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Protein

SH3 domain-containing kinase-binding protein 1

Gene

SH3KBP1

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

Functioni

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.By similarity10 Publications

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell-cell signaling Source: UniProtKB
  • cell migration Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  • regulation of cell shape Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12484. EGFR downregulation.
SignaLinkiQ96B97.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SH3KBP1
Synonyms:CIN85
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:13867. SH3KBP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37822.

Polymorphism and mutation databases

BioMutaiSH3KBP1.
DMDMi31077034.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665SH3 domain-containing kinase-binding protein 1PRO_0000097728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine6 Publications
Modified residuei254 – 2541Phosphothreonine1 Publication
Modified residuei436 – 4361Phosphoserine2 Publications
Modified residuei509 – 5091Phosphoserine2 Publications
Modified residuei511 – 5111Phosphoserine2 Publications
Modified residuei521 – 5211Phosphoserine1 Publication
Modified residuei587 – 5871Phosphoserine2 Publications

Post-translational modificationi

Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96B97.
PaxDbiQ96B97.
PRIDEiQ96B97.

PTM databases

PhosphoSiteiQ96B97.

Expressioni

Tissue specificityi

Ubiquitously expressed. Also expressed in some cancer cell lines.

Gene expression databases

BgeeiQ96B97.
CleanExiHS_SH3KBP1.
ExpressionAtlasiQ96B97. baseline and differential.
GenevisibleiQ96B97. HS.

Organism-specific databases

HPAiCAB021892.
HPA003351.
HPA003355.

Interactioni

Subunit structurei

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 SH3KBP1.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAP3Q8WWN82EBI-346595,EBI-4402732
ASAP1Q9ULH18EBI-346595,EBI-346622
CAPZA1P529072EBI-346595,EBI-355586
CBLP2268118EBI-346595,EBI-518228
CBLBQ1319119EBI-346595,EBI-744027
CD2P067293EBI-346595,EBI-3912464
Dab2P980789EBI-346595,EBI-1391846From a different organism.
DDNO948505EBI-346595,EBI-5240523
DNM2P505705EBI-346595,EBI-346547
Dnm2P390524EBI-346595,EBI-349613From a different organism.
Hip1rQ9JKY53EBI-346595,EBI-642457From a different organism.
INPP5DQ928356EBI-346595,EBI-1380477
MAP3K4Q9Y6R45EBI-346595,EBI-448104
SH3BP2P783148EBI-346595,EBI-727062
SH3GL2Q999622EBI-346595,EBI-77938
SPRY2O435972EBI-346595,EBI-742487
SQSTM1Q135014EBI-346595,EBI-307104
STAP1Q9ULZ24EBI-346595,EBI-6083058
SYNJ2O150563EBI-346595,EBI-310513
UBCP0CG486EBI-346595,EBI-3390054

Protein-protein interaction databases

BioGridi119029. 258 interactions.
DIPiDIP-31803N.
IntActiQ96B97. 42 interactions.
MINTiMINT-233697.
STRINGi9606.ENSP00000380921.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi25 – 306Combined sources
Turni33 – 353Combined sources
Beta strandi36 – 416Combined sources
Beta strandi44 – 496Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 553Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi124 – 1263Combined sources
Helixi130 – 1323Combined sources
Beta strandi149 – 1535Combined sources
Turni161 – 1644Combined sources
Beta strandi270 – 2767Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi293 – 2997Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi306 – 3116Combined sources
Beta strandi314 – 3196Combined sources
Helixi320 – 3223Combined sources
Beta strandi323 – 3253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZ8X-ray2.00A/B1-58[»]
2K6DNMR-A267-328[»]
2K9GNMR-A262-333[»]
2O2ONMR-A92-168[»]
2YDLX-ray2.05A270-328[»]
ProteinModelPortaliQ96B97.
SMRiQ96B97. Positions 1-182, 262-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96B97.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 15760SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini267 – 32862SH3 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili602 – 66463Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi327 – 428102Pro-richAdd
BLAST

Domaini

The SH3 domains mediate interaction with SHKBP1.By similarity

Sequence similaritiesi

Contains 3 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG319250.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ96B97.
KOiK12470.
OMAiEDKEEHV.
OrthoDBiEOG7W41BC.
PhylomeDBiQ96B97.
TreeFamiTF350191.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 3 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96B97-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVEAIVEFDY QAQHDDELTI SVGEIITNIR KEDGGWWEGQ INGRRGLFPD
60 70 80 90 100
NFVREIKKEM KKDPLTNKAP EKPLHEVPSG NSLLSSETIL RTNKRGERRR
110 120 130 140 150
RRCQVAFSYL PQNDDELELK VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN
160 170 180 190 200
FIKELSGESD ELGISQDEQL SKSSLRETTG SESDGGDSSS TKSEGANGTV
210 220 230 240 250
ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV EKTIGKKLPA
260 270 280 290 300
TTATPDSSKT EMDSRTKSKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD
310 320 330 340 350
CIDVGWWEGE LNGRRGVFPD NFVKLLPPDF EKEGNRPKKP PPPSAPVIKQ
360 370 380 390 400
GAGTTERKHE IKKIPPERPE MLPNRTEEKE RPEREPKLDL QKPSVPAIPP
410 420 430 440 450
KKPRPPKTNS LSRPGALPPR RPERPVGPLT HTRGDSPKID LAGSSLSGIL
460 470 480 490 500
DKDLSDRSND IDLEGFDSVV SSTEKLSHPT TSRPKATGRR PPSQSLTSSS
510 520 530 540 550
LSSPDIFDSP SPEEDKEEHI SLAHRGVDAS KKTSKTVTIS QVSDNKASLP
560 570 580 590 600
PKPGTMAAGG GGPAPLSSAA PSPLSSSLGT AGHRANSPSL FGTEGKPKME
610 620 630 640 650
PAASSQAAVE ELRTQVRELR SIIETMKDQQ KREIKQLLSE LDEEKKIRLR
660
LQMEVNDIKK ALQSK
Note: Interacts with CBL.
Length:665
Mass (Da):73,126
Last modified:May 23, 2003 - v2
Checksum:i3BD350FCDB14BD4C
GO
Isoform 2 (identifier: Q96B97-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:628
Mass (Da):68,550
Checksum:i8AD93481480879D6
GO
Isoform 3 (identifier: Q96B97-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVEA → MGEE
     5-242: Missing.

Note: No experimental confirmation available.
Show »
Length:427
Mass (Da):46,610
Checksum:iCDD6AC2770E695F4
GO

Sequence cautioni

The sequence AAH50663.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881I → T in BAH11471 (PubMed:14702039).Curated
Sequence conflicti426 – 4261V → A in BAH11471 (PubMed:14702039).Curated
Sequence conflicti570 – 5701A → V in AAH15806 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti382 – 3821P → L.1 Publication
VAR_015667

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454MVEAI…DNFVR → MEVSAAKAPSAADLSEI in isoform 2. 2 PublicationsVSP_007504Add
BLAST
Alternative sequencei1 – 44MVEA → MGEE in isoform 3. 1 PublicationVSP_044655
Alternative sequencei5 – 242238Missing in isoform 3. 1 PublicationVSP_044656Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14193.1. [Q96B97-1]
CCDS35213.1. [Q96B97-2]
CCDS55383.1. [Q96B97-3]
PIRiJC7191.
RefSeqiNP_001019837.1. NM_001024666.2. [Q96B97-2]
NP_001171889.1. NM_001184960.1. [Q96B97-3]
NP_114098.1. NM_031892.2. [Q96B97-1]
UniGeneiHs.726365.

Genome annotation databases

EnsembliENST00000379698; ENSP00000369020; ENSG00000147010. [Q96B97-2]
ENST00000379716; ENSP00000369039; ENSG00000147010. [Q96B97-3]
ENST00000397821; ENSP00000380921; ENSG00000147010.
GeneIDi30011.
KEGGihsa:30011.
UCSCiuc004czl.3. human. [Q96B97-2]
uc004czm.3. human. [Q96B97-1]
uc011mjf.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14193.1. [Q96B97-1]
CCDS35213.1. [Q96B97-2]
CCDS55383.1. [Q96B97-3]
PIRiJC7191.
RefSeqiNP_001019837.1. NM_001024666.2. [Q96B97-2]
NP_001171889.1. NM_001184960.1. [Q96B97-3]
NP_114098.1. NM_031892.2. [Q96B97-1]
UniGeneiHs.726365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZ8X-ray2.00A/B1-58[»]
2K6DNMR-A267-328[»]
2K9GNMR-A262-333[»]
2O2ONMR-A92-168[»]
2YDLX-ray2.05A270-328[»]
ProteinModelPortaliQ96B97.
SMRiQ96B97. Positions 1-182, 262-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119029. 258 interactions.
DIPiDIP-31803N.
IntActiQ96B97. 42 interactions.
MINTiMINT-233697.
STRINGi9606.ENSP00000380921.

PTM databases

PhosphoSiteiQ96B97.

Polymorphism and mutation databases

BioMutaiSH3KBP1.
DMDMi31077034.

Proteomic databases

MaxQBiQ96B97.
PaxDbiQ96B97.
PRIDEiQ96B97.

Protocols and materials databases

DNASUi30011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379698; ENSP00000369020; ENSG00000147010. [Q96B97-2]
ENST00000379716; ENSP00000369039; ENSG00000147010. [Q96B97-3]
ENST00000397821; ENSP00000380921; ENSG00000147010.
GeneIDi30011.
KEGGihsa:30011.
UCSCiuc004czl.3. human. [Q96B97-2]
uc004czm.3. human. [Q96B97-1]
uc011mjf.2. human.

Organism-specific databases

CTDi30011.
GeneCardsiGC0XM019552.
HGNCiHGNC:13867. SH3KBP1.
HPAiCAB021892.
HPA003351.
HPA003355.
MIMi300374. gene.
neXtProtiNX_Q96B97.
PharmGKBiPA37822.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG319250.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ96B97.
KOiK12470.
OMAiEDKEEHV.
OrthoDBiEOG7W41BC.
PhylomeDBiQ96B97.
TreeFamiTF350191.

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12484. EGFR downregulation.
SignaLinkiQ96B97.

Miscellaneous databases

ChiTaRSiSH3KBP1. human.
EvolutionaryTraceiQ96B97.
GeneWikiiSH3KBP1.
GenomeRNAii30011.
NextBioi52832.
PROiQ96B97.
SOURCEiSearch...

Gene expression databases

BgeeiQ96B97.
CleanExiHS_SH3KBP1.
ExpressionAtlasiQ96B97. baseline and differential.
GenevisibleiQ96B97. HS.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 3 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-509 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  35. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB.

Entry informationi

Entry nameiSH3K1_HUMAN
AccessioniPrimary (citable) accession number: Q96B97
Secondary accession number(s): B7Z1D5
, Q5JPT4, Q5JPT5, Q8IWX6, Q8IX98, Q96RN4, Q9NYR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: July 22, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.