wanglab/gogpt-training-data huggingface dataset:
Protein: RAC-gamma serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-3) (Protein kinase B gamma) (PKB gamma) (RAC-PK-gamma) (STK-2) (Q9Y243)
Organism: Homo sapiens (Human)
Function: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20018949}. Cytoplasm {ECO:0000269|PubMed:20018949}. Membrane {ECO:0000269|PubMed:20018949}; Peripheral membrane protein {ECO:0000269|PubMed:20018949}. Note=Membrane-associated after cell stimulation leading to its translocation.
Interaction partners:
- PH domain leucine-rich repeat-containing protein phosphatase 2
- PH domain leucine-rich repeat-containing protein phosphatase 1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Tuberin
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Forkhead box protein O1
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE
Protein: Neuroplastin (Stromal cell-derived receptor 1) (SDR-1) (Q9Y639)
Organism: Homo sapiens (Human)
Function: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). Also acts as a chaperone for ATP2B1; stabilizes ATP2B1 and increases its ATPase activity. Promotes localization of XKR8 at the cell membrane.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P97546}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P97546}.; SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density {ECO:0000250|UniProtKB:P97546}.
Interaction partners:
- Erythropoietin receptor
- Ubiquitin-like protein FUBI
- Plasma membrane calcium-transporting ATPase 1
- Basigin
Sequence:
MSGSSLPSALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRDSPVLPVTLQCNLTSSSHTLTYSYWTKNGVELSATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDATMYCKSVGYPHPDWIWRKKENGMPMDIVNTSGRFFIINKENYTELNIVNLQITEDPGEYECNATNAIGSASVVTVLRVRSHLAPLWPFLGILAEIIILVVIIVVYEKRKRPDEVPDDDEPAGPMKTNSTNNHKDKNLRQRNTN
Protein: E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33) (Q99PP7)
Organism: Mus musculus (Mouse)
Function: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway (By similarity). May act as a transcriptional repressor (By similarity). Inhibits the transcriptional response to TGF-beta/BMP signaling cascade (By similarity). Plays a role in the control of cell proliferation (By similarity). Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor. Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15314655, ECO:0000269|PubMed:16751102}. Note=In discrete nuclear dots resembling nuclear bodies (PubMed:15314655, PubMed:16751102). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9UPN9, ECO:0000269|PubMed:15314655, ECO:0000269|PubMed:16751102}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 4
- Cell division cycle protein 20 homolog
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 1
- Cyclin-A2
- Anaphase-promoting complex subunit 7
- Cell division cycle protein 23 homolog
- Cell division cycle protein 16 homolog
Sequence:
MAENKGGGEAESGGGGSGSAPVTAGAAGPTAQEAEPPLAAVLVEEEEEEGGRAGAEGGAAGPDDGGVAAASSSSAPAASVPAASVGSAVPGGAASTPAPAAAPAPAPAPAPAPAPAPAPAPAPGSSSGPPLGPPASLLDTCAVCQQSLQSRREAEPKLLPCLHSFCLRCLPEPERQLSVPIPGGSNGDVQQVGVIRCPVCRQECRQIDLVDNYFVKDTSEAPSSSDEKSEQVCTSCEDNASAVGFCVECGEWLCKTCIEAHQRVKFTKDHLIRKKEDVSESVGTSGQRPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQKGAIENLLAKLLEKKNYVHFAATQVQNRIKEVNETNKRVEQEIKVAIFTLINEINKKGKSLLQQLENVTKERQMKLLQQQNDITGLSRQVKHVMNFTNWAIASGSSTALLYSKRLITFQLRHILKARCDPVPAANGAIRFHCDPTFWAKNVVNLGNLVIESKPAPGYTPNVVVGQVPPGTNHISKTPGQINLAQLRLQHMQQQVYAQKHQQLQQMRLQQPPAPIPTTTATTQQHPRQAAPQMLQQQPPRLISVQTMQRGNMNCGAFQAHQMRLAQNAARIPGIPRHSAPQYSMMQPHLQRQHSNPGHAGPFPVVSAHNPINPTSPTTATMANANRGPTSPSVTAIELIPSVTNPENLPSLPDIPPIQLEDAGSSSLDNLLSRYISGSHLPPQPTSTMNPSPGPSALSPGSSGLSNSHTPVRPPSTSSTGSRGSCGSSGRTAEKSAHSFKSDQVKVKQEPGTEEEICSFSGAVKQEKTEDGRRSACMLSSPESSLTPPLSTNLHLESELDTLTGLENHVKTEPTDISESCKQSGLSNLVNGKSPIRNLMHRSARIGGDGNSKDDDPNEDWCAVCQNGGDLLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCRDIGKPEVEYDCDNMQHSKKGKTAQGLSPVDQRKCERLLLYLYCHELSIEFQEPVPVSIPNYYKIIKKPMDLSTVKKKLQKKHSQHYQIPDDFVADVRLIFKNCERFNEMMKVVQVYADTQEINLKGDSEVAKAGKAVALYFEDKLSEIYSDRTFTPLPEFEQDEDDGEVTEDSDEDFIQPRRKRLKSDERPVHIK
Protein: Chaperonin 60 subunit alpha 2, chloroplastic (CPN-60 alpha 2) (Protein EMBRYO DEFECTIVE 3007) (Q56XV8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein assisted folding.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- 10 kDa chaperonin 2, chloroplastic
- 10 kDa chaperonin 1
- NAD
- tRNA wybutosine-synthesizing protein 2/3/4
- Heat shock 70 kDa protein 6, chloroplastic
- Zinc finger CCCH domain-containing protein 24
- Protein groES
- Oxysterol-binding protein-related protein 1D
- AT3g17020/K14A17_14
Sequence:
MFAVSPSSFSPTTISPRRSGQRNEPRKFSVVRAGAKRILYGKDSREKLQAGIDKLADAVSITLGPRGRNVVLAEKDTIKVINDGVTIAKSIELPDTIENAGATLIQEVAIKMNESAGDGTTTAIILAREMIKAGSLAIAFGANAVSVKNGMNKTVKELVRVLQMKSIPVQGKNDIKAVASISAGNDEFVGNLIAETVEKIGPDGVISIESSSTSETSVIVEEGMKFDKGYMSPHFITNQEKSTVEFDKAKILVTDQKITSAKELVPLLEKTSQLSVPLLIIAEDISAEVLEILVVNKKQGLINVAVVKCPGMLDGKKALLQDIALMTGADYLSGDLGMSLMGATSDQLGVSRRVVITANSTTIVADASTKPEIQARIAQMKKDLAETDNSYLSKKIAERIAKLTGGVAVIKVGGHTETELEDRKLRIEDAKNATFAAMREGIVPGGGATYIHLLDEIPRIKKNLMEDSYEQIGADIVAMALTAPAMAIATNAGVDGSVVVQKTRELEWRSGYNAMSGKYEDLLNAGIADPCRVSRFALQNAVSVAGIILTTQAVLVEKIKQPKPAVPQVPGIPTS
Protein: Leiomodin-1 (64 kDa autoantigen 1D) (64 kDa autoantigen 1D3) (64 kDa autoantigen D1) (Leiomodin, muscle form) (Smooth muscle leiomodin) (SM-Lmod) (Thyroid-associated ophthalmopathy autoantigen) (P29536)
Organism: Homo sapiens (Human)
Function: Required for proper contractility of visceral smooth muscle cells. Mediates nucleation of actin filaments.
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:26370058}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0A0G2K0D3}. Note=Colocalizes with actin filaments in sarcomeres. {ECO:0000250|UniProtKB:A0A0G2K0D3}.
Interaction partners:
- Myosin-11
- Actin, alpha skeletal muscle
- Caldesmon
- Cleavage stimulation factor subunit 2
- Actin, gamma-enteric smooth muscle
- Myosin regulatory light polypeptide 9
- Myosin light chain kinase, smooth muscle
- Calponin-1
- Tropomyosin alpha-1 chain
- Actin, aortic smooth muscle
Sequence:
MSRVAKYRRQVSEDPDIDSLLETLSPEEMEELEKELDVVDPDGSVPVGLRQRNQTEKQSTGVYNREAMLNFCEKETKKLMQREMSMDESKQVETKTDAKNGEERGRDASKKALGPRRDSDLGKEPKRGGLKKSFSRDRDEAGGKSGEKPKEEKIIRGIDKGRVRAAVDKKEAGKDGRGEERAVATKKEEEKKGSDRNTGLSRDKDKKREEMKEVAKKEDDEKVKGERRNTDTRKEGEKMKRAGGNTDMKKEDEKVKRGTGNTDTKKDDEKVKKNEPLHEKEAKDDSKTKTPEKQTPSGPTKPSEGPAKVEEEAAPSIFDEPLERVKNNDPEMTEVNVNNSDCITNEILVRFTEALEFNTVVKLFALANTRADDHVAFAIAIMLKANKTITSLNLDSNHITGKGILAIFRALLQNNTLTELRFHNQRHICGGKTEMEIAKLLKENTTLLKLGYHFELAGPRMTVTNLLSRNMDKQRQKRLQEQRQAQEAKGEKKDLLEVPKAGAVAKGSPKPSPQPSPKPSPKNSPKKGGAPAAPPPPPPPLAPPLIMENLKNSLSPATQRKMGDKVLPAQEKNSRDQLLAAIRSSNLKQLKKVEVPKLLQ
Protein: Mini-ribonuclease 3 (Mini-3) (Mini-RNase 3) (EC 3.1.26.-) (Mini-RNase III) (Mini-III) (A0A0H2UNY0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}.
Interaction partners:
Sequence:
MIDVNLINGIALAFEGDAVYSMYIRRHLILKGMTKPNKLHQEATKYVSAKAQARLIALMLEEQVLTEKEEEIYKRGRNTNSHTKAKNADVVTYRMSTGFEAVMGYLHMTENLERLESLVSWCIQKVEG
Protein: Putative L-lactate dehydrogenase operon regulatory protein (P0ACL7)
Organism: Escherichia coli (strain K12)
Function: May be a regulatory protein for the LCT genes.
Interaction partners:
- L-lactate dehydrogenase
- L-lactate permease
- Fatty acid metabolism regulator protein
Sequence:
MIVLPRRLSDEVADRVRALIDEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRWRHDTWSEQNIVQPLKTLMADDPDYSFDILEARYAIEASTAWHAAMRATPGDKEKIQLCFEATLSEDPDIASQADVRFHLAIAEASHNIVLLQTMRGFFDVLQSSVKHSRQRMYLVPPVFSQLTEQHQAVIDAIFAGDADGARKAMMAHLSFVHTTMKRFDEDQARHARITRLPGEHNEHSREKNA
Protein: Leucine-rich repeat protein kinase family protein (Leucine-rich repeat receptor-like protein kinase) (Putative receptor kinase) (Receptor-kinase like protein) (Q9SN80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKLFLLLSFSAHLLLGADGFTDETDRQALLEFKSQVSEGKRDVLSSWNNSFPLCNWKWVTCGRKHKRVTHLNLGGLQLGGIVSPSIGNVSFLISLDLSDNAFGGIIPREVGNLFRLEHLYMAFNSLEGGIPATLSNCSRLLNLDLYSNPLRQGVPSELGSLTKLVILDLGRNNLKGKLPRSLGNLTSLKSLGFTDNNIEGEVPDELARLSQMVGLGLSMNKFFGVFPPAIYNLSALEDLFLFGSGFSGSLKPDFGNLLPNIRELNLGENDLVGAIPTTLSNISTLQKFGINKNMMTGGIYPNFGKVPSLQYLDLSENPLGSYTFGDLEFIDSLTNCTHLQLLSVGYTRLGGALPTSIANMSTELISLNLIGNHFFGSIPQDIGNLIGLQRLQLGKNMLTGPLPTSLGKLLRLGLLSLYSNRMSGEIPSFIGNLTQLEILYLSNNSFEGIVPPSLGKCSHMLDLRIGYNKLNGTIPKEIMQIPTLVNLSMEGNSLSGSLPNDIGSLQNLVKLSLENNKFSGHLPQTLGNCLAMEQLFLQGNSFDGAIPNIRGLMGVRRVDLSNNDLSGSIPEYFANFSKLEYLNLSINNFTGKVPSKGNFQNSTIVFVFGNKNLCGGIKDLKLKPCLAQEPPVETKHSSHLKKVAILVSIGIALLLLLVIASMVLCWFRKRRKNQQTNNLVPSKLEIFHEKISYGDLRNATNGFSSSNMVGSGSFGTVFKALLPTESKIVAVKVLNMQRRGAMKSFMAECESLKDTRHRNLVKLLTACASTDFQGNEFRALIYEYLPNGSVDMWLHPEEVEEIRRPPRTLTLLERLNIVIDVASVLDYLHVHCHEPIAHCDLKPSNVLLEDDLTAHVSDFGLARLLLKFDKESFLNQLSSAGVRGTIGYAAPEYGMGGQPSIHGDVYSFGVLLLEMFTGKRPTDELFGGNLTLHSYTKLALPEKVFEIADKAILHIGLRVGFRTAECLTLVLEVGLRCCEEYPTNRLATSEVAKELISIRERFFKTRRTPRR
Protein: Probable 26S proteasome regulatory subunit p27 (Proteasome non-ATPase subunit 2) (P40555)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process.
Interaction partners:
- 26S proteasome regulatory subunit 6A
- 26S proteasome subunit RPT4
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit RPN2
- 26S proteasome regulatory subunit 7 homolog
- Probable 26S proteasome regulatory subunit p28
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN5
Sequence:
MEEEELSKLLANVKIDPSLTSRISQIDSFKLSELMVLKTDIETQLEAYFSVLEQQGIGMDSALVTPDGYPRSDVDVLQVTMIRKNVNMLKNDLNHLLQRSHVLLNQHFDNMNVKSNQDARRNNDDQAIQYTIPFAFISEVVPGSPSDKADIKVDDKLISIGNVHAANHSKLQNIQMVVMKNEDRPLPVLLLREGQILKTSLTPSRNWNGRGLLGCRIQEL
Protein: Pinin (Q66HU9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, desmosome {ECO:0000256|ARBA:ARBA00004568}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
KMAVAVRSLQDQLEKAKEGLKSVDENIRKLTGRDPGELRPGQNRRLTIPGPGGGRGRGINLLRRGLSDSGGGPPAKLRDIDGALLRLAGDQRARRDSRHDSDAEDDDDVKKPALQSSVVATSKERTRRDLIQDQTMDERGKQRNRRMFGLLMGTLQKFKQESTVSTERLKRRQEIEQKLEVQAEQERKKVECERRELFEERRAKQTELRLLEHKVELAQLQEDWNAHNSKLIKFIRTKTKPPIFYLPGRMCSATQKLLEESQKKLNGVFDERREAFAEQINKMEARPRRQSQRTGDKEMEGSRRAEETKKEDQEEGKAGAGRAGNRHVVEMEDEDEDVVEEEAEESSEVRERDEDQEQEQEQGEEKEEKNEESERKAEEDEEEEDEDPGAVEVKEDEEEQMEVTEVVGEVEAQGKLQVESPEATVEEVGNVRIEEEQEVESETQQEVTADSQQTPESQTETQPEESKEPQADAPSPNETQQDSKEEEAAVPESQQLQAEPEPEPEVPSQEPSQELSEEPQAAKTDTKEAGEEADDARGRAKVRAKKSKSRSSSSSSSSSSSSSSSSGSSSSSSGSSSSSSGSSSSSSSRSRSRGRDRENRDHKRRRRPSDRERRRSGSERAHKSSKSSGREGKGSKDKTSKPDRKRTSSEGRRSRSERDRKSDRKDRR
Protein: Single-stranded DNA-binding protein WHY2, mitochondrial (Protein WHIRLY 2) (AtWHY2) (Q8VYF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Single-stranded DNA-binding protein that associates with mitochondrial DNA and may play a role in the regulation of the gene expression machinery. Seems also to be required to prevent break-induced DNA rearrangements in the mitochondrial genome. Can bind to melt double-stranded DNA in vivo.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15967440, ECO:0000269|PubMed:18423020, ECO:0000269|PubMed:22762281}.
Interaction partners:
- DNA repair protein recA homolog 2, mitochondrial
- Protein OSB1, mitochondrial
- DNA repair protein recA homolog 3, mitochondrial
- Protein OSB3, chloroplastic/mitochondrial
- DNA repair RAD52-like protein 1, mitochondrial
- DNA mismatch repair protein MSH1, mitochondrial
- SWIB/MDM2 domain superfamily protein
- Single-stranded DNA-binding protein
- DNA polymerase I B, chloroplastic/mitochondrial
- Protein OSB4, chloroplastic
Sequence:
MMKQARSLLSRSLCDQSKSLFEASTLRGFASWSNSSTPGRGFPGKDAAKPSGRLFAPYSIFKGKAALSVEPVLPSFTEIDSGNLRIDRRGSLMMTFMPAIGERKYDWEKKQKFALSPTEVGSLISMGSKDSSEFFHDPSMKSSNAGQVRKSLSVKPHADGSGYFISLSVNNSILKTNDYFVVPVTKAEFAVMKTAFSFALPHIMGWNRLTGHVNTEALPSRNVSHLKTEPQLELEWDK
Protein: Expansin-B3 (At-EXPB3) (AtEXPB3) (Ath-ExpBeta-1.6) (Beta-expansin-3) (Q9M0I2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular location: Secreted, cell wall. Membrane; Peripheral membrane protein.
Interaction partners:
- Transglycosylase
- Endonuclease 1
- Auxin transporter protein 1
- Basic leucine zipper 8
- Sucrose synthase 1
- Alpha-L-arabinofuranosidase 1
- Alpha-L-arabinofuranosidase 2
- Floral homeotic protein APETALA 2
- Xyloglucan endotransglucosylase/hydrolase protein 9
- Sucrose synthase 2
Sequence:
MQLFPVMLATLCIVLQLLIGSSALATTNRHVSNSHWLPAVATWYGSPNGDGSDGGACGYGTLVDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGCSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRRTACKYRGKNIAFHVNEGSTDFWLSLLVEFEDGEGDIGSMHIRQAGAREWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSATDVVPRNWAPKATYSSRLNFSPVL
Protein: Copine-C (Q54P51)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MIPSSKPNSRVELRFRCHHLKNLDIVSKSDPQIFISEKRGPGGFQFVDCTEKIKNNLSPEFKKTITLDYYFEEIQTLTFTVMDIDKEITLFGDLDKNDKIGEFTTSLSNILSRPGRKIVADLIHHSKVTGKIEISAEEICQTNHHIFLSAEGIGLDKKDLFSSDPYYKIYKTNPNGEQLLVFQSIVIKSNVNPLWPELHMELEKFNGGDMFRELLIEVYDYDSIGAHDLIGITRTTTDAILRGVIEYPLINPKKTSKSGYKNSGILKFYKVRLEKTHTFLEFLAGGCEISLMTAIDCTGSNGSVNSFSGLHYNDLEKGGSAYARSIASVGSVLSSYDSDGFIDVFGFGGEYQGRTSHCFPFSLDPNVPSAFGVAGVLEMYNRNISKIPFSGPTNFASVIQEAIARASESRLPYQQKYTVLLIITDGEICDMDETIKCLVQASNLPLSVVIVGVGLSSFENMNLLDGDNGCLVDYKGNRAKRDIVQFVPFNKYSGNINALAQETLKEIPGQLLSYFKSIGVPPNPPRTFIPVDILPPPPQ
Protein: candidapepsin (EC 3.4.23.24) (G8B6Z1)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKFIYNVSLTATLLSLIPIASSATVAAAAPANASPPQGSFKIDFNVRRGSSKENLSPIDDQKPRFVKRADEDGSFNMELINEQTFYLAELHIGSNKDKNDVLVDTGSSDLWVMSHDLNCVSASSSSGSSKRRKRDPKNVFGHISGTGVKFPFEAEQEDTKKEREDQTEQEQTQQEQKRETPSKSEDVVEDANKRADSYYTTIYLSEMPDGTNLPAPGGGIGSGSSSSRGSGSGSNTCTSYGSFNTGNSDTFKRNDTGSFQIQYADGTFATGIWGHDTVRIGDISVPDLSFAIANETSSDIGVLGIGLPGLETTTSFGYMYENLPMKMKSDGVIKRVLYSLYLDQADADSGSLLFGAIDHAKYEGTLETVPMLKTYRQIDYPVRFEVEVGNITLNNNQGVTANVMTDSVGAVLDSGSTLSYLYSEQIEAVGEALHGRYSSSAGAYIVDCRFLNTNSTLDIQFGGKTIKVPVSDLVLQASRSTCYLGLFEQSSSSSYILFGDNVLRSAYIVYDLEEYEVHIGQVYYTDDEDIEVVDGSVSTGGGQNSTRVGGGSGSGSSSSSSSSSSSSAGNKNGASSMFSLSWACVFAGVMVSVVSTL
Protein: F-box protein At3g26010 (Q9LU90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription regulator
- Transcription regulator NOT2/NOT3/NOT5 family protein
Sequence:
METRNRTIHLTDAIWTEILARLPLRIIARFKSVSKTWKSTIESVYFRRLFVSVHRKSSTSWSLMWYGQKDLVGFHGCETWGLPKSLSFYIPSSLCIIEGSSHGLVLISENDDDCCFVGNPVLQQWIKIPPPPVHSSVFGLVSRVDDDGFVLGFKVVKLAEVIVTNNYVSCSLSVFVYSSETGIWTCKTIHCPYQITNFGSFTLDGTIYFDHLSEPGVLVAYDFYSEISDQFWVIPLPDHPNHGFNSDFKGALTTSQGFVMYIRTLAQSSSNVFKAWRLNNDSTWQLLWKIGLPSLIGDYVPMAMHPFDSDIVHLWSQDHRHVVSWNLRTQKNRILGAEDNDEDHKDCYLNQPVCEECMDEICGCKASVRLLQLVLPRWMESVPCPPQVEMMNTASVISYVTSMQETMIRNWLHQ
Protein: Beta-glucosidase 21 (AtBGLU21) (EC 3.2.1.21) (Protein PHOSPHATE STARVATION-RESPONSE 3.2) (Q9C525)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-D-glucosidase active on scopolin >> esculin >> 4-MU-glucoside > DIMBOA-glucoside. No activity with pNP-glucoside, oNP-glucoside and sinigrin as substrates.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Beta-glucosidase 22
- PYK10-binding protein 2
- Jacalin-related lectin 20
- PYK10-binding protein 1
- TSA1-like protein
- Transcription factor NAI1
- Membrane protein of ER body 2
- MD-2-related lipid-recognition protein ROSY1
- Membrane protein of ER body 1
- Protein TEEBE
Sequence:
MALQKFPLMGLLLLLTILVSVTTAVDDPVCPATSKLSRASFPNGFLFGTATAAFQVEGAINETCRGPALWDIYCRRNPERCSGDHADVAVDFFHRYKEDIQLMKNLNTDAFRLSIAWSRIFPHGRKEKGVSQAGVQFYHELIDELLKNGIVPFVTVFHWDTPQDLEDEYGGFLSQNIVKDFREYADYVFTEYGGKVKNWITFNEPWVFAHAGYDLGKKAPGRCSRYVPGCEDREGQSGKEAYLVSHNLLNAHAEAVEVFRQKVKGGKIGIAHSPAWFEPHDLKDSNDAPTVSRVLDFMLGWHLEPTTSGDYPQIMKDLLGYRLPQFTAAQKAKLKDSTDFVGLNYYTSTFSNYNEKPDPSKPSWKQDSLVSWEPKNVDHSAIGSMPLTAALPVYAKGFRKLLKYIKDKYANPEIMIMENGYGDKLGTTDSVDVGTADHNRKYYLQRHLLAMNEAICIDKVRVTGYFVWSLLDNFEWQDGYKNRFGLYYVDFKNNLTRYEKESAKYYKDFLAQGVRPSALKRDEL
Protein: Regulatory protein YeiL (P0A9E9)
Organism: Escherichia coli (strain K12)
Function: Transcription regulator involved in mid-term, stationary-phase viability under nitrogen starvation. Might control expression of the salvage pathways or in some other way repress the recycling of nucleobases to nucleic acids and enhance their use as general nitrogen sources during nitrogen-limited growth.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11101674}.
Interaction partners:
- Sensor protein EvgS
Sequence:
MSESAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEECWCLALPMKHYRPLLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFILLSQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLALEMDPENKFSGMMQ
Protein: MIP18 family-like domain-containing protein (A0A0H2URY4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MRDDIKINDRALALQDQIIEKLEKVFDTDVELDVYNLGLIYEINLDETGLCKIVMTFTDTACDCAESLPIEIVAGLKQIEGIKDIKVEVTWSPAWKITRISRYGRIALGLPPR
Protein: Chitin synthase 3 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 3) (Class-IV chitin synthase 3) (P30573)
Organism: Candida albicans (Yeast)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSNFRDSSSPRRGYSEFDPESGEGLGRKKSLIRPERSRMDESHPRFHYTQVANQESNHIKVQPSSTGVDPRKSNELSTSRSHLSNYATPPHQEEEEDEGIPLMDIHNASPNVSSDQNNDLKGGREVYGLNDEINDYGSSPKKNQVISSSRPMNNEKPAKPKHDIYFWKVYCYAITFWAPAPLLKLFGLPTKDRQFAWREKIGLISCILYVGAFVAYLTFGFTKTVCSSQVVRTQINHVNGGYLIINGRAYDLTSSQHPKAAGIQAGSNVLYPPMNAGGKDASFLFQNVNGNCKGLIKPRDNCSIPYDGDELAWYMPCRLFNQDGSTKPNNTFAYYKGWACHTSETARDAYYKLKVNGDVYFTWDDVKNSSRNLVVYSGNVLDLDLINWIETDDVTYPELFDKLRDDETYRGLDISLVLTNSEERQAARCLTEIIKVGSIDTDTIGCIASKVVLYMSLVFILSVVVVKFIMACWFKWVTSRKQGATMYDSKAWAKRNREIEDWVDHDHGIGAEVKTVPVKARANYKAAKTNRQSVFHRAQKLSLGPNADLSQYYDNPNALSKTFKYTTMSTQAALLGRNGYGKRGNNANKSVSGGFNGRQSNLYLTDQGSSTDLLNRPVSSYNPFDSMGDDSIVINGLSPDIIHPDVVPQPPVEYQPFGYPLAHTINLVTCYSEDEEGIRITLDSIATTDYPNSHKLILVICDGIIKGSGNDETTPDIVLDMMSDLTVPRDEVEAYSYVAVAQGSKRHNMAKVYAGFYKYNDETVPPEKQQRIPMITIVKCGTPEEASAPKPGNRGKRDSQIILMSFLQKVVFDERMTSLEYEMLQSIWRITGLMAEFYEIVLMVDADTKVFPDSLTHMVAEMVKDPTIMGLCGETKISNKAQTWVTAIQVFEYYISHHQAKAFESIFGGVTCLPGCFCMYRIKAPKGSDGYWVPILANPDIVERYSDNVVDTLHRKNLLLLGEDRYLSSLMLRTFPTRKQVFVPKAACKTVVPDKFKVLLSQRRRWINSTVHNLFELVLVKDLCGTFCFSMQFVIFIELIGTLVLPAAITFTIYVIIVAIVSKPTPVMSLVLLAVIFGLPGCLIVITVSSLSYLVYFVIYLFALPIWNFVLPSYAYWKFDDFSWGETRTVAGGDKGDHSAVEGKFDSSKIAMKRWREWERERRSTENRKQQQQQQLTNNSSNNLAVPGAAWDPSNTGGNLIDDLSQGSSSGSS
Protein: Protein TANC2 (F1LTE0)
Organism: Rattus norvegicus (Rat)
Function: Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines.
Subcellular location: Cell projection, dendritic spine {ECO:0000269|PubMed:30021165}.
Interaction partners:
Sequence:
MFRNSLKMLLTGGKSSRKNRSSDGGSEEPPDRRQSSVDSRQSRSGPGGISTESDCAFEPDYAVPALPVSEGDVEQELGPPPSVDEAANTLMTRLGFLLGEKVTEVQPGDQYSMEVQDENQTSAITQRISPCSTLTSSTASPPASSPCSTLPPVSTNATAKDCSYGAVTSPTSTLESRDSGIIATLTNYSENMERTKYVGEAGKELGSGGNLKPWQSQKSSMDSCLYRVDENMAASTYSLNKIPERNLETVLSQSVQSIPLYLMPRPNSVAATSSAHLEDLAYLDEQRHTPLRTSLRMPRQSMSGARTQQDLRVRFAPYRPPDISLKPLLFEVPSITTESVFVGRDWVFHEIDAQLQSSNASVNQGVVIVGNIGFGKTAIISRLVALSCHGTRMRQIASDSPHASPKHVDANRELPLTQAPSAHSSIASGSCPGTPEMRRRQEEAMRRLASQVVAYHYCQADNAYTCLVPEFVHNVAALLCRSPQLTAYREQLLREPHLQSMLSLRSCVQDPMASFRRGVLEPLENLHKERKIPDEDFIILIDGLNEAEFHKPDYGDTIVSFLSKMIGNFPSWLKLIVTVRTSLQEITKLLPFHRIFLDRLEENEAIDQDLQAYILHRIHSSSEIQNNISLNGKMDNTTFGKLSSHLKTLSQGSYLYLKLTFDLIEKGYLVLKSSSYKVVPVSLSEVYLLQCNMKFPTQSSFDRVMPLLNVAVASLHPLTDEHIFQAINAGSIEGTLEWEDFQQRMENLSMFLIKRRDMTRMFVHPSFREWLIWREEGEKTKFLCDPRSGHTLLAFWFSRQEGKLNRQQTIELGHHILKAHIFKGLSKKVGVSSSILQGLWISYSTEGLSMALASLRNLYTPNIKVSRLLILGGANINYRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDASSESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIQCDWTMAGQQQGVFKKSQAIQQALIAAASMGYTEIVSYLLDLPEKDEEEVERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGAVPLFSTVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVDFLLAQGASIALMDKEGLTALSWACLKGHLSVVRSLVDNGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKIGPATWAMATSKPDIMIILLSKLMEEGDMFYKKGKVKEAAQRYQYALKKFPREGFGEDLKTFRELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLKEAIKLCPNNREIQRLLMRVEEECRQMQQQQQPPPPPQQPPEELPEEETEPEPQPEDIYSVQDIFEEEYLEQDVENVSIGLQTEARPSQGLPVIQSPPSSPAHRDSAYISSSPLGSHQVFDFRSNSSVGSPTRQGYQSTSPALSPTHQNSHYRPSPPHTSPAHQGASYRFSPPPVGGQGKEYPSPPPSPLRRGPQYRASPPAESMSIYRSQSGSPVRYQQEANVSQLPGRPKSPLSKMAQRPYQMPQLPVAVPQQGLRLQPAKAQIVRSNQPSSAVHSSTVIPTGAYGQVAHPMASKYQSSQGDMGVSQSRLVYQGSIGGIVGDGRPVQHVQASLSAGAICQHGGLTKEDLPQRPSSAYRGGMRYSQTPQIGRSQSASYYPVCHSKLDLERSSSQLGSPDVSHLIRRPISVNPNEIKPHPPTPRPLLHSQSVGLRFSPSSNSISSTANLTPTFRPSSSIQQMEIPLKPAYDRSCDELSPVSPTQGGYPSEPTRSRTTPFMGIIDKTARTQQYPHLHQQNRTWAVSSVDTVLSPTSPGNLSQPESFSPPSSISNIAFYNKTNNAQNGHLLEDDYYSPHGMLANGSRGDLLERVSQASSYPDVKVARTLPVAQAYQDNLYRQLSRDSRQGQTSPIKPKRPFVESNV