wanglab/gogpt-training-data huggingface dataset:
Protein: CUB_2 domain-containing protein (H2L0Q1)
Organism: Caenorhabditis elegans
Interaction partners:
- Putative serine protease K12H4.7
- CUB domain-containing protein
- CUB-like domain-containing protein
- ShKT domain-containing protein
Sequence:
MKIFTVFLTLSALFLVGSAQQLQPLSSFKGMSVHNEFSDFKVYPPYNIYVSAHSDATSALQQISVVTESGTKTLFELKQNLQASGEITGYPVLKPAYLTTTLSDNDLKRLNGVIYISSSKQYADNTFHVYGVSKSQNINLQALGKVDTTILFLNTNMGTNPYKSTIISQWKQDSTALAYLYAGFPQDTAEGKNTQIFSNPMHTDKADLYFANVEKFSLTLVAFYLKTYRGVNFRIEPGYSSIDSSTTTDVTTTGFYMKPLEKDDSTITVNIKRDTRFSGASGANVIGNLTTGGMVTVGFYEGASKYEDSAAPNPFCSPWSIPYILQNMKIWSTSSNPKNGQYFVQYFIAQGAIGSGTTSRPGQTTTRSSGTVQFFVSVASLMILWL
Protein: Iron-sulfur cluster assembly enzyme ISCU (NifU-like N-terminal domain-containing protein) (NifU-like protein) (Q9H1K1)
Organism: Homo sapiens (Human)
Function: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (Probable). Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form. May modulate NFS1 desulfurase activity in a zinc-dependent manner. Modulates the interaction between FXN and the cysteine desulfurase complex.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:11060020, ECO:0000269|PubMed:26702583}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus {ECO:0000269|PubMed:11060020}.
Interaction partners:
- Molybdenum cofactor sulfurase
- Cysteine desulfurase
- Frataxin, mitochondrial
- LYR motif-containing protein 4
- Selenocysteine lyase
- Stress-70 protein, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB
- Ferredoxin-2, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
Sequence:
MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGEAEKK
Protein: ADA histone acetyltransferase complex component 2 (Putative transcriptional regulator AHC2) (P25649)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein AHC1
- Mediator of RNA polymerase II transcription subunit 12
- SAGA complex subunit ADA2
- Histone acetyltransferase GCN5
- SAGA complex subunit SGF29
- SAGA complex subunit NGG1
- SAGA complex subunit SGF73
- SAGA complex subunit SPT8
- SAGA complex subunit SPT7
- SAGA complex/transcription factor TFIID complex subunit TAF6
Sequence:
MITPKGTHDAVAKFQKTDLHQDLDYIVLQQRRTQLETLINERESFVKNLCSLFHKIQNTKNYQEFVDVLAENRDLLREIFTVENGFQKQKWISNDDIPQIDWDKFALDINAYIAENDQLLALYEDGLL
Protein: Crooked neck protein, putative / cell cycle protein (F4JZX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pre-mRNA-processing-splicing factor 8A
- DExH-box ATP-dependent RNA helicase DExH12
- Tetratricopeptide repeat
- SNW/SKI-interacting protein
- AT3G18790 protein
- Cell division cycle 5-like protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Pre-mRNA-splicing factor SYF2
- Cwf15 / Cwc15 cell cycle control family protein
- ATPase E1
Sequence:
MASGGKDSDRTLGYMTRKDTEVKLPRPTRVKNKTPAPIQITAEQILREARERQEAEIRPPKQKITDSTELSDYRLRRRKEFEDQIRRARWNIQVWVKYAQWEESQKDYARARSVWERAIEGDYRNHTLWLKYAEFEMKNKFVNSARNVWDRAVTLLPRVDQLWYKYIHMEEILGNIAGARQIFERWMDWSPDQQGWLSFIKFELRYNEIERARTIYERFVLCHPKVSAYIRYAKFEMKGGEVARCRSVYERATEKLADDEEAEILFVAFAEFEERCKEVERARFIYKFALDHIPKGRAEDLYRKFVAFEKQYGDKEGIEDAIVGKRRFQYEDEVRKSPSNYDSWFDYVRLEESVGNKDRIREIYERAIANVPPAEEKRYWQRYIYLWINYALFEEIETEDIERTRDVYRECLKLIPHSKFSFAKIWLLAAQFEIRQLNLTGARQILGNAIGKAPKDKIFKKYIEIELQLGNMDRCRKLYERYLEWSPENCYAWSKYAELERSLVETERARAIFELAISQPALDMPELLWKAYIDFEISEGELERTRALYERLLDRTKHYKVWVSFAKFEASAAELEEDENEDEDQEEDVIEHKKDCIKRARAIFDRANTYYKDSTPELKEERATLLEDWLNMESSFGNLGDVSIVQSKLPKKLKKRKAITREDGSTEYEEYIDYLYPEESQTTNLKILEAAYKWKKQKVAASEDD
Protein: Uncharacterized protein YjjA (Protein P-18) (P18390)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Replicative helicase loader DnaC
- Probable succinate transporter subunit YjjB
- Replication restart protein DnaT
Sequence:
MMKTVKHLLCCAIAASALISTGVHAASWKDALSSAASELGNQNSTTQEGGWSLASLTNLLSSGNQALSADNMNNAAGILQYCAKQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTPLAEKVKTKACDLVLKQGLNFIS
Protein: Homocitrate synthase, mitochondrial (HCS) (EC 2.3.3.14) (Q9Y823)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- 3-isopropylmalate dehydratase
- Probable acetyl-coenzyme A synthetase
- Acetyl-CoA acetyltransferase
- Dihydroxy-acid dehydratase, mitochondrial
- Acetyl-CoA hydrolase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Acetyl-CoA carboxylase
- 2-isopropylmalate synthase
- Homoisocitrate dehydrogenase
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MSVSEANGTETIKPPMNGNPYGPNPSDFLSRVNNFSIIESTLREGEQFANAFFDTEKKIQIAKALDNFGVDYIELTSPVASEQSRQDCEAICKLGLKCKILTHIRCHMDDARVAVETGVDGVDVVIGTSQYLRKYSHGKDMTYIIDSATEVINFVKSKGIEVRFSSEDSFRSDLVDLLSLYKAVDKIGVNRVGIADTVGCATPRQVYDLIRTLRGVVSCDIECHFHNDTGMAIANAYCALEAGATHIDTSILGIGERNGITPLGALLARMYVTDREYITHKYKLNQLRELENLVADAVEVQIPFNNYITGMCAFTHKAGIHAKAILANPSTYEILKPEDFGMSRYVHVGSRLTGWNAIKSRAEQLNLHLTDAQAKELTVRIKKLADVRTLAMDDVDRVLREYHADLSDADRITKEASA
Protein: SIRP-beta B-type (Q6F5F0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLLLDAWTHIPHCVLLLILLLGLKGAAMRELKVIQPVKSFFVGAGGSATLNCTVTSLLPVGPMRWYRGIGQSRLLIYSFTGEGFPRITNTSDTTKRNNMDFSIRISNVTPADSGTYYCVKFQRGPSDFYTEIQSGGGTELSVLAKPSSPMVSGPAARAVPQQTVTFTCRSHGFFPRNLTLKWFKNGDEISHLETSVEPEETSVSYRVSSTVQVVLEPRDVRSQIICEVDHVTLDRAPLRGIAHISEFIQVPPTLEIRQQPTMVWNVINVTCQIQKFYPPSFQLTWLENGNISRREVPFTLTVNKDGTYNWISCLLVNISALEENMVVTCQVEHDGQAEVIETHTVVVTEHQRVKELKTAGIAKIPVAVLLGSKILLLIVATVIYMRKKQNA
Protein: BcDNA.LD24702 (Spindle defective 2 (EC 3.6.1.13)) (Q9VV79)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Centrosomin
- Serine/threonine-protein kinase PLK4
- Asterless
- Spindle assembly abnormal 4
- Pericentrin-like protein, isoform F
- Spindle assembly abnormal protein 6 homolog
- Aurora kinase
- Anastral spindle 2, isoform A
- Centrosomal protein 135kDa, isoform B
- Centriolar coiled coil protein 110kDa, isoform B
Sequence:
MDSSSGSQGNGSFMDQNSLGILNMDNLKVFGDLSSFSKSGRRSGTGRDSPAVHERLREERLRALETLEKPRPSRSSQAKSTALQMRLSTNISELVTDDTIDLNSSSSFALVTPATKGTNISFEPAEITGRSTLCQAGKQRRREKPSLSVAEILKSSFVEKARLLERKLQDASQAEASYHLSRGSSSSLSDSFNCSRSLPRTADMSELSLNGGGGFSFGSASLAAEGQDESFAPAELMQSKLVLGEISWAQEFTAMPTATLSTQALKKIAAPTSEIETSVSNSVLAGDPDFSLGNYFQTRSENIWNIVSNSSPNRSRTNQPLLEPESNVTLDSVGEKTPQPDNKTYTKTDAITGSNLGRNLMRKMQQDRIETALKSRNGLAAKETKRPPSSSEILSLSAIDKALRDIDLNSDTSTVEVVNHLWEHGRGNNYDDGENKENQSSNSHAERTSCGSNKLTDTMSFTDSVLNSTDFRHLQQSISRKPLSPLADHPQITISRADTDPVETEAEADIDEWPSTPVKEPSRRVRRTKISPRAASPSSSDGVRPLTCTEDENDEEDEDKTPVNKKRVSIATMGLIPRKASSLSSTRLDGCDVAVASSTERDFGISPNLAKNLSPLSSPRSCLSSPLLDSTTSSDRRQLMSGAARKANSSPAGSEASSTSGFTASGRRGLGTSSVAVPRSISRCSNSSEFSHRDGKLLPLKVTHTTLCWGSTKLRTDVRKSMQVKNTADKRLVIRLGIQGPGFQLVGTDSSTITLQAMECRSVVINFCPTVCGAAIGALSFYAPPGAHNSNQPGLEIPLYGYGGSASITINGLLKGPVGASFLTIGDVCELSAGPLSANLKFHNKGPLTAFVGISVDSTVLMKLRLSEAFEVRPSRLILPPNSERCVQILFRPNREDLKNILKKTAQVLTLANMRIFCGDEPNRQRMRSLVQRMSSRQREKLTSPMLDSIWGEFPDEQPVRNIGQLNEPPEFILDLVTVVRIIDVALTLNRDFDESSESSLMFLPEADETVLFRTICVANSPTPTQSHLLEPVDELLEADTTTLTPVEQNWCVQPGLLEFGVGCSPLATLSVTNSFCSRQLIEVTCNVPDLVRISPSECYVSPDGGHAEIDVRLLRSPRQDLLEREPLIVVSMENERISVPISFKF
Protein: X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (G3V817)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
Interaction partners:
- DNA-dependent protein kinase catalytic subunit
- X-ray repair cross-complementing protein 6
- Non-homologous end-joining factor 1
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA ligase
- Serine-protein kinase ATM
- Protein artemis
- Aprataxin and PNK-like factor
- Double-strand break repair protein MRE11
- DNA repair protein XRCC1
Sequence:
MAWSGNKAAVVLCMDVGVAMGNSFPGEESPLEQAKKVMTMFVQRQVFSESKDEIALVLYGTESTDNALAGKDQYQNITVHRHLMLPDFDLLEDIGNKIQPSSQQADFLDALIVCMDLIQRETIGKKFGKKHIEVFTDLSSPFSQDQLDIIICNLKKSSISLQFFLPFPIDKNGEPGETEDHDSSFDHCAPSFPQKGLTEQQKEGIHMVTRVMLSLEGKDGLDEIYSFSESLQQLCIFKKIERRSLPWPCQLTIGPNLSIRIVAYKSIVQEKFKKSWVVVDARTLKKEDIQKETVYCLNDDDETEVSKEDTIQGFRYGSDIIPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVHRRFFMGHQVLKVFAAKDDEAAAVALSSLVHALDELNMVAIVRYAYDKRANPQVGVAFPFIKDAYECLVYVQLPFMEDLRQYMFSSLKNNKKCTPTEAQLSAIDDLIDSMSLVKKNEEEDIIEDLFPTSKIPNPEFQRLYQCLLHRALHLQERLPPIQQHILNMLDPPTEMKAKCEIPLSKVKTLFPLTEVVKKKDQVTAQDVFQDNIEEGPAAKKYKTEKEEGHISISSLAEGNVTKVGSVNPVENFRVLVRQKIASFEEASLQLMSHIEQFLDTNETLYFMKSMDCIKALREEAIQFSEEQRFNSFLEGLREKVEIKQLNHFWEIVVQDGITLITKDESPGSSVTAEEATKFLTPKDKAKEDTTGLEEGGDVDDLLDMI
Protein: Kallikrein-2 (EC 3.4.21.35) (Glandular kallikrein-1) (hGK-1) (Tissue kallikrein-2) (P20151)
Organism: Homo sapiens (Human)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Interaction partners:
- Kallistatin
- Prostate-specific antigen
- Prostatic acid phosphatase
- Androgen receptor
- Kininogen-1
- Kallikrein-1
- Beta-microseminoprotein
- Plasma serine protease inhibitor
- Protein-glutamine gamma-glutamyltransferase 4
- Alpha-1-antichymotrypsin
Sequence:
MWDLVLSIALSVGCTGAVPLIQSRIVGGWECEKHSQPWQVAVYSHGWAHCGGVLVHPQWVLTAAHCLKKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLYNMSLLKHQSLRPDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEPALGTTCYASGWGSIEPEEFLRPRSLQCVSLHLLSNDMCARAYSEKVTEFMLCAGLWTGGKDTCGGDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRKWIKDTIAANP
Protein: Leukotriene C4 synthase (LTC4 synthase) (EC 4.4.1.20) (Glutathione S-transferase LTC4) (EC 2.5.1.-) (Leukotriene-C(4) synthase) (Leukotriene-C4 synthase) (Q16873)
Organism: Homo sapiens (Human)
Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions.
Subcellular location: Nucleus outer membrane {ECO:0000269|PubMed:12023288}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12023288, ECO:0000269|PubMed:19233132}; Multi-pass membrane protein. Nucleus membrane {ECO:0000269|PubMed:19233132}; Multi-pass membrane protein.
Interaction partners:
- Leukotriene A-4 hydrolase
- Polyunsaturated fatty acid 5-lipoxygenase
- Cysteinyl leukotriene receptor 1
- Microsomal glutathione S-transferase 1
- Cysteinyl leukotriene receptor 2
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 1 proenzyme
- Glutathione S-transferase 3, mitochondrial
- Leukotriene B4 receptor 2
- Prostaglandin E synthase
Sequence:
MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA
Protein: RAB GTPase homolog G3A (F4JKR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046278}; Lipid-anchor {ECO:0000256|ARBA:ARBA00046278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00046278}.
Interaction partners:
Sequence:
MATRRRTLLKVIVLGDSGVGKTSLMNQYVHKKFSMQYKATIGADFVTKELQIGEKLVTLQIWDTAGQERFQSLGAAFYRGADCCALVYDVNVLRSFDNLETWHEEFLKQAWNIGMWTIAEASPSDPKTFPFIVLGNKIDVDGGSSRVVSDKKAADWCASNGNIPYFETSAKDDFNVDEAFLTIAKTALANEHEQDIYFQGIPDAVTENEPKGGGCAC
Protein: Meep (EC 3.1.-.-) (RE72485p) (Q8SXQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNGSHLQTEQLLFEERPLHVPPLSELKRVIQGALDENFRTVDVSVEACPDLRDSQFGLVERGLGGKATLLEAGGPPYLRPLVQRDKLYNLKEITRRTQGAGKIFAVGPGAGPWPIRHSNCEGIFNFSLNEEDELTQGSYTATVRGANEDCVLERIPETESRAALILNLFLSEGKPGQVLRISAKQRTGGENFVECIRKGLERHYGDQVVGLGGMFVVRRGCVHQHVMRDFSKTPIHTQEQIQNWLKFYEMPAQLNAVGTLVTKDMGLDLRLQHFHSFSFANWGGHYHYDTTPDIVEYEAYLNVAERVIRVDRPVATDQLGRD
Protein: MIP05841p (Tyrosine decarboxylase 2 (EC 4.1.1.-, EC 4.1.1.25)) (A1Z6N4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyramine beta-hydroxylase
- Tyrosine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- monoamine oxidase
- Tyrosine aminotransferase
- Aromatic-L-amino-acid decarboxylase
- Phenoloxidase 3
- tyrosinase
Sequence:
MDSTEFRKRGMEMVEYICNYLETLNERRVTPSVEPGYLRHLLPPEAPQEPEDWDQIMRDVEDKIMPGVTHWQHPRFHAYFPAGNSFPSILGDMLGDGIGCIGFSWAASPACTELETIVLDWLGKAIGLPDHFLALKEGSTGGGVIQTSASECVLVTMLAARAQALKRLKAQHPFVEEGHLLSKLMAYCSKEAHSCVEKAAMICFVKLRILEPDDDASLRGQTIYEAMEEDELQGLVPFFVSTTLGTTGSCAFDNLPEIGKQLQRFPGVWLHVDAAYAGNSFICPELKPLLKGIEYADSFNTNPNKWLLTNFDCSTLWVRDRIRLTSALVVDPLYLKHGYSDAAIDYRHWGVPLSRRFRSLKLWFVLRSYGISGLQHYIRHHIKLAKRFEELVLKDKRFEICNQVKLGLVCFRLKGSDKLNEKLLSIINESGKLHMVPASVGDRYIIRFCAVAQNATAEDIDYAWDIIVDFANELLEKEQHDELSEIMNRKKQDTLAQKRSFFVRMVSDPKIYNPAINKAGTPKLSMELPSPVVSRGSAPIIRTQSSVDHNSWISWPLAFLFNSNNEEKGSNVSLRFRHLDTNVRPSSSRRNSGAGSSPSPENELDYVNVQQQQMEQRSPRRSPMAVRKASSTRDNLN
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 (Complex I-B17) (CI-B17) (NADH-ubiquinone oxidoreductase B17 subunit) (Q02367)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 subunit C2
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
Sequence:
MSGYTPEEKLRLQQLRELRRRWLKDQELSPREPVLPPQRVSPVERFWNKFLQDGALWKNVIYKTYRHSIFAFTHVLIPVWIIHYYLKYHVTTKPYTIVEKKPRIFPGDTILETGEVIPPMKEFPDQHH
Protein: Mud protein (Q9NCL3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDTRSWRKVLFQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETETVKGKNELQDQPTEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQPSSSTPQLRNHREQLRLNGCDMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQTEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLIEKEKQIKDVGAEIQELRKRNINLENMLSQIADKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLRQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELEKERKELAQVKSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAKVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDIIETLEMRCTQMEEERATAYEQINKLENRCQEKDNVKSSQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAENVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMKGSRRRRWPQLMLLFIGLIILIVFFLYYILYINGINVIFKSRSPIVY
Protein: SRC kinase signaling inhibitor 1 (SNAP-25-interacting protein) (SNIP) (p130Cas-associated protein) (p140Cap) (Q9QWI6)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of SRC by activating CSK which inhibits SRC activity and downstream signaling, leading to impaired cell spreading and migration. Regulates dendritic spine morphology. Involved in calcium-dependent exocytosis. May play a role in neurotransmitter release or synapse maintenance (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QXY2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXY2}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXY2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXY2}. Presynapse {ECO:0000250|UniProtKB:Q9QXY2}. Postsynapse {ECO:0000250|UniProtKB:Q9QXY2}. Postsynaptic density {ECO:0000250|UniProtKB:Q9QXY2}. Note=Localized to the perinuclear region, lamellopodia, cortical actin and actin stress fibers but not to focal adhesions. Strongly expressed in axons and dendrites of the CA1 and CA3 hippocampal regions and of the dentate gyrus. Detected in both presynapses and postsynapses and enriched in postsynaptic density fractions. {ECO:0000250|UniProtKB:Q9QXY2}.
Interaction partners:
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
- Microtubule-associated protein RP/EB family member 3
- Disks large homolog 4
- Proto-oncogene tyrosine-protein kinase Src
- Neurabin-2
- Citron Rho-interacting kinase
- Synaptosomal-associated protein 25
Sequence:
MQPWQCLRRFALAWWERTAEGRARSPREEVGPRDPGGRGEPDPERSSPPMLSADDAEYPREYRTLGGGGGGGSGGRRFSNVGLVHTSERRHTVIAAQSLEALSGLQKADADRKRDAFMDHLKSKYPQHALALRGQQDRMREQVGGWTVDPVCLLSSLCSHLHGDSTPSGAGQPAQQPNYWSFKTRSSRHTQGAQPGLADQAAKLSYASAESLETMSEAELPLGFSRMNRFRQSLPLSRSASQTKLRSPGVLFLQFGEETRRVHITHEVSSLDTLHALIAHMFPQKLTMGMLKSPNTAILIKDEARNVFYELEDVRDIQDRSIIKIYRKEPLYAAFPGSHLTNGDLRREMVYASRESSPTRRLNNLSPASHLASSSPPPGLPSGLPSGLPSGSPSRSRLSYAGGRPPSYAGSPVHHAAERLGGAPTGQGVSPSPSAILERRDVKPDEDLAGKAGGMVLVKGEGLYADPYGLLHEGRLSLAAAAETHSHTRARAACTSGVPCALSAPTPLPRCSPTWRTRCTRRALAALYGDGYGFRLPPSSPQKLADVSAPSGGPPPPHSPYSGPPSRGSPVRQSFRKDSGSSSVFAESPGGKARSTGSASTAGAPPSELFPGPGERSLVGFGPPVPAKDTETRERMEAMEKQIASLTGLVQSALLRGSEPETPSEKVEGSNGAATPSAPVCGSGSKSSGATPVSGPPPPSASSTPAGQPTAVSRLQMQLHLRGLQNSASDLRGQLQQLRNVQLQNQESVRALLKPTEADVSMRVSEAARRQEDPLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVAHNHRLMPGPELEEKALVLKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGMWPPPNNLLNQSPKKVAAETDFSKGLDFEIPPPSPPLNLHELSGPAEGTPLTPKSTNPTKCLDASSKRNTDKAVSVEAAERDWEEKRAALTQYSAKDINRLLEETQAELLKAIPDLDCASKTHPGPAPTPDHKPPKAPHGQKAAPRTEPSGRRGSDELTVPRYRTEKPSKSPPPPPPRRSFPSSHGLTTTRTGEVVVTSKKDSVFIKKAESEELEVQKPQVKLRRAVSEVVRPASTPPIMASAIKDEDDEERIIAELESGGSSVPPMKVVTPGASRLKAAQGPAGSPDKGKHGKQRTEYMRIQAQQQATKPSKEVSGPNETSSPGSEKPSGSRTSIPVLTSFGARNSSISF
Protein: Rap1 GTPase-GDP dissociation stimulator 1 (Exchange factor smgGDS) (SMG GDS protein) (SMG P21 stimulatory GDP/GTP exchange protein) (P52306)
Organism: Homo sapiens (Human)
Function: Acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP. Additionally, appears to chaperone the processing and/or trafficking of small GTPases containing a C-terminal polybasic region independently of GEF activity. Targets include RAP1A/RAP1B, RHOA, RHOB, RHOC, RAC1 and KRAS. Regulates mitochondrial dynamics by controlling RHOT function to promote mitochondrial fission during high calcium conditions. Able to promote the Ca(2+) release from the endoplasmic reticulum via both inositol trisphosphate (Ins3P) and ryanodine sensitive receptors leading to a enhanced mitochondrial Ca(2+) uptake.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24349085}. Endoplasmic reticulum {ECO:0000269|PubMed:24349085}. Mitochondrion {ECO:0000269|PubMed:24349085}. Nucleus {ECO:0000269|PubMed:12551911}. Note=Nuclear import is dependent on complexing with a GTPase containing a C-terminal polybasic region. {ECO:0000269|PubMed:12551911}.
Interaction partners:
- Transforming protein RhoA
- Ras-related C3 botulinum toxin substrate 1
- Mitochondrial Rho GTPase 1
- GTPase KRas
- Rho-related GTP-binding protein RhoC
- Mitochondrial Rho GTPase 2
- GTP-binding protein Di-Ras1
- Ras-related protein Rap-1A
- Nuclear pore complex protein Nup98-Nup96
- GTPase HRas
Sequence:
MDNLSDTLKKLKITAVDKTEDSLEGCLDCLLQALAQNNTETSEKIQASGILQLFASLLTPQSSCKAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCSITDPANEKLLTVFCGMLMNYSNENDSLQAQLINMGVIPTLVKLLGIHCQNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSDKEDDITELKTGSDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDANCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVINKAKMLSAGVTEAVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNVKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGTAEKDLESAKLVQILHRLLADERSAPEIKYNSMVLICALMGSECLHKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVES
Protein: Protein Ami (EC 3.2.1.-) (Autolysin) (O33983)
Organism: Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
Function: A bacteriolysin able to lyse both L.monocytogenes and S.aureus.
Subcellular location: Cell surface {ECO:0000269|PubMed:9282740}. Cell membrane {ECO:0000305|PubMed:10594817}. Note=Anchored by its GW repeats to the cell surface. {ECO:0000305|PubMed:9282740}.
Interaction partners:
Sequence:
MKKLVKSAVVFAGLVFIGTSATMITEKASAASTDPVQKVDGQATYIPKGVRDGTATEEHDGFEDGTNSVLQQVPLLRATTGYPDVNAYIKSNKFSTAKIEKQLKSQFPKFNYRNGYGKPEGIVIHETANNSSTITGEINYMSTNYNNAFVHAFVDKSRIIQIHPTENGVWGAGQYANARFIQVELVRSKTFDEFARSINNYAYYAAYLLDQYNLPVDSAHSDGKGTVWSHDAVTRYLGGTTHTDPVAYFNQWGYNFNNFVSLINEKYKAMQVNYEKIEYDKAITAYSRVKTATGNSVWTKPNKTEGAKLVNPLSSYSGKNLRIIREAKTSGGTIWYQFSVGGKTIGWVDSKALNTFYTPSMEKTITGTRYVLPSKQTVHYYGLPVEDSAIDRGPLSKFNGQALTLQREATIEGQLWYRVKDLGWVKAVNLTTTKYDLIEYDKAITAYSRVKTAAGNYVWSKPNKTEGAKQGSALSTYSGKNMRIIREAKTSSGTIWYQFSIDGKTIGWVDTKALNTFYTPSMEKNLTATRYVAPGQETQHYYGLPVADSAIDRGPLSKFAGQTLTVQREATIEGQLWYRVKDLGWTKASTLTATQYDKLEYDKAITAYSRVKTATGNSVWTKPYRTSGYKLVNPLSSYAGKNLRIIREAKTSSGIWYQFSVGGKTIGWVDSKALNTFYTPSMEKTITGTRYVLPSKQTVHYYGLPVEDSAIDRGPLSKFNGQALTLQREATIEGQLWYRVKDLGWVKAANLTTTKYDTLSYDKAITAYSRVKTATGNSVWTKPNKIEGAQKISALSTYSGKNMRILREAKTSSGTIWYQFSVGGKTIGWVETKALNTFYTPSMEKNLTATRYVLTSKKNEHYYGLPVVDSAIDRGPLSKFSGKTLTVQREATIEGQLWYRVKDLGWTKAANLSAKKQ