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Q96B97 (SH3K1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH3 domain-containing kinase-binding protein 1
Alternative name(s):
CD2-binding protein 3
Short name=CD2BP3
Cbl-interacting protein of 85 kDa
Human Src family kinase-binding protein 1
Short name=HSB-1
Gene names
Name:SH3KBP1
Synonyms:CIN85
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.17 Ref.19 Ref.21 Ref.22 Ref.31

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/FAK1 AND PTK2B/PYK2, 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.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junctionsynapsesynaptosome. Cell junctionfocal 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. Ref.8 Ref.9 Ref.17 Ref.25

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: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processApoptosis
Endocytosis
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
SH3 domain
SH3-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype Ref.31. Source: UniProtKB

cell-cell signaling

Non-traceable author statement Ref.1. Source: UniProtKB

cytoskeleton organization

Inferred from mutant phenotype Ref.31. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of cell shape

Inferred from mutant phenotype Ref.31. Source: UniProtKB

   Cellular_componentcytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: Q96B97-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVEA → MGEE
     5-242: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665SH3 domain-containing kinase-binding protein 1
PRO_0000097728

Regions

Domain1 – 5858SH3 1
Domain98 – 15760SH3 2
Domain267 – 32862SH3 3
Coiled coil602 – 66463 Potential
Compositional bias327 – 428102Pro-rich

Amino acid modifications

Modified residue2301Phosphoserine Ref.16 Ref.24 Ref.27 Ref.29 Ref.30 Ref.33
Modified residue2541Phosphothreonine Ref.28
Modified residue4361Phosphoserine Ref.28 Ref.30
Modified residue5091Phosphoserine Ref.28
Modified residue5111Phosphoserine Ref.28
Modified residue5211Phosphoserine Ref.28
Modified residue5871Phosphoserine Ref.28 Ref.30

Natural variations

Alternative sequence1 – 5454MVEAI…DNFVR → MEVSAAKAPSAADLSEI in isoform 2.
VSP_007504
Alternative sequence1 – 44MVEA → MGEE in isoform 3.
VSP_044655
Alternative sequence5 – 242238Missing in isoform 3.
VSP_044656
Natural variant3821P → L. Ref.6
VAR_015667

Experimental info

Sequence conflict2881I → T in BAH11471. Ref.3
Sequence conflict4261V → A in BAH11471. Ref.3
Sequence conflict5701A → V in AAH15806. Ref.5

Secondary structure

...................................... 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: 3BD350FCDB14BD4C

FASTA66573,126
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8AD93481480879D6
Show »

FASTA62868,550
Isoform 3 [UniParc].

Checksum: CDD6AC2770E695F4
Show »

FASTA42746,610

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: T-cell.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Adrenal cortex and Uterus.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, VARIANT LEU-382.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, SELF-ASSOCIATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC, FUNCTION IN RECEPTOR INTERNALIZATION, SUBCELLULAR LOCATION.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1; SH3GL2; SH3GL3 AND CBL, SUBCELLULAR LOCATION.
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH SH3GL1; SH3GL2; SH3GL3; CBL AND MET.
[11]"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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY CBL AND CBLB.
[12]"Dab2 links CIN85 with clathrin-mediated receptor internalization."
Kowanetz K., Terzic J., Dikic I.
FEBS Lett. 554:81-87(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2, IDENTIFICATION IN A COMPLEX WITH DAB2 AND CLATHRIN.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH PDCD6IP; PTK2/FAK1 AND PTK2B/PYK2.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN.
[15]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR INTERNALIZATION.
[16]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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] [Europe PMC] [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.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB.
[19]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K4.
[20]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPRY2.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH SRC; LCK; LYN; FGR; FYN; HCK; TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1.
[22]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR INTERNALIZATION.
[23]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP17.
[24]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDN AND MAGI2, SUBCELLULAR LOCATION.
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MVB12A.
[27]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[28]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-436; SER-509; SER-511; SER-521 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-436 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230904 mRNA. Translation: AAF37854.1.
AF542051 mRNA. Translation: AAN77231.1.
AK293234 mRNA. Translation: BAH11470.1.
AK293237 mRNA. Translation: BAH11471.1.
AL732423, AL732325, AL732327 Genomic DNA. Translation: CAI40277.1.
AL732423, AL732327 Genomic DNA. Translation: CAI40278.1.
AL732327, AL732325, AL732423 Genomic DNA. Translation: CAI40511.1.
AL732327, AL732423 Genomic DNA. Translation: CAI40512.1.
AL732325, AL732327, AL732423 Genomic DNA. Translation: CAI41254.1.
AL732409 Genomic DNA. No translation available.
AL772197 Genomic DNA. No translation available.
BC015806 mRNA. Translation: AAH15806.1.
BC050663 mRNA. Translation: AAH50663.1. Sequence problems.
AF329267 mRNA. Translation: AAK95587.1.
AF329268 mRNA. Translation: AAO13348.1.
PIRJC7191.
RefSeqNP_001019837.1. NM_001024666.2.
NP_001171889.1. NM_001184960.1.
NP_114098.1. NM_031892.2.
XP_005274554.1. XM_005274497.1.
UniGeneHs.726365.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZ8X-ray2.00A/B1-58[»]
2K6DNMR-A267-328[»]
2K9GNMR-A262-333[»]
2O2ONMR-A92-168[»]
2YDLX-ray2.05A270-328[»]
ProteinModelPortalQ96B97.
SMRQ96B97. Positions 2-182, 262-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119029. 240 interactions.
DIPDIP-31803N.
IntActQ96B97. 42 interactions.
MINTMINT-233697.
STRING9606.ENSP00000380921.

PTM databases

PhosphoSiteQ96B97.

Polymorphism databases

DMDM31077034.

Proteomic databases

PaxDbQ96B97.
PRIDEQ96B97.

Protocols and materials databases

DNASU30011.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379698; ENSP00000369020; ENSG00000147010. [Q96B97-2]
ENST00000379716; ENSP00000369039; ENSG00000147010. [Q96B97-3]
ENST00000397821; ENSP00000380921; ENSG00000147010. [Q96B97-1]
GeneID30011.
KEGGhsa:30011.
UCSCuc004czl.3. human. [Q96B97-2]
uc004czm.3. human. [Q96B97-1]
uc011mjf.2. human.

Organism-specific databases

CTD30011.
GeneCardsGC0XM019552.
HGNCHGNC:13867. SH3KBP1.
HPACAB021892.
HPA003351.
HPA003355.
MIM300374. gene.
neXtProtNX_Q96B97.
PharmGKBPA37822.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319250.
HOGENOMHOG000231405.
HOVERGENHBG057824.
InParanoidQ96B97.
KOK12470.
OMAMDSRTKT.
OrthoDBEOG7W41BC.
PhylomeDBQ96B97.
TreeFamTF350191.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ96B97.

Gene expression databases

ArrayExpressQ96B97.
BgeeQ96B97.
CleanExHS_SH3KBP1.
GenevestigatorQ96B97.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
PROSITEPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSH3KBP1. human.
EvolutionaryTraceQ96B97.
GeneWikiSH3KBP1.
GenomeRNAi30011.
NextBio52832.
PROQ96B97.
SOURCESearch...

Entry information

Entry nameSH3K1_HUMAN
AccessionPrimary (citable) accession number: Q96B97
Secondary accession number(s): B7Z1D5 expand/collapse secondary AC list , Q5JPT4, Q5JPT5, Q8IWX6, Q8IX98, Q96RN4, Q9NYR0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: March 19, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM