKB/Swiss-Prot Q96B97 (SH3K1_HUMAN)
Last modified
July 7, 2009.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: SH3 domain-containing kinase-binding protein 1 Alternative name(s): Cbl-interacting protein of 85 kDa Human Src family kinase-binding protein 1 Short name=HSB-1 CD2-binding protein 3 Short name=CD2BP3 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 665 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (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 structure | 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, ASAP1, ARAP3, 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 ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3. 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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21 Ref.23 Ref.24 |
| 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 ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions By similarity. Colocalized with MAGI2 in synaptosomes By similarity. |
| Tissue specificity | Ubiquitously expressed. Also expressed in some cancer cell lines. |
| Domain | The SH3 domains mediate interaction with SHKBP1 By similarity. |
| Post-translational modification | Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus. |
| Sequence similarities | Contains 3 SH3 domains. |
| Sequence caution | The sequence AAH50663.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| HCK | P08631 | 1 | EBI-346595,EBI-346340 | |
| PIK3R1 | P27986 | 1 | EBI-346595,EBI-79464 |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q96B97-1) 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. | ||||||
| Note: Interacts with CBL. | ||||||
| Isoform 2 (identifier: Q96B97-2) The sequence of this isoform differs from the canonical sequence as follows: 1-54: MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNFVR → MEVSAAKAPSAADLSEI | ||||||
| Note: Interacts with CD2 cytoplasmic tail and does not interact with F-actin. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 665 | 665 | SH3 domain-containing kinase-binding protein 1 | PRO_0000097728 | ||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||
| Domain | 1 – 58 | 58 | SH3 1 | |||||||||||||||||||||||||||||
| Domain | 98 – 157 | 60 | SH3 2 | |||||||||||||||||||||||||||||
| Domain | 267 – 328 | 62 | SH3 3 | |||||||||||||||||||||||||||||
| Coiled coil | 602 – 664 | 63 | Potential | |||||||||||||||||||||||||||||
| Compositional bias | 327 – 428 | 102 | Pro-rich | |||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Modified residue | 156 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||
| Modified residue | 230 | 1 | Phosphoserine Ref.22 Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 254 | 1 | Phosphothreonine Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 436 | 1 | Phosphoserine Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 509 | 1 | Phosphoserine Ref.22 Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 511 | 1 | Phosphoserine Ref.22 Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 521 | 1 | Phosphoserine Ref.25 | |||||||||||||||||||||||||||||
| Modified residue | 587 | 1 | Phosphoserine Ref.25 Ref.20 | |||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 54 | 54 | MVEAI…DNFVR → MEVSAAKAPSAADLSEI in isoform 2. | VSP_007504 | ||||||||||||||||||||||||||||
| Natural variant | 382 | 1 | P → L Ref.4 | VAR_015667 | ||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||
| Sequence conflict | 570 | 1 | A → V in AAH15806. Ref.3 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Beta strand | 4 – 8 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 25 – 30 | 6 | ||||||||||||||||||||||||||||||
| Turn | 33 – 35 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 36 – 41 | 6 | ||||||||||||||||||||||||||||||
| Beta strand | 44 – 49 | 6 | ||||||||||||||||||||||||||||||
| Helix | 50 – 52 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 53 – 55 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 102 – 105 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 113 – 115 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 124 – 126 | 3 | ||||||||||||||||||||||||||||||
| Helix | 130 – 132 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 149 – 153 | 5 | ||||||||||||||||||||||||||||||
| Turn | 161 – 164 | 4 | ||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl." Take H., Watanabe S., Takeda K., Yu Z.-X., Iwata N., Kajigaya S. Biochem. Biophys. Res. Commun. 268:321-328(2000) [PubMed: 10679202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CBL. |
| [2] | "CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the same CD2 cytoplasmic segment but elicit divergent functional activities." Tibaldi E.V., Reinherz E.L. Int. Immunol. 15:313-329(2003) [PubMed: 12618476] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: T-cell. |
| [3] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Adrenal cortex and Uterus. |
| [4] | "Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in situ hybridization." Narita T., Amano F., Yoshizaki K., Nishimoto N., Nishimura T., Tajima T., Namiki H., Taniyama T. Cytogenet. Cell Genet. 93:133-134(2001) [PubMed: 11474197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, VARIANT LEU-382. |
| [5] | "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes." Watanabe S., Take H., Takeda K., Yu Z.X., Iwata N., Kajigaya S. Biochem. Biophys. Res. Commun. 278:167-174(2000) [PubMed: 11071869] [Abstract] Cited for: INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, SELF-ASSOCIATION. |
| [6] | "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases." Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S., Dikic I. J. Biol. Chem. 277:39666-39672(2002) [PubMed: 12177062] [Abstract] Cited for: INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC, FUNCTION IN RECEPTOR INTERNALIZATION, SUBCELLULAR LOCATION. |
| [7] | "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors." Soubeyran P., Kowanetz K., Szymkiewicz I., Langdon W.Y., Dikic I. Nature 416:183-187(2002) [PubMed: 11894095] [Abstract] Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1; SH3GL2; SH3GL3 AND CBL, SUBCELLULAR LOCATZION. |
| [8] | "The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met." Petrelli A., Gilestro G.F., Lanzardo S., Comoglio P.M., Migone N., Giordano S. Nature 416:187-190(2002) [PubMed: 11894096] [Abstract] Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH SH3GL1; SH3GL2; SH3GL3; CBL AND MET. |
| [9] | "Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors." Haglund K., Shimokawa N., Szymkiewicz I., Dikic I. Proc. Natl. Acad. Sci. U.S.A. 99:12191-12196(2002) [PubMed: 12218189] [Abstract] Cited for: UBIQUITINATION BY CBL AND CBLB. |
| [10] | "Dab2 links CIN85 with clathrin-mediated receptor internalization." Kowanetz K., Terzic J., Dikic I. FEBS Lett. 554:81-87(2003) [PubMed: 14596919] [Abstract] Cited for: INTERACTION WITH DAB2, IDENTIFICATION IN A COMPLEX WITH DAB2 AND CLATHRIN. |
| [11] | "SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion." Schmidt M.H., Chen B., Randazzo L.M., Boegler O. J. Cell Sci. 116:2845-2855(2003) [PubMed: 12771190] [Abstract] Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH PDCD6IP; PTK2 AND PTK2B. |
| [12] | "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85." Hutchings N.J., Clarkson N., Chalkley R., Barclay A.N., Brown M.H. J. Biol. Chem. 278:22396-22403(2003) [PubMed: 12690097] [Abstract] Cited for: INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN. |
| [13] | "Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization." Schmidt M.H., Furnari F.B., Cavenee W.K., Bogler O. Proc. Natl. Acad. Sci. U.S.A. 100:6505-6510(2003) [PubMed: 12734385] [Abstract] Cited for: FUNCTION IN RECEPTOR INTERNALIZATION. |
| [14] | "CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors." 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. Mol. Biol. Cell 15:3155-3166(2004) [PubMed: 15090612] [Abstract] Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH ASAP1; ARAP3; HIP1R; SYNJ2; INPP5D; STAP1 AND EGFR, IDENTIFICATION IN A COMPLEX WITH ASAP1 AND ARAP3, SUBCELLULAR LOCATION. |
| [15] | "Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex." Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I., Bogler O. Mol. Cell. Biol. 24:8981-8993(2004) [PubMed: 15456872] [Abstract] Cited for: INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB. |
| [16] | "CIN85 regulates the ability of MEKK4 to activate the p38 MAP kinase pathway." Aissouni Y., Zapart G., Iovanna J.L., Dikic I., Soubeyran P. Biochem. Biophys. Res. Commun. 338:808-814(2005) [PubMed: 16256071] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAP3K4. |
| [17] | "Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation." Haglund K., Schmidt M.H., Wong E.S., Guy G.R., Dikic I. EMBO Rep. 6:635-641(2005) [PubMed: 15962011] [Abstract] Cited for: INTERACTION WITH SPRY2. |
| [18] | "CIN85 associates with TNF receptor 1 via Src and modulates TNF-alpha-induced apoptosis." Narita T., Nishimura T., Yoshizaki K., Taniyama T. Exp. Cell Res. 304:256-264(2005) [PubMed: 15707590] [Abstract] Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH SRC; LCK; LYN; FGR; FYN; HCK; TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1. |
| [19] | "CIN85 regulates the ligand-dependent endocytosis of the IgE receptor: a new molecular mechanism to dampen mast cell function." Molfetta R., Belleudi F., Peruzzi G., Morrone S., Leone L., Dikic I., Piccoli M., Frati L., Torrisi M.R., Santoni A., Paolini R. J. Immunol. 175:4208-4216(2005) [PubMed: 16177060] [Abstract] Cited for: FUNCTION IN RECEPTOR INTERNALIZATION. |
| [20] | "Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, MASS SPECTROMETRY. |
| [21] | "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells." 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. Cell 125:535-548(2006) [PubMed: 16678097] [Abstract] Cited for: INTERACTION WITH ARHGAP17. |
| [22] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-509 AND SER-511, MASS SPECTROMETRY. Tissue: Epithelium. |
| [23] | "CIN85 is localized at synapses and forms a complex with S-SCAM via dendrin." Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y. J. Biochem. 139:931-939(2006) [PubMed: 16751601] [Abstract] Cited for: INTERACTION WITH DDN AND MAGI2, SUBCELLULAR LOCATION. |
| [24] | "CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP." Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H. J. Biol. Chem. 281:28919-28931(2006) [PubMed: 16895919] [Abstract] Cited for: INTERACTION WITH FAM125A. |
| [25] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-254; SER-436; SER-509; SER-511; SER-521 AND SER-587, MASS SPECTROMETRY. |
| [26] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [27] | "Cbl promotes clustering of endocytic adaptor proteins." Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D., Groemping Y., Dikic I., Rittinger K., Bravo J. Nat. Struct. Mol. Biol. 12:972-979(2005) [PubMed: 16228008] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF230904 mRNA. Translation: AAF37854.1. AF542051 mRNA. Translation: AAN77231.1. BC015806 mRNA. Translation: AAH15806.1. BC050663 mRNA. Translation: AAH50663.1. Sequence problems. AF329267 mRNA. Translation: AAK95587.1. AF329268 mRNA. Translation: AAO13348.1. | |||||||||||||||||||||||||
| IPI | IPI00294962. IPI00477897. | ||||||||||||||||||||||||
| PIR | JC7191. | ||||||||||||||||||||||||
| RefSeq | NP_001019837.1. NP_114098.1. | ||||||||||||||||||||||||
| UniGene | Hs.444770 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| SMR | Q96B97. Positions 264-326. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | Q96B97. 2 interactions. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | Q96B97. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | Q96B97. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSG00000147010. Homo sapiens. [Contig view] | ||||||||||||||||||||||||
| GeneID | 30011. | ||||||||||||||||||||||||
| KEGG | hsa:30011. | ||||||||||||||||||||||||
| NMPDR | fig|9606.3.peg.32531. | ||||||||||||||||||||||||
| UCSC | uc004czl.1. human. uc004czm.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| GeneCards | GC0XM019462. | ||||||||||||||||||||||||
| H-InvDB | HIX0021848. | ||||||||||||||||||||||||
| HGNC | HGNC:13867. SH3KBP1. | ||||||||||||||||||||||||
| HPA | HPA003351. HPA003355. | ||||||||||||||||||||||||
| MIM | 300374. gene. | ||||||||||||||||||||||||
| PharmGKB | PA37822. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | Q96B97. | ||||||||||||||||||||||||
| HOVERGEN | Q96B97. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| Pathway_Interaction_DB | met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met). | ||||||||||||||||||||||||
| Reactome | REACT_9417. Signaling by EGFR. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | Q96B97. | ||||||||||||||||||||||||
| Bgee | Q96B97. | ||||||||||||||||||||||||
| CleanEx | HS_SH3KBP1. | ||||||||||||||||||||||||
| GermOnline | ENSG00000147010. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR000108. Neu_cyt_fact_2. IPR001452. SH3_domain. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF00018. SH3_1. 3 hits. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00499. P67PHOX. | ||||||||||||||||||||||||
| ProDom | PD000066. SH3. 2 hits. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||
| SMART | SM00326. SH3. 3 hits. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS50002. SH3. 3 hits. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| NextBio | 52832. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | SH3K1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96B97 Secondary accession number(s): Q8IWX6 Q9NYR0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


