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Protein

SH3 domain-binding protein 4

Gene

Sh3bp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 domain-binding protein 4
Gene namesi
Name:Sh3bp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2138297. Sh3bp4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 962962SH3 domain-binding protein 4PRO_0000274575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei250 – 2501PhosphoserineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei636 – 6361PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated upon EGF stimulation. Phosphorylation prevents interaction with DNM2 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ921I6.
PaxDbiQ921I6.
PRIDEiQ921I6.

PTM databases

iPTMnetiQ921I6.
PhosphoSiteiQ921I6.

Expressioni

Gene expression databases

BgeeiQ921I6.
CleanExiMM_SH3BP4.
GenevisibleiQ921I6. MM.

Interactioni

Subunit structurei

Homodimer or homooligomer. Interacts with DNM2, EPS15, clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most probably direct, preferentially occurs with their inactive GDP-bound form and is negatively regulated by amino acids (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221051. 1 interaction.
STRINGi10090.ENSMUSP00000067581.

Structurei

3D structure databases

ProteinModelPortaliQ921I6.
SMRiQ921I6. Positions 61-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 11460SH3PROSITE-ProRule annotationAdd
BLAST

Domaini

The SH3 domain mediates localization to the clathrin-coated pits and vesicles. The SH3 domain mediates interaction with DNM2 and the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also mediates interaction with RRAGB, RRAGC and is required for the negative regulation of mTORC1 (By similarity).By similarity

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410IEE9. Eukaryota.
ENOG41118AI. LUCA.
GeneTreeiENSGT00390000013151.
HOGENOMiHOG000015297.
HOVERGENiHBG057439.
InParanoidiQ921I6.
OMAiFFCRAEL.
OrthoDBiEOG7GJ6C4.
PhylomeDBiQ921I6.
TreeFamiTF105572.

Family and domain databases

InterProiIPR011511. SH3_2.
IPR001452. SH3_domain.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q921I6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQRIRAAN ASGLPRCKSE GTLIDLSEGF SETSFNDVKV PSPSALLVDN
60 70 80 90 100
PTPFGNAKEV IAIKDYCPNN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE
110 120 130 140 150
MGYIPSSYVQ PLNYRNSTLS DSGMIDNLPD SPEEVAKELD LLGGGWTDDQ
160 170 180 190 200
KESGRPYSNN PFWNGVRTNP FLNGNAQPST DELNPKSTVD LLLFDTGTSS
210 220 230 240 250
FTESSSATTN STGNIFDELP ATNGLQVEQP VKRDNPFFRS KRSYSLSELS
260 270 280 290 300
VLQAKSDAPP TSSFFTGLKS PVPEQFQSRE DFRTAWLNHR KLARSCHDLD
310 320 330 340 350
LLGQSPGWGQ TQAVETNIVC KLDSSGGSVQ LPDTNISIHV PEGHVAPGET
360 370 380 390 400
QQISMKALLD PPLDLNSDRS TSVSPVVEVK LSNLEVSTFI ILEMKVSAEV
410 420 430 440 450
KGDIFSKSTV VLQCLRSDSK EGPYVPIPLA YSYGDTIQVQ LDNLEPCMYL
460 470 480 490 500
AIVAQGPNIL YPSTVWDFIN KRVTVGLYGP KHIHPSFKTV VTIFGHDCAP
510 520 530 540 550
KTLLVSEVTR QAPSPAPVAL QLWGKHQFIL SRPQDLRVCM FSNMTNYEVK
560 570 580 590 600
ANEQARVVRG FQMKLGKVSR LIFSVISQNP NELSDFTLRV QVKDDQDTIL
610 620 630 640 650
TQFCVQTPQP PPKSAIKPSG QRRFLKKNEV GKIILSPFVV TTKYPTFQDR
660 670 680 690 700
PVSSLKFGKL LKTVVRQNKS HYLLEYKKGD VVALLSEERI RLKGQLWTKE
710 720 730 740 750
WYIGYYQGKV GLVHTKNVLV VGKARPSLFS GPELSTSVLL EQILRPCKFL
760 770 780 790 800
TYIYASVRTL LMENISSWRA FADALGYGNL PLTFFCRAEL DSEPERVASV
810 820 830 840 850
LEKLKEDCNN PDNKDRKSFQ KELVMALLKM DCQGLVVRLI QDFVLLTTAV
860 870 880 890 900
EVAQRWRELA EKLAKVSKQQ MDAYESPHRD RNGVVDSEAM WKPAYDFLLT
910 920 930 940 950
WSHQIGDSYR DVIQELHIGL DKMKNPITRR WKHLTGTLIL VNSLDILRAA
960
AFSPADHDDF VI
Length:962
Mass (Da):107,584
Last modified:December 1, 2001 - v1
Checksum:i11154849455F4063
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121Q → K in BAC30966 (PubMed:16141072).Curated
Sequence conflicti340 – 3401V → E in BAC27961 (PubMed:16141072).Curated
Sequence conflicti534 – 5341Q → K in BAC27961 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028826 mRNA. Translation: BAC26140.1.
AK032634 mRNA. Translation: BAC27961.1.
AK041504 mRNA. Translation: BAC30966.1.
AK043259 mRNA. Translation: BAC31506.1.
BC012284 mRNA. Translation: AAH12284.1.
BC034733 mRNA. Translation: AAH34733.1.
CCDSiCCDS15147.1.
RefSeqiNP_598577.1. NM_133816.2.
XP_006530038.1. XM_006529975.2.
UniGeneiMm.170983.

Genome annotation databases

EnsembliENSMUST00000066279; ENSMUSP00000067581; ENSMUSG00000036206.
GeneIDi98402.
KEGGimmu:98402.
UCSCiuc007byv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028826 mRNA. Translation: BAC26140.1.
AK032634 mRNA. Translation: BAC27961.1.
AK041504 mRNA. Translation: BAC30966.1.
AK043259 mRNA. Translation: BAC31506.1.
BC012284 mRNA. Translation: AAH12284.1.
BC034733 mRNA. Translation: AAH34733.1.
CCDSiCCDS15147.1.
RefSeqiNP_598577.1. NM_133816.2.
XP_006530038.1. XM_006529975.2.
UniGeneiMm.170983.

3D structure databases

ProteinModelPortaliQ921I6.
SMRiQ921I6. Positions 61-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221051. 1 interaction.
STRINGi10090.ENSMUSP00000067581.

PTM databases

iPTMnetiQ921I6.
PhosphoSiteiQ921I6.

Proteomic databases

MaxQBiQ921I6.
PaxDbiQ921I6.
PRIDEiQ921I6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066279; ENSMUSP00000067581; ENSMUSG00000036206.
GeneIDi98402.
KEGGimmu:98402.
UCSCiuc007byv.1. mouse.

Organism-specific databases

CTDi23677.
MGIiMGI:2138297. Sh3bp4.

Phylogenomic databases

eggNOGiENOG410IEE9. Eukaryota.
ENOG41118AI. LUCA.
GeneTreeiENSGT00390000013151.
HOGENOMiHOG000015297.
HOVERGENiHBG057439.
InParanoidiQ921I6.
OMAiFFCRAEL.
OrthoDBiEOG7GJ6C4.
PhylomeDBiQ921I6.
TreeFamiTF105572.

Miscellaneous databases

ChiTaRSiSh3bp4. mouse.
NextBioi353456.
PROiQ921I6.
SOURCEiSearch...

Gene expression databases

BgeeiQ921I6.
CleanExiMM_SH3BP4.
GenevisibleiQ921I6. MM.

Family and domain databases

InterProiIPR011511. SH3_2.
IPR001452. SH3_domain.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Skin and Thymus.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-250 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSH3B4_MOUSE
AccessioniPrimary (citable) accession number: Q921I6
Secondary accession number(s): Q8BXV5, Q8BY95, Q8C007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: December 1, 2001
Last modified: January 20, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.