Q96B97 (SH3K1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SH3KBP1
Synonyms:	CIN85

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
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. 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	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. 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 process	Apoptosis Endocytosis
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat SH3 domain SH3-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic 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_component	cytoplasmic 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBL	P22681	6	EBI-346595,EBI-518228
Dab2	P98078	9	EBI-346595,EBI-1391846	From a different organism.
DDN	O94850	5	EBI-346595,EBI-5240523

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 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.16 Ref.24 Ref.27 Ref.29 Ref.30 Ref.33

Modified residue

254

1

Phosphothreonine Ref.28

Modified residue

436

1

Phosphoserine Ref.28 Ref.30

Modified residue

468

1

Phosphoserine By similarity

Modified residue

509

1

Phosphoserine Ref.28

Modified residue

511

1

Phosphoserine Ref.28

Modified residue

521

1

Phosphoserine Ref.28

Modified residue

587

1

Phosphoserine Ref.28 Ref.30

Natural variations

Alternative sequence

1 – 54

54

MVEAI…DNFVR → MEVSAAKAPSAADLSEI in isoform 2.

VSP_007504

Alternative sequence

1 – 4

4

MVEA → MGEE in isoform 3.

VSP_044655

Alternative sequence

5 – 242

238

Missing in isoform 3.

VSP_044656

Natural variant

382

1

P → L. Ref.6

VAR_015667

Experimental info

Sequence conflict

288

1

I → T in BAH11471. Ref.3

Sequence conflict

426

1

V → A in BAH11471. Ref.3

Sequence conflict

570

1

A → V in AAH15806. Ref.5

Secondary structure

1

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665

Helix Strand Turn

Details...

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

Beta strand

270 – 276

7

Beta strand

283 – 285

3

Beta strand

293 – 299

7

Beta strand

301 – 303

3

Beta strand

306 – 311

6

Beta strand

314 – 319

6

Helix

320 – 322

3

Beta strand

323 – 325

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 23, 2003. Version 2. Checksum: 3BD350FCDB14BD4C	FASTA	665	73,126
	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
	Isoform 2 [UniParc]. Checksum: 8AD93481480879D6	FASTA	628	68,550
	10 20 30 40 50 60 MEVSAAKAPS AADLSEIEIK KEMKKDPLTN KAPEKPLHEV PSGNSLLSSE TILRTNKRGE 70 80 90 100 110 120 RRRRRCQVAF SYLPQNDDEL ELKVGDIIEV VGEVEEGWWE GVLNGKTGMF PSNFIKELSG 130 140 150 160 170 180 ESDELGISQD EQLSKSSLRE TTGSESDGGD SSSTKSEGAN GTVATAAIQP KKVKGVGFGD 190 200 210 220 230 240 IFKDKPIKLR PRSIEVENDF LPVEKTIGKK LPATTATPDS SKTEMDSRTK SKDYCKVIFP 250 260 270 280 290 300 YEAQNDDELT IKEGDIVTLI NKDCIDVGWW EGELNGRRGV FPDNFVKLLP PDFEKEGNRP 310 320 330 340 350 360 KKPPPPSAPV IKQGAGTTER KHEIKKIPPE RPEMLPNRTE EKERPEREPK LDLQKPSVPA 370 380 390 400 410 420 IPPKKPRPPK TNSLSRPGAL PPRRPERPVG PLTHTRGDSP KIDLAGSSLS GILDKDLSDR 430 440 450 460 470 480 SNDIDLEGFD SVVSSTEKLS HPTTSRPKAT GRRPPSQSLT SSSLSSPDIF DSPSPEEDKE 490 500 510 520 530 540 EHISLAHRGV DASKKTSKTV TISQVSDNKA SLPPKPGTMA AGGGGPAPLS SAAPSPLSSS 550 560 570 580 590 600 LGTAGHRANS PSLFGTEGKP KMEPAASSQA AVEELRTQVR ELRSIIETMK DQQKREIKQL 610 620 LSELDEEKKI RLRLQMEVND IKKALQSK
	Isoform 3 [UniParc]. Checksum: CDD6AC2770E695F4	FASTA	427	46,610
	10 20 30 40 50 60 MGEETIGKKL PATTATPDSS KTEMDSRTKS KDYCKVIFPY EAQNDDELTI KEGDIVTLIN 70 80 90 100 110 120 KDCIDVGWWE GELNGRRGVF PDNFVKLLPP DFEKEGNRPK KPPPPSAPVI KQGAGTTERK 130 140 150 160 170 180 HEIKKIPPER PEMLPNRTEE KERPEREPKL DLQKPSVPAI PPKKPRPPKT NSLSRPGALP 190 200 210 220 230 240 PRRPERPVGP LTHTRGDSPK IDLAGSSLSG ILDKDLSDRS NDIDLEGFDS VVSSTEKLSH 250 260 270 280 290 300 PTTSRPKATG RRPPSQSLTS SSLSSPDIFD SPSPEEDKEE HISLAHRGVD ASKKTSKTVT 310 320 330 340 350 360 ISQVSDNKAS LPPKPGTMAA GGGGPAPLSS AAPSPLSSSL GTAGHRANSP SLFGTEGKPK 370 380 390 400 410 420 MEPAASSQAA VEELRTQVRE LRSIIETMKD QQKREIKQLL SELDEEKKIR LRLQMEVNDI KKALQSK

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00294962.
IPI00477897.
IPI00643458.

PIR

JC7191.

RefSeq

NP_001019837.1. NM_001024666.2.
NP_001171889.1. NM_001184960.1.
NP_114098.1. NM_031892.2.

UniGene

Hs.726365.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BZ8	X-ray	2.00	A/B	1-58	[»]
2K6D	NMR	-	A	267-328	[»]
2K9G	NMR	-	A	262-333	[»]
2O2O	NMR	-	A	92-168	[»]
2YDL	X-ray	2.05	A	270-328	[»]

ProteinModelPortal

Q96B97.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96B97. 16 interactions.

MINT

MINT-233697.

STRING

9606.ENSP00000380921.

PTM databases

PhosphoSite

Q96B97.

Polymorphism databases

DMDM

31077034.

Proteomic databases

PaxDb

Q96B97.

PRIDE

Q96B97.

Protocols and materials databases

DNASU

30011.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379698; ENSP00000369020; ENSG00000147010.
ENST00000379716; ENSP00000369039; ENSG00000147010.
ENST00000397821; ENSP00000380921; ENSG00000147010.

GeneID

30011.

KEGG

hsa:30011.

UCSC

uc004czm.3. human.

Organism-specific databases

CTD

30011.

GeneCards

GC0XM019552.

HGNC

HGNC:13867. SH3KBP1.

HPA

CAB021892.
HPA003351.
HPA003355.

MIM

300374. gene.

neXtProt

NX_Q96B97.

PharmGKB

PA37822.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG319250.

HOGENOM

HOG000231405.

HOVERGEN

HBG057824.

InParanoid

Q96B97.

KO

K12470.

OMA

KAPEKPM.

OrthoDB

EOG4FN4HD.

PhylomeDB

Q96B97.

Enzyme and pathway databases

Pathway_Interaction_DB

met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q96B97.

Bgee

Q96B97.

CleanEx

HS_SH3KBP1.

Genevestigator

Q96B97.

GermOnline

ENSG00000147010. Homo sapiens.

Family and domain databases

InterPro

IPR000108. p67phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 2 hits.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 3 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 3 hits.

PROSITE

PS50002. SH3. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SH3KBP1. human.

EvolutionaryTrace

Q96B97.

GenomeRNAi

30011.

NextBio

52832.

SOURCE

Search...

Entry information

Entry name

SH3K1_HUMAN

Accession

Primary (citable) accession number: Q96B97
Secondary accession number(s): B7Z1D5 , Q5JPT4, Q5JPT5, Q8IWX6, Q8IX98, Q96RN4, Q9NYR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.