wanglab/gogpt-training-data huggingface dataset:
Protein: Annexin A10 (Annexin-10) (Annexin-14) (Q9UJ72)
Organism: Homo sapiens (Human)
Interaction partners:
- Enhancer of mRNA-decapping protein 3
Sequence:
MFCGDYVQGTIFPAPNFNPIMDAQMLGGALQGFDCDKDMLINILTQRCNAQRMMIAEAYQSMYGRDLIGDMREQLSDHFKDVMAGLMYPPPLYDAHELWHAMKGVGTDENCLIEILASRTNGEIFQMREAYCLQYSNNLQEDIYSETSGHFRDTLMNLVQGTREEGYTDPAMAAQDAMVLWEACQQKTGEHKTMLQMILCNKSYQQLRLVFQEFQNISGQDMVDAINECYDGYFQELLVAIVLCVRDKPAYFAYRLYSAIHDFGFHNKTVIRILIARSEIDLLTIRKRYKERYGKSLFHDIRNFASGHYKKALLAICAGDAEDY
Protein: Glycine-rich protein (F4JV81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Dual specificity phosphatase Cdc25
Sequence:
MISISIPMVRFCLCFAFVILVSANPKLINSWDETAIRFEPLSPSPAPEPSPDDDDSSVSCVDDLGGVGSLDSTCKLVADLNLTRDLNITGKGNLHVLPGVRLVCQFPGCSISVNISGNFSLAENSSVIAGTFRLAAENAEFGLSSAVDTTGLAGEPPPDTSGTPEGVEGAGGGYGGRGACCLSDTTTKIPEDVFGGDVYGWSSLEKPEIYGSRGGSTSNEVDYGGGGGGTVAIEILGYISLNGSVLADGASGGVKGGGGSGGSIFVMAHKMAGNGRLSASGGDGYAGGGGGRVSVDIYSRHSDPKIFFNGGRSFGCPENAGAAGTLYDVISESLTIDNHNKTTYTDTLLLEFPNHRLFTNLYIRNMAKVAVPLRWSRVQVQGLISLSNGGELNFGLPRYASSEFELFAEELLMSNSAIKVYGALRMTVKVFLMLKSRMFIDGGGVTILGTSMLEISNLLVLKESSVIQSNGNLGVHGQGLLNLTGTGDTIEAQRLILSLFYSIQVGAGAVLRGPLQNASTGGLTPKLYCQRQDCPVELLHPPEDCNVNSSLPFTLQICRVEDITVEGLIKGSVIQFHLARTVLVRSSGTISADGMGCKGGVGTGRFLRSGIGSGGGHGGKGGSGCYNHTCIEGGESYGNADLPCELGSGSGNEESTDSVAGGGIIVLGSLEHPLSSLSLEGSITTDGESPRKTLKGLSNSSLGPGGGSGGTVLLFLRTLEIGRSAILSSIGGNGSLKGGGGGSGGRIHFHWSDIPTGDVYHPVAIVKGRVYVRGGMGIIEDNIGGNGTLTGKACPEGLYGLFCEECPSGTYKNVTGSDKALCHLCPANDIPHRAVYVTVRGGVAETPCPYKCISDRYHMPHCYTTLEELIYTFGGPWLFGVLLVVVLLLLALVFSVARMKFVSGDELHGSAPTQHGSQIDHSFPFLESLNEVMETSRVEESQGHMHRIYFLGPNTFSEPWHLSHTPPEEIKEIVYEAAFNGFVDEVNVIAAYQWWEGAIYIMLSVLVYPLAWSWQQSRRRLKFQKLRDFVRSEYDHSCLRSCRSRALYEGLKVAATPDLMLAHLDFFLGGDEKRSDLPPQVHQRLPMPLIFGGDGSYMAYYSLQSDDILTSLLSQLVPPTTWYRFVAGLNAQLRLVQQGKLRSTFRSVMRWIETHGNPALKRHGVRVDLARFQALSSSSCQYGILVHTIADEVASTRSDDETEQQHPWGTQIENHSGDFRENFQPLRSEINHVRHQECGEIIDIGSLQFLKEEKDVLSLISFLIHNTKPVGHQDLVGLVISVLLLGDLTLTLLTLLQLYSISLLEVFLAMFILPLSIIFPFPAGVSALFSHGPRRSASRTRVYALWNVTSLVNVVVAFVCGYVHYHGSSSGKKIPYLQPWNISMDENEWWIFPVALFLCKVLQSQLVNWHVANLEIQDYSLYSDDSELFWQS
Protein: GUK-holder, isoform B (RE59757p) (Q9VE16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPFVQRVVQPVNVAQATAASLGHASGRFHCTPGKCRNNNCINKQSPDVEVPNGHGSPTSLTRVLVHQAPEDQPVPPAPAPMKKLKHHVEFLSTSPTRHQSQSLPNSRHPSQQRPALGRIASAPQSPTAGSSKVVSGHEFDSISNITLSNALRQLASLVLIASDIFDDLQRDLQAVGERAGRVQRKIAAVERRVCAYDPKTVTVPESDLLTFAQRKHHFETDKSFQQELFTGETRPLSVRQLYTEAGKELPVATGATATALASLAHSQSLIPSRSISFNGEVLSSDHEVLQLNGSTDTEDHLLCVSDFGNANRKLRTRIDAEIEIRLPAAIEDLRKWTSSEALGDVTVTPDCMHHVDTSVSTSLAIGENGILTPALSPSVLSADAVDALYAQNLSQAADSSRHNHHTQALIPNDINKDVPLNHRLPSPEEQTKQIALKYPAEVISVNTSGKHFQRMCAARKSTSGGYAGGATAGSSSSTSPENAGQTEGNNLDDNVQTVSRRSRSRKVRGKRRNTIAGIDQKEIQDAANGVSTFL
Protein: Zinc finger CCHC domain-containing protein 8 (TRAMP-like complex RNA-binding factor ZCCHC8) (Q6NZY4)
Organism: Homo sapiens (Human)
Function: Scaffolding subunit of the trimeric nuclear exosome targeting (NEXT) complex that is involved in the surveillance and turnover of aberrant transcripts and non-coding RNAs. NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. May be involved in pre-mRNA splicing (Probable). It is required for 3'-end maturation of telomerase RNA component (TERC), TERC 3'-end targeting to the nuclear RNA exosome, and for telomerase function.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:16263084, ECO:0000269|PubMed:21855801}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Note=Excluded from nucleolus. {ECO:0000269|PubMed:21855801}.
Interaction partners:
- Exosome RNA helicase MTR4
- RNA-binding protein 7
- Terminal nucleotidyltransferase 4B
- Exosome complex component RRP40
- Exosome complex component RRP43
- Exosome complex component RRP42
- Nuclear cap-binding protein subunit 2
- Zinc finger CCHC domain-containing protein 7
- Exosome complex component CSL4
- Exosome complex component RRP46
Sequence:
MAAEVYFGDLELFEPFDHPEESIPKPVHTRFKDDDGDEEDENGVGDAELRERLRQCEETIEQLRAENQELKRKLNILTRPSGILVNDTKLDGPILQILFMNNAISKQYHQEIEEFVSNLVKRFEEQQKNDVEKTSFNLLPQPSSIVLEEDHKVEESCAIKNNKEAFSVVGSVLYFTNFCLDKLGQPLLNENPQLSEGWEIPKYHQVFSHIVSLEGQEIQVKAKRPKPHCFNCGSEEHQMKDCPMPRNAARISEKRKEYMDACGEANNQNFQQRYHAEEVEERFGRFKPGVISEELQDALGVTDKSLPPFIYRMRQLGYPPGWLKEAELENSGLALYDGKDGTDGETEVGEIQQNKSVTYDLSKLVNYPGFNISTPRGIPDEWRIFGSIPMQACQQKDVFANYLTSNFQAPGVKSGNKRSSSHSSPGSPKKQKNESNSAGSPADMELDSDMEVPHGSQSSESFQFQPPLPPDTPPLPRGTPPPVFTPPLPKGTPPLTPSDSPQTRTASGAVDEDALTLEELEEQQRRIWAALEQAESVNSDSDVPVDTPLTGNSVASSPCPNELDLPVPEGKTSEKQTLDEPEVPEIFTKKSEAGHASSPDSEVTSLCQKEKAELAPVNTEGALLDNGSVVPNCDISNGGSQKLFPADTSPSTATKIHSPIPDMSKFATGITPFEFENMAESTGMYLRIRSLLKNSPRNQQKNKKASE
Protein: Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) (P55834)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Interaction partners:
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL11
- Bifunctional DNA-directed RNA polymerase subunit beta-beta'
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS7
- Elongation factor G
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein bL33
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL5
Sequence:
MAISKEEVLEYIGSLSVLELSELVKMFEKKFGVSATPTVVAGAAVAGGAAAESEEKTEFNVILADSGAEKIKVIKVVREITGLGLKEAKDATEKTPHVLKEGVNKEEAETIKKKLEEVGAKVEVK
Protein: Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase) (Fatty acid hydroxylase domain-containing protein 1) (Q7L5A8)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydroxylation of free fatty acids at the C-2 position to produce 2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis. FA2H is stereospecific for the production of (R)-2-hydroxy fatty acids. Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath (By similarity). Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier. Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis (By similarity). Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5MPP0}; Multi-pass membrane protein {ECO:0000269|PubMed:15337768}. Microsome membrane {ECO:0000269|PubMed:15337768}; Multi-pass membrane protein {ECO:0000269|PubMed:15337768}.
Interaction partners:
- Alkylglycerol monooxygenase
- Protein C19orf12
- Fatty acid hydroxylase domain-containing protein 2
- Aldehyde dehydrogenase family 3 member A2
- Methylsterol monooxygenase 1
- Pantothenate kinase 2, mitochondrial
- DDB1- and CUL4-associated factor 17
- Bifunctional coenzyme A synthase
- Cholesterol 25-hydroxylase
Sequence:
MAPAPPPAASFSPSEVQRRLAAGACWVRRGARLYDLSSFVRHHPGGEQLLRARAGQDISADLDGPPHRHSANARRWLEQYYVGELRGEQQGSMENEPVALEETQKTDPAMEPRFKVVDWDKDLVDWRKPLLWQVGHLGEKYDEWVHQPVTRPIRLFHSDLIEGLSKTVWYSVPIIWVPLVLYLSWSYYRTFAQGNVRLFTSFTTEYTVAVPKSMFPGLFMLGTFLWSLIEYLIHRFLFHMKPPSDSYYLIMLHFVMHGQHHKAPFDGSRLVFPPVPASLVIGVFYLCMQLILPEAVGGTVFAGGLLGYVLYDMTHYYLHFGSPHKGSYLYSLKAHHVKHHFAHQKSGFGISTKLWDYCFHTLTPEKPHLKTQ
Protein: Neuronatin (Q61979)
Organism: Mus musculus (Mouse)
Function: May participate in the maintenance of segment identity in the hindbrain and pituitary development, and maturation or maintenance of the overall structure of the nervous system.
Interaction partners:
- Apoptosis inducing factor BLCAP
- Nucleosome assembly protein 1-like 5
- Retrotransposon-derived protein PEG10
- Epsilon-sarcoglycan
- Mesoderm-specific transcript protein
- Pleiomorphic adenoma gene-like 1
Sequence:
MAAVAAASAELLIIGWYIFRVLLQVFLECCIYWVGFAFRNPPGTQPIARSEVFRYSLQKLAHTVSRTGRQVLGERRQRAPN
Protein: Palustrin-1a (P84274)
Organism: Lithobates palustris (Pickerel frog) (Rana palustris)
Function: Antimicrobial activity against Gram-negative bacterium E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:11087945}.
Interaction partners:
Sequence:
ALFSILRGLKKLGKMGQAFVNCEIYKKC
Protein: N-acetylmuramate/N-acetylglucosamine kinase (MurNAc/GlcNAc kinase) (EC 2.7.1.221) (Anomeric sugar kinase) (Q88QT3)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Sugar kinase that catalyzes the ATP-dependent phosphorylation of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1 hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P, respectively. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Is also able to use N-acetylgalactosamine (GalNAc) as a substrate, but not N-acetylmannosamine, N-deacetylated sugars or glucose.
Interaction partners:
- N-acetylmuramate alpha-1-phosphate uridylyltransferase
- Beta-hexosaminidase
- N-acetylmuramic acid 6-phosphate phosphatase
- Bifunctional protein GlmU
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
- Muropeptide permease AmpG
- Anhydro-N-acetylmuramic acid kinase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Acetylglutamate kinase
Sequence:
MPEHDVRLQQLTVWLDEQLNDLFRDNAWGEVPAGSLTAASSDASFRRYFRWQGAGHSFVIMDAPPPQENCRPFVAIDHLLASADVHVPLIHAQDLERGFLLLGDLGTQTYLDIINADNADGLFADAIDALLKFQRLPMDAPLPSYDDALLRREVELFPEWYVGRELGLTFTDAQKATWQRVSQLLIDSALAQPKVLVHRDYMPRNLMQSTPNPGVLDFQDAVYGPVTYDITCLFKDAFVSWPQARVEGWLGDYWQQAQAAGIPVHAEFEAFHRASDLMGVQRHLKVIGIFARICHRDGKPRYLGDVPRFFAYINEVIGRRPELAELGELIAELQAGARA
Protein: Syncrip, isoform B (Syncrip, isoform L) (Q7KSA0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPVVGKRKFDGGHQNPADVKRRYPSGLIGNGGSWGSLPLPQQPLGTNGEQWYMDTFSAWS
Protein: Eukaryotic translation initiation factor 4E-5 (eIF-4E-5) (eIF4E-5) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (P56570)
Organism: Caenorhabditis elegans
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps.
Interaction partners:
- MIF4G domain-containing protein
- Cytoplasmic FMR1-interacting protein homolog
- Eukaryotic initiation factor 4A
- RNA helicase
- mRNA cap guanine-N
- Translational repressor ifet-1
- Eukaryotic translation initiation factor 5
- Nucleolar protein 14
- Histone RNA hairpin-binding protein
- RRM domain-containing protein
Sequence:
MTELTTPIYPLQRNWSWWFLNDDRNASWQDRLKKVYTFNTVPEFWAFYEAILPPSGLNDLCDYNVFRDDIQPKWEAPENWDGGRWLIIINKGKTPEVLDAVWLEILLALIGEQFGKDMESICGLVCNVRGQGSKISVWTKNCNDDDTNMRIGVVLKEKLMAAASKAHSKPLFDVIHYQTHRNCVKKTTSALKYKFSLKSIV
Protein: Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.24) (Glutathione peroxidase homolog 2) (GPx 2) (P38143)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress. Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin). Involved in sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21763276}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:21763276}. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side {ECO:0000269|PubMed:21763276}.
Interaction partners:
- Glutathione reductase
- Peroxiredoxin TSA1
- Thioredoxin-2
- Peroxiredoxin AHP1
- Peroxiredoxin PRX1, mitochondrial
- Superoxide dismutase
- Catalase T
- Thioredoxin-1
- Peroxiredoxin TSA2
- AP-1-like transcription factor YAP1
Sequence:
MTTSFYDLECKDKKGESFKFDQLKGKVVLIVNVASKCGFTPQYKELEELYKKYQDKGFVILGFPCNQFGKQEPGSDEQITEFCQLNYGVTFPIMKKIDVNGSNADSVYNYLKSQKAGLLGFKGIKWNFEKFLVDSNGKVVQRFSSLTKPSSLDQEIQSLLSK
Protein: Complement component C3-3 (Q98977)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
DYSGDDFNVKITVKNFPAKDQELPSTSVSLNLVNKYQALIDVTILERPGFFDEDYTVNQYVYLQAEFPGHLLLEKVVLVSFQTGYIFVQTDKTIYTPESQVHYRVFAVNSGLEPVSDIINVEIMNPDGITLKQNNYKPHNGIISGHFPIPEITRNGNWKVVSNFKNNPHKNFTADFEVKEYVLPSFEVILKVSKSFFHVDDVELSVNIDARYLFGEPVTGFGFVVFGVIQGDGRTSFPSSLQRVELIKGVGKAVLKRQHIKETFPDINNLLQKSLYISVNVLTDTGSEMVKAEKKGIFIVKSPYSIHFKKTPLYFKPGMPYDISVYVTNPDDSPAKDIDVEASHKHQQVQGKTHENGIAKMTINTDVGTAELPITVKTNVNGLRDDRQGTQMMTAKPYKSKDNSQNYIHINIHSAEVKIGERLKVDLSLGSSPAAQHSKHEITYLILSKGQLISSQRLEWRKGQGLVNTHYLTVNKDMIPSFRIVAYYHVGQKEVVSDSVWVDVKDTCMGSLKVDAVSPRASYAPGAEVTLSVIGDSEARVGLVAVDNGVYVLNDKNRLTQTKIWDMIEKHDTGCTAGSGMDSMGVFYDAGLVFASSGAGHTRERTVSSCPVNSRRRRAVTINDVVTTLASQYIGLERQCCMDGMRKNILDYTCERRAQYISDGTDCVEAFLKCCREMATKREEAKTDQLILARSEEEDEDFEVLTTSFPVPSFPESWLWIEESLPRCPDNKQCPVHNRKITLPGSITSWQITAIGLSKTHGICVSEPLKLIVWKNFFLDLKLPYSAVRNEQLEIKAILHNYMEGSITVRVELRETPDVCSSASKKGRYIVTVMVDPRSTRSVPFVIIPMKLGLHTIEVKASVRDWGGRDGVKKELRVVPEGVLTRLQVKKVELDPAKHGGTDTVRVRSGPLANQVPNTPARTHISVTGEQLASTIEAAISGSPLGDLLRQPGGCGEQNMIGMTLPLSPHITWTRPNTWDKVGLERRNQAVSYIQRGYEQELAYRKKDGSYAAFDNEPSGTWLTAYVAKVFAMANPLIVISEDVLCSAVKWLVMKRQRPNGIFEETGKLLHPTMMGDVLGKDVDDTLTAFVLITMQEAHTICIKDDGIRNLPESIEKAKQYLEFRNQHLTNPYSVAITSYALANEGKLNQSILFKHSSTDRTHWPVSENHLLTLEATPSTLEATAYALLALVKAGAFEEAGPIVRWLKSQGFQRGGDSSTQSTIMVFQAVAEYMAKAGKVKDIDLNVDIDISGRTEVVKWSFSKSTALLTRTDKVQQHDNFTVTAKGTGLGELLVTTIYYATPIEKNQDCKNFVLDVDLIKQAKVALNGAQETYMLHIDMLFKSDRNATMTILDISLLTGFVVEVQDLKQLSTGTERYIQRFEMDKKLSERGSLIIYLDQVSNKLADKVAFRIHKVQDVGLLQPVGVTVYEYYAQENRCVKFYHPNKKDGTLNRLCQEDVCRCAEESCSFQKKHGDMSKVKLLDKACEAGMDYVFKASLVNATLESYTDTYLMEIKRIIKEGTDLLLNGEKRLFLAHPSCRKALDLEEGQSYLLMGDTAALIQSGDRFEYVLGERTWIESWPTSDECSIQGPTRERCLEINDFVHVMENEGCVN
Protein: Kinesin, putative (Q57UP1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSERETTSHSPELGGDNNGSVVVAVRVRPLEGLSIEAGGALSMSRFTAQQRMHRRGMSAQEGDKPAVRVGVDRKTVVVLDPENLQYIRESFVFNHVFSPVLLDESLMGTDGGSVGDIARPSGDVYGGISSSGGYNSGVLGCCTKGTKLSAEDRRAELEQQEVYELLGAPLTEHFMKGHNSCLFAYGQEGSGKSYTLSGTARCVGVIPRICKDLLSRASAPCRSPPCEVQRKQEAVKNNLLPLQVSHMSFALRGAYTSAKSGGNFSSPIKNAPPTVLPPSLRNKQNASRVEVTISYMEVCNDWVRDLLKPKRDRDPKCGDADSCTYGSDAFERLKVRYYPRHGPSVEGLTTINVRTWEECWSYIQYGNMERQQLISLRKTHGHTHTIFRITSPKVDPFDECITSVECSPKIDVVELSSVGCLKNSRSPPNTAGITTYEDCRRQLREFNAVQRSLGVLSRVLQAVASGSKNAPYRENLLTHLLSDGLVGGSLTIFCATVLSDVCAHAETLTTLRYAAQTCSTICCMKPNVASVASTGCLNQKQLGTTVESLSPRFEGSTPTVRNDVRGMTTSVSLPFWSDCSGSRAGAVGAASDDGSPSKNGAKGAFCVECLPYIPGAKVERVGTDSYVPPNNCSGVTNITALNQGGCSGPGTLLRRDQQTVGLPPLTGSPGVSSSPRVSWSERLKASASFNNLGCGNTSRGGVEGWQLRSPSSVSDKPSSPSTSAFSSPRNLLRPSSLVPNSGTAVTDSPLQPHTPNRGVGRVSALASSFLILTSPSAVAPSGRIAGLTALGGAHDVISASGVTTGAFPSEVLGGSPIHSWTQHGFLGSPEFVRKKESRRNLVKVFTPEELQPSLASPESCSPKQSCPPTPILSTKNNPTLKPLATSNPVSPTVK
Protein: Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Myristoylated and palmitoylated serine/threonine-protein kinase) (MPSK) (Protein kinase PKL12) (TGF-beta-stimulated factor 1) (TSF-1) (Tyrosine-protein kinase STK16) (EC 2.7.10.2) (hPSK) (O75716)
Organism: Homo sapiens (Human)
Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
Subcellular location: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
Protein: ETS family transcription factor efr1 (Fli-1 proto-oncogene, ETS transcription factor-related sequence) (Q5MBG6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MDCTIKEALSVVSEDQSIFESPFSGPQAMHMKAEIGSPAVFRQASEESIEPTEPDWSGSAAQNSAKRAEHINGTSRESPVDCSVTKRTRHMSNSDGGQLSYQASYPEPRSSPQTATPPSSTTEEKRVIVPADPEVWTQDHVRQWVDWAIKEYALSDVDVSLFQTLDGKALCKLSKEDMMRITSAYNTDILLSHLNYLRESSPTFSYPTNPTNTQPQPRVQVKAAENSFEEIGRRNSWSSSGLPAVPKGSPIEHQHNTRITEPPSRLPQDPYQALGSISSRLANPGSGQIQLWQFLLELLSDSNNSTIITWEGTNGEFKMTDPDEVAKRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFQGISQSHQNHSTEGSVYKFQTEGSYMQSYHSHQPKMNFISPHSTPMSVTTSNFFTPQSTYWNSATSVVYPSSPMPRHPSTHTHLNTYY
Protein: ATP-binding cassette sub-family D member 3 (EC 3.1.2.-) (EC 7.6.2.-) (70 kDa peroxisomal membrane protein) (PMP70) (P16970)
Organism: Rattus norvegicus (Rat)
Function: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty acyl-CoA thioesterase and ATPase activities (By similarity). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10207018}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family D member 1
- Peroxisomal biogenesis factor 19
- DNA repair protein RAD51 homolog
- ATP-binding cassette sub-family D member 2
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal biogenesis factor 11 beta
Sequence:
MAAFSKYLTARNSSLAGAAFLLFCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLILIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRFVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSIIAKYIATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQDKGIEGAQASPLIPGAGEIINADNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGHLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKKGISDQVLKGYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKITEDTVEFGS
Protein: Oxaloacetate tautomerase FMP41, mitochondrial (EC 5.3.2.2) (P53889)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Mitochondrial inner membrane protein SHH4
- 3-isopropylmalate dehydratase
Sequence:
MSYNYLKAARKIICIGRNYAAHIKELNNSTPKQPFFFLKPTSSIVTPLSSSLVKTTRPANSTFNGLNEDGTNPGPIFIPRGVKVHHEIELALIVSKHLSNVTKMKPEEVYDSISGVALALDLTARNVQDEAKKKGLPWTISKGFDTFMPISAIVSREKFSSYKSNLQDIFRVKCSVNGQLRQDGGTNLMLHPLHKILQHISTMISLEPGDIILTGTPAGVGELKPGDRVHCELLQNNDNIVDMNFECENRPGPYEFRET
Protein: Tachykinin-related peptide 6 (TKRP-6) (P86562)
Organism: Acrosternum hilare (Green stink bug) (Nezara hilaris)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APSMGFMGMR
Protein: Suppressor of cytokine signaling 7 (A0A087X1Q5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRPPQLMVFRNVGRPPEEEDVEAAPEPGPSELLCPRHRCALDPKALPPGLALERTWGPAAGLEAQLAALGLGQPAGPGVKTVGGGCCPCPCPPQPPPPQPQPPAAAPQAGEDPTETSDALLVLEGLESEAESLETNSCSEEELSSPGRGGGGGGRLLLQPPGPELPPVPFPLQDLVPLGRLSRGEQQQQQQQQPPPPPPPPGPLRPLAGPSRKGSFKIRLSRLFRTKSCNGGSGGGDGTGKRPSGELAASAASLTDMGGSAGRELDAGRKPKLTRTQSAFSPVSFSPLFTGETVSLVDVDISQRGLTSPHPPTPPPPPRRSLSLLDAFPRIAPIRAAESLHSQPPQHLQCPLYRPDSSSFAASLRELEKCGWYWGPMNWEDAEMKLKGKPDGSFLVRDSSDPRYILSLSFRSQGITHHTRMEHYRGTFSLWCHPKFEDRCQSVVEFIKRAIMHSKNGKFLYFLRSRVPGLPPTPVQLLYPVSRFSNVKSLQHLCRFRIRQLVRIDHIPDLPLPKPLISYIRKFYYYDPQEEVYLSLKEAQLISKQKQEVEPST
Protein: Transcription factor AP-2-alpha (AP2-alpha) (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (AP-2) (P05549)
Organism: Homo sapiens (Human)
Function: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region.
Subcellular location: Nucleus {ECO:0000269|PubMed:12586840}.
Interaction partners:
- Cbp/p300-interacting transactivator 2
- BTB/POZ domain-containing protein KCTD1
- Transcription factor AP-2-beta
- Myc proto-oncogene protein
- Transcription factor AP-2 gamma
- Cellular tumor antigen p53
- Cbp/p300-interacting transactivator 4
- Estrogen receptor
- Transcription factor Sp1
- BTB/POZ domain-containing protein KCTD15
Sequence:
MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK