wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GTPase-activating protein 27 (CIN85-associated multi-domain-containing Rho GTPase-activating protein 1) (Rho-type GTPase-activating protein 27) (Q6TLK4)
Organism: Rattus norvegicus (Rat)
Function: Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15147912}. Membrane {ECO:0000269|PubMed:15147912}; Peripheral membrane protein {ECO:0000269|PubMed:15147912}.
Interaction partners:
Sequence:
MAADVEGDVYVLVEHPFEYTGKDGRLIAIQPNERCRLLRRSTEHWWHVRREPGGRPFYLPAQYVRELPALGDPVPAPQPSVLQQRPTVPEPLAYDYRFVSTPVGADGSSAEPRGRASSLCGPARQRTSGQRNSLAPGGPACLYLRPAAPVRPAQSLDDLARGGTAPPAGLLGSAGHFKASSVAGSWVCPRPLARSDSENVYEAIPDLRCPPRAKSPKQVDEPPEPVYANVERQPQVTSPRSAAAPPRLSPVWETHTDAGTGRPYYYNPDTGVTTWESPFEAPEGATSPTTSRASVGSGESLETEWGQYWDEESGRVFFYNPLTGETVWEDETEELEDDPEEQLEMQPSLSPRSPGQQRPPTPETDYPELLTSYPEEDYSPVGSFSDLGPTSPLVAPPGWSCQITPEKQMLYTNQFTQEQWVRLEDQEGKPYFYNPEDSSVQWELPQVPVPAPRSGRKSSQDSDTPAQASPPEEKIKTLDKAGVLHRTKTVDKGKRLRKKHWNASWTVLEGGVLTFFKDSKTSAASGLRQPSKLSTPEYTVELRGASLSWAPKDKSSKKNVLELRSRDGSEYLIQHDSEAIISTWHKAIAEGIEELSADLPQREEGEPSSADFGSSERLGSWKEEDVRPNAASPSLNPGSQESDLSRVRHKLRKFLQRRPTLQSLREKGYIKDQVFGCALAQLCERERSPVPRFVQQCIRTVEARGLDIDGLYRISGNLATIQKLRYKVDHDERLDLDDGRWEDVHVITGALKLFFRELPEPLFPFSHFHQFIAAIKLQDPAQRSRCVRDLVRTLPAPNHDTLRLLIQHLCRVIEHGEQNRMSVQNVAIVFGPTLLRPEMEEASMPMTMVFQNQVVELILHQCADIFPPH
Protein: Protocatechuate 3,4-dioxygenase beta chain (EC 1.13.11.3) (3,4-PCD) (P20372)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Interaction partners:
- Protocatechuate 3,4-dioxygenase alpha chain
- p-hydroxybenzoate hydroxylase
- 3-carboxy-cis,cis-muconate cycloisomerase
- 4-carboxymuconolactone decarboxylase
- 3-oxoadipate enol-lactonase 1
- p-hydroxybenzoate hydroxylase transcriptional activator
- 4-hydroxybenzoate transporter PcaK
Sequence:
MSQIIWGAYAQRNTEDHPPAYAPGYKTSVLRSPKNALISIAETLSEVTAPHFSADKFGPKDNDLILNYAKDGLPIGERVIVHGYVRDQFGRPVKNALVEVWQANASGRYRHPNDQYIGAMDPNFGGCGRMLTDDNGYYVFRTIKPGPYPWRNRINEWRPAHIHFSLIADGWAQRLISQFYFEGDTLIDSCPILKTIPSEQQRRALIALEDKSNFIEADSRCYRFDITLRGRRATYFENDLT
Protein: RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (CTD phosphatase fcp1) (Q9P376)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription initiation factor IIF subunit alpha
- DNA-directed RNA polymerase II subunit rpb1
- DNA-directed RNA polymerase II subunit rpb7
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit rpb4
- Putative RNA polymerase II subunit B1 CTD phosphatase rtr1
- Transcription elongation factor spt5
- Transcription initiation factor IIF subunit beta
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MSKRLTPIHLPNSLNYPIEIASCLVPQGSYVKKGTPLLLYRFFTKVKEDQEDGSEVYVDREFVEQFECPVEGELVEWAVKKEESIENFSKIVAKLHEPCTHEVNYGGLCAICGKNITSQDYMGYSDMARANISMTHNTGDLTVSLEEASRLESENVKRLRQEKRLSLIVDLDQTIIHATVDPTVGEWMSDPGNVNYDVLRDVRSFNLQEGPSGYTSCYYIKFRPGLAQFLQKISELYELHIYTMGTKAYAKEVAKIIDPTGKLFQDRVLSRDDSGSLAQKSLRRLFPCDTSMVVVIDDRGDVWDWNPNLIKVVPYEFFVGIGDINSNFLAKSTPLPEQEQLIPLEIPKDEPDSVDEINEENEETPEYDSSNSSYAQDSSTIPEKTLLKDTFLQNREALEEQNKERVTALELQKSERPLAKQQNALLEDEGKPTPSHTLLHNRDHELERLEKVLKDIHAVYYEEENDISSRSGNHKHANVGLIIPKMKQKVLKGCRLLFSGVIPLGVDVLSSDIAKWAMSFGAEVVLDFSVPPTHLIAAKIRTEKVKKAVSMGNIKVVKLNWLTESLSQWKRLPESDYLLYPSYDLPDRNLSEHSYSSSSDDEQRISELNDRELDEIDWQAADQDVENALKDLSDDNDFDTGSISASQSQPEALEVNTPIKRKADLIQPSYNYDGEKRRKENDNHEGYDLLPNSSTKGEESAENENELDDLADIMEAELSKDTA
Protein: Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Dopamine receptor-interacting protein 5) (Repressor/activator protein 1 homolog) (RAP1 homolog) (hRap1) (Q9NYB0)
Organism: Homo sapiens (Human)
Function: Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q91VL8}. Cytoplasm {ECO:0000250|UniProtKB:Q91VL8}. Chromosome {ECO:0000250|UniProtKB:Q91VL8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q91VL8}. Note=Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex. {ECO:0000250|UniProtKB:Q91VL8}.
Interaction partners:
- Telomeric repeat-binding factor 2
- TERF1-interacting nuclear factor 2
- Telomeric repeat-binding factor 1
- Protection of telomeres protein 1
- Adrenocortical dysplasia protein homolog
- X-ray repair cross-complementing protein 6
- Structure-specific endonuclease subunit SLX4
- 5' exonuclease Apollo
- X-ray repair cross-complementing protein 5
- Double-strand break repair protein MRE11
Sequence:
MAEAMDLGKDPNGPTHSSTLFVRDDGSSMSFYVRPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGEALAEASGDFISTQYILDCVERNERLELEAYRLGPASAADTGSEAKPGALAEGAAEPEPQRHAGRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYLLGDAPVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQENEEAVKKMLVEATREFEEVVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEEEEEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFLASGQRADGYPIWSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKK
Protein: Transmembrane protein 230 (Q96A57)
Organism: Homo sapiens (Human)
Function: Involved in trafficking and recycling of synaptic vesicles.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:27270108}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:27270108}. Early endosome {ECO:0000269|PubMed:27270108}. Recycling endosome {ECO:0000269|PubMed:27270108}. Late endosome {ECO:0000269|PubMed:27270108}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:27270108}.
Interaction partners:
- DnaJ homolog subfamily C member 13
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 2
Sequence:
MMPSRTNLATGIPSSKVKYSRLSSTDDGYIDLQFKKTPPKIPYKAIALATVLFLIGAFLIIIGSLLLSGYISKGGADRAVPVLIIGILVFLPGFYHLRIAYYASKGYRGYSYDDIPDFDD
Protein: Growth hormone (H6UQ67)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPHETVATFPTMPLSNMFANAVLRAQHLHLLAAETYKEFERTYIPEDQRYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMELLRFSLVLIQSWLTPVQYLSKVFTNNLVFGTKKRVFEKLKDLEEGLQPLMRELEDRSPRGPQLLRPTYDKFDIHLRNEDALLKNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: T-cell surface glycoprotein CD3 epsilon chain (T-cell surface antigen T3/Leu-4 epsilon chain) (CD antigen CD3e) (P22646)
Organism: Mus musculus (Mouse)
Function: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development. Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24470497}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07766}.
Interaction partners:
- T-cell surface glycoprotein CD3 gamma chain
- T-cell surface glycoprotein CD3 delta chain
- T-cell surface glycoprotein CD3 zeta chain
- Tyrosine-protein kinase ZAP-70
- SH2/SH3 adapter protein Nck1
- Tyrosine-protein kinase SYK
- T-cell surface glycoprotein CD8 alpha chain
- Tyrosine-protein kinase Fyn
- Proto-oncogene tyrosine-protein kinase LCK
- T-cell surface glycoprotein CD4
Sequence:
MRWNTFWGILCLSLLAVGTCQDDAENIEYKVSISGTSVELTCPLDSDENLKWEKNGQELPQKHDKHLVLQDFSEVEDSGYYVCYTPASNKNTYLYLKARVCEYCVEVDLTAVAIIIIVDICITLGLLMVIYYWSKNRKAKAKPVTRGTGAGSRPRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRAV
Protein: Parkin coregulated gene protein (Molecular chaperone/chaperonin-binding protein) (PARK2 coregulated gene protein) (Q96M98)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9DAK2}.
Interaction partners:
- Meiosis expressed gene 1 protein homolog
- EF-hand domain-containing protein 1
- Enkurin
- EF-hand domain-containing family member C2
- EF-hand domain-containing family member B
- Cilia- and flagella-associated protein 20
- E3 ubiquitin-protein ligase parkin
- WD repeat-containing protein 90
- Cilia- and flagella-associated protein 107
- Cilia- and flagella-associated protein 45
Sequence:
MVAEKETLSLNKCPDKMPKRTKLLAQQPLPVHQPHSLVSEGFTVKAMMKNSVVRGPPAAGAFKERPTKPTAFRKFYERGDFPIALEHDSKGNKIAWKVEIEKLDYHHYLPLFFDGLCEMTFPYEFFARQGIHDMLEHGGNKILPVLPQLIIPIKNALNLRNRQVICVTLKVLQHLVVSAEMVGKALVPYYRQILPVLNIFKNMNGSYSLPRLECSGAIMARCNLDHLGSSDPPTSASQVAEIIVNSGDGIDYSQQKRENIGDLIQETLEAFERYGGENAFINIKYVVPTYESCLLN
Protein: Plasma phospholipid transfer protein (Q8WMN7)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MALLGALFLVLLAGAHAELPGCKIRITSKALELVKQEGLRFLEQELETITIPDLRGREGHFYYNISEVKVTELQLTSSELHFQPEQELMLQINNGSLGLRFRRQLLYWFFYDGGYINASAEGVSIHTALQLSRDPTGRIKVSNVSCQASVSRMHAAFGGTFKKVYEFLSTFITSGMRFLLNQQICPVLYHAGMVLLNSLLDTVPVRGAVDELVGIDYSLLKDPVASTSNLDMEFRGAFYPLAEGNWSLPNRRVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALKLSLVGDKVPHDLDMLLRATYFGSIVLLSPAVIDSPLKLELRVMAPPRCTIKPSGTTISVTASVTIALVPPGQPEVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNQSALESLALIPLQAPLKTMLQIGVMPMLNERTWRGVQIPLPEGINFVREVVTNNAGFLTIGADLHFAKGLREVIEKNRPADTRGPQASSAPPPSTAAV
Protein: Auxin-responsive protein SAUR40 (Protein SMALL AUXIN UP RNA 40) (O64538)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion. Plays a role in the regulation of cell expansion, root meristem patterning and auxin transport (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23759547}.
Interaction partners:
- Auxin-responsive protein SAUR77
Sequence:
MKPLIRRLSRIADSSSCNRNRSGDIHHPTSTYSSSVFLVKRATVASSVPSGHVPVNVGEDKERFVVSAELLNHPVFVGLLNRSAQEYGYTQKGVLHIPCNVFVFEQVVESLRSGIADDTSELIASLSGEDVSTE
Protein: FHA domain-containing protein (Q583Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTTGSWTIERSDGVIVKIDKPNVSFRFGRGKELPPGQQLNDKYISRNHISFECKSSSLFAKQSGRNPTFYSAAFRQVPRAGLEFRPADANKTSAAQPDGSGNKNEENIVFVPCGNEKTNQVVISSSGNEIELCTLHFPEELRLPKLTVRYTPPRIEKVDHMPRGVPAVPLVFPKDDDDDDDDDNNNNNNSHGSTPPAWRGILDAVLQSNKGSDS
Protein: DNA (cytosine-5)-methyltransferase CMT3 (EC 2.1.1.37) (Chromomethylase 3) (OsCMT3a) (C0SQ89)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in CpXpG DNA methylation. Plays a critical role in the maintenance of CpXpG DNA methylation and suppression of a wide spectrum of transposable element (TE) activities. Required for proper plant development in reproductive stage.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Os03g0786900 protein
- Trafficking protein particle complex subunit
- DNA
- DNA
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Os03g0746600 protein
- Os09g0244900 protein
Sequence:
MAPSSPSSAAAPTRTSTRKRAASASASAKATDEPSTKRTRRPKAETKPRKKKDEVKEEEKPPMEDDACGEEPDAEEMALGEEAEAEEAEAEQKQLDAPAPGVARKRVAQPSRVRHGSDGDHDPEFVGDPFPAKEARDKWPQRYQRNAATRRPDEEEDIKARCHYSSAKVDGTLYCLHDDVYVKAEEDKADYIGRITEFFEGTDHCHYFTCRWFFRAEDTVISSIMMENADDEKHDLKRVFLSEEKNDNVLDCIISKVKIVYIDPNMESEAKARRLADCDLYYDMSYTVAYSTFANIPLENGASGSDTASDISSDDVDSSKGKVVSDSEASSVGKATLLDLYSGCGGMSTGLCLGAALAGLNLETRWAVDFNSFACESLKYNHPRTEVRNEKADEFLALLKGWHSLCDEYVKKDIDFSSAGASENEEDDDEPLEKDEFVVEKLAGICYGGSGREDGLYFKVQWKGYGREEDTWEPIENLRDCPLKIKEFVQEGYRRKILPLPGDVDVICGGPPCQGISGFNRFRNRKEPLKDEKNKQMVTFMDIVAYLKPKYVLMENVVDILKFADGYLGRYALSRLVAMKYQARLGMMVAGCYGLPQFRMRVFLWGALPTMVLPKYPLPTHNVVVRGGAPNAFSQSIVAYDETQKPTLKNALLLGDAISDLPEVNNHQPNEVMEYGSSPKTEFQRYIRLSRKEMLDSSFEGKDGPDLGKLLDHQPLKLNKDDHERVQQIPVKKGANFRDLKGVRVGANNIVEWDPDVPRVYLSSGKPLVPDYAMSFIKGRSLKPFGRLWWDETVPTVVTRAEPHNQIILHPNQARVLTVRENARLQGFPDYYKMFGPIKEKYIQVGNAVAVPVARALGYSLGLAYQRESEGSSPLFVLPDSFTEVGRQAAPARASSVGIPVGEVVEQ
Protein: Dihydropyrimidinase (EC 3.5.2.2) (Dihydropyrimidine amidohydrolase) (Protein PYRIMIDINE 2) (Q9FMP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamoyl-alanine and of 5,6-dihydrothymine to N-carbamoyl-amino isobutyrate. Involved in the recycling of nitrogen from nucleobases to general nitrogen metabolism.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:19413687}.
Interaction partners:
- Dihydropyrimidine dehydrogenase
- Beta-ureidopropionase
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase, chloroplastic
- Uridine 5'-monophosphate synthase
- Carbamoyl phosphate synthase small chain, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Vesicle transport protein GOT1
- At3g49420
- Got1/Sft2-like vescicle transport protein family
Sequence:
MALDAFFFIVSLFLLFPSPSASESTTQFCSAGRENGVGSCGVSSTRILIKGGTVVNAHHQELADVYVENGIIVAVQPNIKVGDEVTVLDATGKFVMPGGIDPHTHLAMEFMGTETIDDFFSGQAAALAGGTTMHIDFVIPVNGNLVAGFEAYENKSRESCMDYGFHMAITKWDEGVSRDMEMLVKEKGINSFKFFLAYKGSLMVTDDLLLEGLKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPVLEGEATARAIRLARFINTPLYVVHVMSVDAMDEIAKARKSGQKVIGEPVVSGLILDDHWLWDPDFTIASKYVMSPPIRPVGHGKALQDALSTGILQLVGTDHCTFNSTQKALGLDDFRRIPNGVNGLEERMHLIWDTMVESGQLSATDYVRITSTECARIFNIYPRKGAILAGSDADIIILNPNSSYEISSKSHHSRSDTNVYEGRRGKGKVEVTIAGGRIVWENEELKVVPRSGKYIEMPPFSYLFDGIEKSDANYLSSLRAPVKRVRTEAT
Protein: T cell receptor alpha variable 27 (A0A087WT01)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition. Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens. Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation. The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity.
Subcellular location: Cell membrane {ECO:0000303|PubMed:20452950}.
Interaction partners:
Sequence:
MVLKFSVSILWIQLAWVSTQLLEQSPQFLSIQEGENLTVYCNSSSVFSSLQWYRQEPGEGPVLLVTVVTGGEVKKLKRLTFQFGDARKDSSLHITAAQTGDTGLYLCAG
Protein: Uncharacterized protein (Q8IC42)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MAYPLLEDDLRSIRVAFGTCPGNSTMQFGERFWQGFFFGVIIFFVLSKYIRSYKKRKGMRILKSSSVTKGRLYRGTVFDEDDNVDGHHKKTKAHGLFEEIEKRNGFDLNDDTTNSNNLGEGTHSAVHNLDGQKESQLYKNNSDGSTENHLSGSNSDGRNSSQHSVGSHSVSSQEHKKEHSTHDLPAGRNYSLGNLSTGTTSQGSTSSRHYSLGGQPSSSGRSFSGSKYNTSNLASSSTTESSVSGLNTNEAHV
Protein: BZIP domain-containing protein (G5EBE5)
Organism: Caenorhabditis elegans
Interaction partners:
- Transcription factor zip-10
- Bestrophin homolog
- Solute carrier organic anion transporter family member
Sequence:
MSDYCSNDASPFGDYDLPSDEPSPKYQKLNKNIFSPLSPTFELKFQSKLRVSGNSTSSTTSDDSDDESLHRSNQLKHLETLFKESILRTSFSRPGVSNTSCDEKLDLVSEDEKKRLRNTEAARRCREKIKRKTDDLETELTRLTARNEVMNQHRIRLLSQVEEQMRMLENIKSRNPELEAEIRYEAKKIVDTYTHQVETKRKAIQDYFDMTCNKLY
Protein: Microtubule-associated protein ssm4 (O42667)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to nuclear microtubules with the effect of either modifying their structure or function. This then promotes meiotic nuclear division.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Note=Mitotic spindle.
Interaction partners:
- Dynein heavy chain, cytoplasmic
- Microtubule integrity protein mal3
- Centractin
- Dynein intermediate chain 1
- Actin-like protein arp10
- Meiotically up-regulated gene 5 protein
- Meiotically up-regulated gene 1 protein
- Probable prefoldin subunit 6
- Meiotic coiled-coil protein 2
Sequence:
MSYLSVGDEVLIRGELGIVRFAGSTDFESGIWLGVELLNGKGKNDGSVKGKRYFSCEKGKGIFVRACSSNVMKRPSVVKSRKKGSENISNFMEKTKAIKQKSRREPSKFERSLARPLCITPIDSSTPTKTATFYTSSTTENLDELNFSTEELSSFDTTLLNSDTSKLSGLDDSSFMEEEFVWQVDNVLQECEKKFTPHSKGSYLKENLKSELRKGRLDELMCENTALKEKIDKLNKELEKVEPQLTFLRSKNSIEKPRNFRREKFLKKFLAMQKEIKYLRKRKLQIRKIPNYKYSDRSLNSKTPKSQDNWTTQVTPSSLLGVSEVSKVLQLKQVQVDITELVKIPKNPFSEKLTISNVNRYLNIVPGSLDLQFSLTNENFVHWNSTVYQELLNLKSNNSSVDGVKTRRQLLEENALLSHKVLKLTEEIQDLETLNQLNTEIEARQSEKLNEVQEETQRLSQLLISSQPALTEVKHLKLCLSDSQEELLQLNAKLEKANIVIDELNSAKLKLSKQVEEESSMKDDLTEMNQRLKEQIESYENEVNSEITSRTLKEFETLKTQYEKNLCNLREQLKTARMKLADKYPQGDNTSENIDWLKHSLRDSNTENSIPSPLTFACKEIRKLVADIKPVSVEKQLALNWKKDIERPSFHHNQQLFNYCQLTDILSKKC
Protein: Laminin beta-1 chain (Q95LE2)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
KYFQMSLEAEERVNASTTDSNSTVEQSALIRDRVEDLMLEQESQFRDKQEEQARLLDELAGKLQSLDLSTAAELTCGTPPGASCSETECGGPNCRTDEGQEKCGGPGCGGLVTVAHSAWQKAMDFDQDVLSAL
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (Q381K5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
- NADH-ubiquinone oxidoreductase complex I subunit
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Uncharacterized protein
- Flavoprotein monooxygenase, putative
- Uncharacterized protein
- Sulfotransferase
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MMRRCFPLLSAGMVEYHEWHLHEPLLQNYEGWRILDNPKYERKSDAYIYDFTGCVRHLDPIIDDPRLTHKQRVCRLYRWALKELQMWLVQLNAHKFNLAYKVVRRRFEMYRYVTDPATCDMMVRQTQKYLRENACFYYLRRNNASPWSTATLANPMFHPDGAQVYDHWTHPEVLWYDDAKLHRWTGHHPMYGSAGEASDRFGDMDVAPHLRFFTTVVFGMVFLWAILNFLAFFDRDEDVHFKEWCSAFSDDLKGALYAAERNSRSHTSMLGWDWDRIMGKVQQDEGFHLYDVDFAAAGSNIARR
Protein: Cryptochrome circadian regulator 2 (A0A0D2X7Z3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGVHVAYRGGAGVAGAVWTVMAATVATAAAVAPAPAPGTDSASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQAIISRMELPKKPVGLVTSQQMESCRAEIQENHDETYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKAFPSRYIYEPWNAPESIQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPSSSQAGSMSSAGPRPLPSGPASPKRKLEAAEEPPGEELSKRARVAELPTPELPSKDA