wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein YGR126W (P53274)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MPVPSVTVTTDNEYEDISSFSSIDSYKPEPFTGFKDSEAPEQPLLKNDTIVGKGQLEDDSNVDDQHRHSDVHSHHSSSTLKRPTSNSIEKMVTHNALEGNSETVDSLKEDGLNLNKKALPDITAPVTNSAHDAAFPEEYRLETETGLVKLKTLESLKREDSRVSSTKKEHINDHTDMHSTRSKVTTNSQGSSLEPNKLNMAVEKNKKRIEKYQKHKSEKGIKGFFHRIFD
Protein: Exodeoxyribonuclease 7 large subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII large subunit) (Exonuclease VII large subunit) (P9WF31)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
Interaction partners:
- Exodeoxyribonuclease 7 small subunit
- Uncharacterized protein Rv1109c
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- Tyrosine recombinase XerC
- UvrABC system protein C
- Large ribosomal subunit protein uL1
Sequence:
MTQNSAENPFPVRAVAIRVAGWIDKLGAVWVEGQLAQITMRPDAKTVFMVLRDPAADMSLTVTCSRDLVLSAPVKLAEGVQVVVCGKPSFYTGRGTFSLRLSEIRAVGIGELLARIDRLRRLLDAEGLFDPRLKRPIPYLPNMIGLITGRASAAERDVTTVASARWPAARFAVRNVAVQGPNAVGQIVEALRELDRDPDVDVIVLARGGGSVEDLLPFSDETLCRAIAACRTPVVSAVGHEPDNPLCDLVVDLRAATPTDAAKKVVPDTAAEQRLIDDLRRRSAQALRNWVSREQRAVAQLRSRPVLADPMTMVSVRAEEVHRARSTLRRNLTLMVAAETERIGHLAARLATLGPAATLARGYAIVQTVAQTGPEGGSEPQVLRSVHDAPEGTKLRVRVADGALAAVSEGQTNGL
Protein: CAAX prenyl protease 2 (EC 3.4.26.1) (Farnesylated proteins-converting enzyme 2) (FACE-2) (Prenyl protein-specific endoprotease 2) (RCE1 homolog) (hRCE1) (Q9Y256)
Organism: Homo sapiens (Human)
Function: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19188362}; Multi-pass membrane protein {ECO:0000269|PubMed:19188362}.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase
- CAAX prenyl protease 1 homolog
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Ubiquitin carboxyl-terminal hydrolase 17
- GTPase NRas
- GTPase KRas
- Ubiquitin carboxyl-terminal hydrolase 17-like protein 24
- GTPase HRas
Sequence:
MAALGGDGLRLLSVSRPERPPESAALGGLGPGLCCWVSVFSCLSLACSYVGSLYVWKSELPRDHPAVIKRRFTSVLVVSSLSPLCVLLWRELTGIQPGTSLLTLMGFRLEGIFPAALLPLLLTMILFLGPLMQLSMDCPCDLADGLKVVLAPRSWARCLTDMRWLRNQVIAPLTEELVFRACMLPMLAPCMGLGPAVFTCPLFFGVAHFHHIIEQLRFRQSSVGNIFLSAAFQFSYTAVFGAYTAFLFIRTGHLIGPVLCHSFCNYMGFPAVCAALEHPQRRPLLAGYALGVGLFLLLLQPLTDPKLYGSLPLCVLLERAGDSEAPLCS
Protein: PIN domain-containing protein (Q387T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Bms1-type G domain-containing protein
- KRR1 small subunit processome component
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- AATF leucine zipper-containing domain-containing protein
- BING4 C-terminal domain-containing protein
- Uncharacterized protein
- CCAAT-binding factor domain-containing protein
- Small ribosomal subunit protein uS4
- DDB1- and CUL4-associated factor 13
- Nrap protein domain-containing protein
Sequence:
MGKKKNTAMHAIKTVLMKEKNLAQKKKREMDSHHEVPEQVLTKVKDTAAVRFQRNQLTVAAPLQTNMFLSYNKSLGPPFHIWLDTNFINFSMQNKIEIVEGLMDCMLAKVIPCVCDCVMAELEKLGKKFRIALKIARDKRFKRLTCDGKYADDCVVRTVTQHPIYIVATCDQELKRRLRKIPGVPIMYISKHRYTIERLPEVYGAPA
Protein: Protogenin A (Q2EY14)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May play a role in anteroposterior axis elongation.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neurotrophin-7
- Sodium/potassium-transporting ATPase subunit beta
- Protogenin B
Sequence:
MASFKRDLYLFLAVFLSISGVWSFSELFFIKEPHDVTAMRRDAVVLDCQAHGEAPIGIRWLKNGVTITESERVYSLSNGSLLISEVESRKDKSDEGFYQCLAQNKYGSILSQRARLTIASLSTFTQQPASIIVMEGSVARFTCKITATPPPIITWEFNRVTLPLATERITVLPSGVLQIQGVEQRDAGSYRCVAANIVSRRRSTEATLTVTPAMSPRAPQRPRIIAGPQNLTVPAHSTALLECMASGNPRPLISWSRADHKSIDVHKTKVLGNGNLIISDVNPQHAGIYFCRATTPGTRNYTIAAANITVLAPPSLVEWPESVTRPRAGTARFVCTAEGFPTPQITWLKNGEPVRSNGRIKMYNSKLVINQIIPEDDGIYQCEAENIQGSVLAMARLIVVMSDNRPSAPRNIRADTVSSSAIVLAWDRPAYNSEKVIAYSVHYMKAEGLNNEEYQIVIGNDTTRYIIDDLEAGRNYTFYIVAYMPMGASRMSDHVIQHTLEDVPLRAPELSLTSRSPSDIQVSWQPLSHKLSRGRVSAYRLSYRTSSDGTLTQLELSAHKTHQLLEGLQPDTTYLLRIAAATAVGWGEPSAWSSHRTPKASSTKVPLAPELQLESLNCTTVTLRWHLPAGSSSGLQGFKLSYHEEGQSEAAQAQIPPHHRQHTIGGLDPRKKYHIKLLAFSFMGDGYQADQTISTPGCVSVRDRLVPPPPPPHHVYAHSNSSSSVFLHWARPAFTSAQTLNYTVRCNPVGLQNASLVLYLQTAAQSLLVTDLEPNTNYEFAVRLHVDLLSSPWSPVVYQTTLPEAPSRAPVGVKVTLIEGDSALVSWKAPDDRSAAAVTHYTVLYATRRAWAAGDWQMLQREGSITMALLENLQPGQVYLVQVSASNQMGDGPFSAAVELTIHTDGHAHRTHGFSHATVFSDGFYHLDQRSMAGIAVGVCIALTCIIICILILACRSKTRKSCTTKSIRQAGGQTPPTAVRLANESAAESVEVMMPMMRDHFIDAKGGTNLIINSYGPVKPNIEKKRRKRWSFFKKNEKEVKKVSSPAYSYHPGTTLLCYTETSPENPPTTLQGLFGPSGGDSEGSHSSEGSHETSDSGRYSHDDTEATNVSIRSRPASLQDDGNQTPVHEKQLETTLQEQEMTDLHPV
Protein: Keratin-associated protein 8-1 (High glycine-tyrosine keratin-associated protein 8.1) (Q8IUC2)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 11-1
- Keratin-associated protein 7-1
- Keratin-associated protein 24-1
- Keratin-associated protein 13-1
- Keratin-associated protein 15-1
- Keratin-associated protein 19-3
- Keratin-associated protein 26-1
- Keratin-associated protein 6-1
- Keratin, type I cuticular Ha8
- Keratin-associated protein 3-1
Sequence:
MLCDNFPGAVFPGCYWGSYGYPLGYSVGCGYGSTYSPVGYGFGYGYNGCGAFGYRRYSPFALY
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (A0A060Y643)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362020}; Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000256|RuleBase:RU362020}.
Interaction partners:
- triacylglycerol lipase
- AAA+ ATPase domain-containing protein
- Uncharacterized protein
- Diacylglycerol kinase iota-like domain-containing protein
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Diacylglycerol kinase
- Uncharacterized protein
- Diacylglycerol kinase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Diacylglycerol kinase
Sequence:
MGKENTFLVTVWIILANICVSFSSTPEQTLFGNSNSTEWLEDYTDIVSKFSLRTAEIPDDDLCYIVPGQPLTIPKCEFNPGYKTFVVIHGWTVTGLFESWVPKLVTALYKREPKANVIVVDWLTRAQQHYLTSAANTKLVGKDVAKFVNWLQKTLDYPWEKIHLLGYSLGAHVAGIAGLLTNHKVSRITGLDPAGPTFEFADAQSTLSPDDALFVDVLHTNTRGSPDRSIGIQRPVGHVDIYPNGGTFQPGCDLQNTMMMIATTGIRNMDQLVKCSHERSIHLFIDSLVNAAEHQTMAYRCSSKEAFMKGMCLNCRKNRCNKVGYGVNKVRLPRNTKMYLKTREMMPFKLFHYQVKVHFFSSEKLAYTEQPMKISLYGTHDEKIDIPYTMPFLNTNSTVSFLLTTDVDVGELLMVKLRWEKDAYFSWSDIWGNKNFHIRKMRVKAGETQSRVIFSAKDGEYAYLIRGKDDVVFVKSKEDNMSRKEKTMHRLKMQGSHFKNNIA
Protein: Auxin-responsive protein IAA18 (Indoleacetic acid-induced protein 18) (Q5W670)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Auxin response factor 7
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 3
- Auxin response factor 9
- Auxin response factor 15
- Auxin response factor 2
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 16
Sequence:
MEEEFKDKGLPPTLLHLIPDGREWKVKEADGEGSRNTNLDADEDKELELKLGLPGVQQEERAADSREKIQQQQRESSSEPSIGCFPTHSKPTTSIGTTGAKRGFFAIVGATLEGYNQSHRDTEECGKELTLGDENMAGERKKGCCPSPPCSAAAHSSNPQGRGAIPPVVGWPPIRSFRRNLTNGSSFKQSPERQNDEADDKAKPICKKRPLVKINMDGIPIGRKVDLQIYDSYQKLSSAVEELFRGFLEAQKDLSCAESGEQGAEDKIFSGLLDGTGVYTLVYEDNDGDRMLAGDIPWKVFVSTVKRLRVMRRSELPHDMIGADPVK
Protein: Alkyl hydroperoxide reductase E (EC 1.11.1.29) (Mycoredoxin-dependent peroxiredoxin) (Peroxiredoxin AhpE) (Prx) (Thioredoxin peroxidase) (TPx) (P9WIE3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection.
Interaction partners:
- Uncharacterized protein Rv2239c
- Uncharacterized protein Rv2240c
- Probable conserved integral membrane protein
- Uncharacterized protein
- Thioredoxin reductase
- Indole-3-glycerol phosphate synthase
- Protein DipZ
Sequence:
MLNVGATAPDFTLRDQNQQLVTLRGYRGAKNVLLVFFPLAFTGICQGELDQLRDHLPEFENDDSAALAISVGPPPTHKIWATQSGFTFPLLSDFWPHGAVSQAYGVFNEQAGIANRGTFVVDRSGIIRFAEMKQPGEVRDQRLWTDALAALTA
Protein: Outer dynein arm-docking complex subunit 4 (Tetratricopeptide repeat protein 25) (TPR repeat protein 25) (Q7ZU45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and in the docking of ODA in ciliary axoneme.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96NG3}.
Interaction partners:
- Armadillo repeat containing 4
- Coiled-coil domain containing 151
- Coiled-coil domain-containing 114.
- Calaxin
- Dynein assembly factor with WD repeat domains 1
- Tektin
- Si:ch211-103e16.5.
- Dynein, axonemal, intermediate chain 1, paralog 1.
- Tetratricopeptide repeat domain 9C
- Dynein axonemal assembly factor 4.
Sequence:
MFDNEEGQGPKSTFTTYMAEGDQLFQRGEYVKAVESFTTALTLQPDDKNCLVSRSRCYVKLGDAENALKDAESSLKDNKNYFKGLYQKAEALYTMGDFEFALVYYHRGHKLRPELQEFRLGIQKAQEAIDNSVGSPSSVKLVNKGDLSFFHNGVHPQNLNPSNKKESKKHSKKTDKGEKTAKQLLGELYSDREYLKKLLQDEDLVKCKIRSGERVQDLIVGSISYLDTRMAFWQQQKPIYARQRDRKLMQQQWSKVLHKPPSDPTRYVLSSLEEIDTALSAGYTESGLNKARELMKVVKDWSEDALPNKNEVLGNLHSYIGNALMDLGNMDRALHHHEKDLELAKKCDLTDSKSRALDNIGRVYARIGKFQQAIEVWEKKLPLACGGLEKAWLFHEIGRCYLELKRYMEARDYGSRSLMAADDISDEKWQLNASVLMAQAELKLSNYKASVLHFERALERAKLLQDDSASEAIQKALCEARLRVTQ
Protein: Guanosine-inosine kinase (EC 2.7.1.73) (P0AEW6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively. Can also use deoxyguanosine and xanthosine, but not adenosine, uridine, cytidine or deoxythymidine. Shows a strong preference for guanosine. dATP can serve as a phosphate donor as well as ATP. Shows weaker activity with UTP and CTP.
Interaction partners:
- Xanthine-guanine phosphoribosyltransferase
- Adenosine deaminase
- Hypoxanthine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Pyrimidine 5'-nucleotidase YjjG
- Adenylosuccinate synthetase
- Guanylate kinase
- Adenine phosphoribosyltransferase
- Purine nucleoside phosphorylase DeoD-type
- GMP reductase
Sequence:
MKFPGKRKSKHYFPVNARDPLLQQFQPENETSAAWVVGIDQTLVDIEAKVDDEFIERYGLSAGHSLVIEDDVAEALYQELKQKNLITHQFAGGTIGNTMHNYSVLADDRSVLLGVMCSNIEIGSYAYRYLCNTSSRTDLNYLQGVDGPIGRCFTLIGESGERTFAISPGHMNQLRAESIPEDVIAGASALVLTSYLVRCKPGEPMPEATMKAIEYAKKYNVPVVLTLGTKFVIAENPQWWQQFLKDHVSILAMNEDEAEALTGESDPLLASDKALDWVDLVLCTAGPIGLYMAGFTEDEAKRKTQHPLLPGAIAEFNQYEFSRAMRHKDCQNPLRVYSHIAPYMGGPEKIMNTNGAGDGALAALLHDITANSYHRSNVPNSSKHKFTWLTYSSLAQVCKYANRVSYQVLNQHSPRLTRGLPEREDSLEESYWDR
Protein: Protrudin (Zinc finger FYVE domain-containing protein 27) (Q6P7B7)
Organism: Rattus norvegicus (Rat)
Function: Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport. Promotes axonal elongation and contributes to the establishment of neuronal cell polarity. Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (By similarity).
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:17082457}; Multi-pass membrane protein {ECO:0000269|PubMed:17082457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5T4F4}; Multi-pass membrane protein {ECO:0000255}. Cell projection, growth cone membrane {ECO:0000269|PubMed:17082457}; Multi-pass membrane protein {ECO:0000269|PubMed:17082457}. Note=Localizes at both dendrites and axons. Localizes to endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q3TXX3, ECO:0000250|UniProtKB:Q5T4F4}.
Interaction partners:
- Ras-related protein Rab-11A
- FYVE and coiled-coil domain-containing protein 1
- PDZ domain-containing protein 8
- Receptor expression-enhancing protein
- Spastin
- Vesicle-associated membrane protein-associated protein A
- StAR-related lipid transfer protein 3
- Vesicle-associated membrane protein-associated protein B
- Atlastin-1
- Kinesin heavy chain isoform 5A
Sequence:
MQSSDRDLSGPEASPSVMPEVLSECSPAPTKSTAFDLFNLVLSYKRLEIYLEPLKDAGDGVRYLLRWQMPLCSLLTCLGLNILFLTLNEGAWYSVGALIISVPALLGYLQEVCRAQLPESELMRRKYHSVRQEDLQRVRLSRPEAVAEVKSFLIRLEAFLARLCYTCESAYRVLHWENPVVSSQFYGALLGMVCMLYLLPLCWVLALLNSTLFLGNGEFFRVVSEYRACLQRRMSPKQEECVCEGSALQDAGGRAVVLDSTPAPTPTEDLTPGSVEEAEEAEPDEEFKDAIEEDDEGTPCPAEDELTMQDNGFLSKNEVLRSKVSKLTERLRKRYPTNNFGNCAGCAATFSVLKKRRSCSNCGNSFCSRCCSFKVPKSSMGATAPEAQRETVFVCASCNQTLSK
Protein: Anion exchange protein (A9NIM6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MTDPVTSDQLTNAVDSVVHNPESSSSPVRVSQREEEEEDDLNKSLGVQRFQQILSPTARVPGDQHRSYNEKDFEYHRQSSHHIHHPLSKLPGDNRRKKSGRKRRRSSSKPHKVCSSPSGALAIEEGEDEEEEEEEESAENQSVTPAPTIDNERKDNVQFFVSDDDPHVSTPETSDPVPTRGILIVPTTAVCSEPQDSTSTEASEAAPASPSTAEHGSIPRVSSRSYDLQERRRTGNMTGTEQAKYQRIPTDEYEARTLASADLDGIKSHRFEDVPGVRRHLVRKSTKGQMVHISKDHKERSTRSRKLDRTPHEVFVELNELIMDKNQEMQWRETARWIKFEEDVEEETDRWGKPHVASLSFRSLLELRKTIAHGAVLLDLDQKTLPGISHQVVEQMIISDQIKAEDRANVLRALLLKHSHPSDEKEHITSFPRNISAASLGSLISHHQSSSNHLTIPETSVMEPLMGSSRASQDSTVHIDIDKNEKDSATPIGMHRSKSKHELKLLEKIPENAEATVVLVGSVDFLEQPTMAFVRLQEAVELDSVLEVPVPVRFLFVLLGPPSTNMDYHQIGRSISTLMSDKQFHEAAYLADDRQDLLNAINGFLDCSIVLPPSELGGEDLLRSVAHFQREMLRKREEQGVALMAKEPKSLQEKEALLAPFKPEDDPLKRTGRLFGGLIRDAQRRYPKYISDFRDALNPQCMAAVIFIYFAALSPAITFGGLLGEKTEGLLGVSELIVATCVQGVLFCLLGAQPLLIVGFSGPILVFEEAFFSFCKGNNMEYLTGRVWIGFWLIIIVVLMVAFEGSFMVRFVSRFTQEIFSFLISLIFIYETFSKLAKIFQEHPLQRCSAVLVDVRNSSLNSSMDEVTESPLAVTNSSSQEVLKVVGEPNTALLSLVLMSGTFLIAFYLRKFKNSAFFPGRLRRVIGDFGVPIAILIMVLVDYSVKDTYTQKLSVPRGFSVTSPDKRGWIVNPLGSDGQFPIWMMFASILPALLVFILIFMETQITTLIVSKKERMLVKGSGFHLDLLLIVTLGGTSALFGLPWMAAATVRSVTHANALTVMSKAVAPGDKPRIQEVKEQRVTGLLVAILVGLSIVIGDLLRQIPIAVLFGIFLYMGVMSLNGIQMTERILLLLMPPKYHPDHTYVRKVRTLRMHLFTAIQVVCLAVLWAVMSTVASLAFPFVLIMTVPVKMFLLPRIFSNREMQCLDADDAEPTFDEKEGQDEYTEMHMPV
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (D3NQA9)
Organism: Caenorhabditis elegans
Interaction partners:
- Mitochondrial fission process protein 1
- Carbonic anhydrase
- Putative carbonic anhydrase-like protein 2
- Putative carbonic anhydrase 5
- Putative carbonic anhydrase 3
- Alpha-carbonic anhydrase domain-containing protein
- Tubulin-specific chaperone D
Sequence:
MPGLERILNGVIRFRQTVRKDLVKQFERIRDNPHPTAVFFTCMDSRMLPARITSSQVGDMFVVRNSGNMIPHANNYGKILRRGDTTGKENREKENWKPRPFLPPETPRREDLVEKVIYCAKSPSGYEVSVTTEPAALELAVKRGKINHVIVCGHSDCKAINTLYNLHKCPKSFDPESPMDHWLRRHGFNSIRKLEKRLADKNAGPIEFVSDNPLFSFSAVIDPEDKLNVEDKLSQINTLQQLENVASHGFLKEFLVSQTVDLHAMWFDIYTGEMHMFSKPNKQFVLVDESNVEELIDEVEKHQT
Protein: Protein RecA (Recombinase A) (A3PLJ2)
Organism: Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter sphaeroides)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
Sequence:
MATANLLDLNGRREMDKAKALESALAQIERQFGKGSIMKLGANSPVMEIEATSTGSLGLDIALGIGGLPKGRIIEIYGPESSGKTTLTLHVVAEEQKKGGVCAFVDAEHALDPQYAKKLGVNLDELLISQPDTGEQALEIVDTLVRSGAVNLIVVDSVAALTPKSEIEGDMGDMQMGSQARLMSQAMRKLTASIGRSNCMVIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRTGAIKDRDNVIGNTTKVKVVKNKVAPPFREVEFDIMYGEGISKTGELVDLGVKAGVVEKSGSWYSYGDERIGQGRENAKAFLRANPTVAGDIEDRIRASHGLDFSTGEDGKGDDLVDM
Protein: N-acetyltaurine hydrolase (EC 3.1.-.-) (Phosphotriesterase-related protein) (Q96BW5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q60866}.
Interaction partners:
Sequence:
MSSLSGKVQTVLGLVEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAISKEPIVMKNLYWIQKNAYSHKENLQLNQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSWPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTILDKKELLEFAQLGCYLEYDLFGTELLHYQLGPDIDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWLTFK
Protein: Large ribosomal subunit protein uL10 (50S ribosomal protein L10) (P9WHE7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Interaction partners:
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein bS6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL18
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL29
Sequence:
MARADKATAVADIAAQFKESTATLITEYRGLTVANLAELRRSLTGSATYAVAKNTLIKRAASEAGIEGLDELFVGPTAIAFVTGEPVDAAKAIKTFAKEHKALVIKGGYMDGHPLTVAEVERIADLESREVLLAKLAGAMKGNLAKAAGLFNAPASQLARLAAALQEKKACPGPDSAE
Protein: Palmitoyltransferase app (EC 2.3.1.225) (Protein approximated) (A2VEY9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Palmitoylates Dlish which is required for the apical cell cortex localization, total cellular level and full activity of dachs.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18719403}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18804377}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ras modification protein ERF4
- Uncharacterized protein, isoform A
- SH3 domain-containing protein Dlish
- aralkylamine N-acetyltransferase
- aralkylamine N-acetyltransferase
- Ras-like protein 1
Sequence:
MNLLCCCCCSNMAPNQRVTRKWELFAGRNKFYCDGLLMSAPHTGVFYLTCILITGTSALFFAFDCPFLADSINPAIPIVGAVLYFFTMSSLLRTTFTDPGVIPRASNDEAAYIEKQIEVPNSLNSPTYRPPPRTKEVLVKGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGKRNYRFFYLFLVSLAFLAVFIFSCSVTHLVLLMKKEHEVFNVIKAAPFTVIVVFICFFSIWSVIGLAGFHTYLTTSDQTTNEDLKGSFSSKGGPRTQNPYSRGNICLNCCHILCGPMTPSLIDRRGIATDEFIQQMQHQSSPRHALSDVLSASHMVTTSQPMMGGLGGGGIGGAGGGISIGGAELKPRFYDESNPSSSTLEGNGGAINGHGNGHGNGFDHPPPSYDLVQNGNSNSLAQLVDNEIPLVQMDIPAYTHQTATQARQYRHRHHKQRQICNGGTVSYENQLANASSEDELDDPDVVVVGSPEVVAAVAAIASNKAREMRNRSGSYSNLFDADFEAALVNSSLADNHVRGEGASSSGKPSAGAALLAAAISGKTENMYSNVLPVDNDTDPADSTLHVYSNIIDERKQQEQANNVLSSTLLCDDLDLDDPVSASCHVKRKSLGDGAEQVKSAERLRMLHDNTMIDTALDLDSLDGSSMGNNSQSCLVKSGKPNATSVTTNVAIV
Protein: Cytosolic sulfotransferase 15 (AtSOT15) (EC 2.8.2.39) (Sulfotransferase 2a) (AtST2a) (Q8L5A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to specifically catalyze the sulfate conjugation of hydroxyjasmonates, with a preference for 12-hydroxyjasmonate over 11-hydroxyjasmonate. No activity with 12-hydroxyjasmonic acid methyl ester, cucurbic acid, 7-iso-cucurbic acid, 6-epi-cucurbic acid, 6-epi-7-iso-cucurbic acid and their methyl esters, prostaglandin E2, arachidonyl alcohol and 11-eicosenol.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Sulfotransferase
- Cytochrome P450 94C1
- Cytochrome P450 94B3
- NAD
- IAA-amino acid hydrolase ILR1-like 6
- IAA-amino acid hydrolase ILR1-like 4
- Cytochrome P450 94B1
Sequence:
MATSSMKSIPMAIPSFSMCHKLELLKEGKTRDVPKAEEDEGLSCEFQEMLDSLPKERGWRTRYLYLFQGFWCQAKEIQAIMSFQKHFQSLENDVVLATIPKSGTTWLKALTFTILNRHRFDPVASSTNHPLFTSNPHDLVPFFEYKLYANGDVPDLSGLASPRTFATHLPFGSLKETIEKPGVKVVYLCRNPFDTFISSWHYTNNIKSESVSPVLLDQAFDLYCRGVIGFGPFWEHMLGYWRESLKRPEKVFFLRYEDLKDDIETNLKRLATFLELPFTEEEERKGVVKAIAELCSFENLKKLEVNKSNKSIKNFENRFLFRKGEVSDWVNYLSPSQVERLSALVDDKLGGSGLTFRLS
Protein: C2H2-type domain-containing protein (Q3TAD2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYKKTDFSFLLYLQAQDAGIGVSILLCVRALQLRSSEDEEMKASVCKTISCLLPEDLEVRRACQLTEFLIEPSLDGFNMLEELYLQPDQKFDEENAPVPNSLRCELLLALKAHWPFDPEFWDWKTLKRHCHQLLGQEASDSDDDLSGYEMSINDTDVLESFLSDYDDGKEDKQYRRSLTDQNKEKRDKKPIGSSERYQRWLQYKFFCLLCKRECIEARILHHSKMHMEDGIYTCPVCIKKFKRKELFVPHVMEHVKMPPSRSHRSRKKLLLKRAQRGIYPKSPTGSLEQNSRASQGRVS
Protein: Hexose transporter 1 (PfHT1) (Q7KWJ5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000269|PubMed:10066789}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Major facilitator superfamily domain-containing protein, putative
Sequence:
MTKSSKDICSENEGKKNGKSGFFSTSFKYVLSACIASFIFGYQVSVLNTIKNFIVVEFEWCKGEKDRLNCSNNTIQSSFLLASVFIGAVLGCGFSGYLVQFGRRLSLLIIYNFFFLVSILTSITHHFHTILFARLLSGFGIGLVTVSVPMYISEMTHKDKKGAYGVMHQLFITFGIFVAVMLGLAMGEGPKADSTEPLTSFAKLWWRLMFLFPSVISLIGILALVVFFKEETPYFLFEKGRIEESKNILKKIYETDNVDEPLNAIKEAVEQNESAKKNSLSLLSALKIPSYRYVIILGCLLSGLQQFTGINVLVSNSNELYKEFLDSHLITILSVVMTAVNFLMTFPAIYIVEKLGRKTLLLWGCVGVLVAYLPTAIANEINRNSNFVKILSIVATFVMIISFAVSYGPVLWIYLHEMFPSEIKDSAASLASLVNWVCAIIVVFPSDIIIKKSPSILFIVFSVMSILTFFFIFFFIKETKGGEIGTSPYITMEERQKHMTKSVV
Protein: Large ribosomal subunit protein bL19cy (50S ribosomal protein L19-2, chloroplastic) (Q8RXX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Located at the 30S-50S ribosomal subunit interface and binds directly to 23S ribosomal RNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein bL31c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL3c
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein bL9c
- Large ribosomal subunit protein bL21c
Sequence:
MATSSHLLPQALHMIPRTPSFSSKNLGVSSILPRASSVNSRLSVSRVFLNHSSSNFGFAIDSKKRKEFIAKAEESTEGETEAVVENAVETEAEGEGEATVAAEEAKPPWKTRVKLGDIMGLLNKKAIEVAETVRPVPGLRTGDIVEIKLEVPENKRRLSIYKGIVMSRQNAGIHTTIRIRRIIAGIGVEIVFPIYSPNIKEIKVVSHRKVRRARLYYLRDKLPRLSTFK