wanglab/gogpt-training-data huggingface dataset:
Protein: Elastin (Tropoelastin) (P54320)
Organism: Mus musculus (Mouse)
Function: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of elastic fibers. {ECO:0000250|UniProtKB:P15502}.
Interaction partners:
- Fibrillin-1
- Fibronectin
- Fibulin-5
- Decorin
- Vitronectin
- Microfibrillar-associated protein 2
- Galectin-3
- Biglycan
- Protein-lysine 6-oxidase
- Microfibril-associated glycoprotein 4
Sequence:
MAGLTAVVPQPGVLLILLLNLLHPAQPGGVPGAVPGGLPGGVPGGVYYPGAGIGGLGGGGGALGPGGKPPKPGAGLLGTFGAGPGGLGGAGPGAGLGAFPAGTFPGAGALVPGGAAGAAAAYKAAAKAGAGLGGVGGVPGGVGVGGVPGGVGVGGVPGGVGVGGVPGGVGGIGGIGGLGVSTGAVVPQVGAGIGAGGKPGKVPGVGLPGVYPGGVLPGTGARFPGVGVLPGVPTGTGVKAKAPGGGGAFAGIPGVGPFGGQQPGVPLGYPIKAPKLPGGYGLPYTNGKLPYGVAGAGGKAGYPTGTGVGSQAAAAAAKAAKYGAGGAGVLPGVGGGGIPGGAGAIPGIGGIAGAGTPAAAAAAKAAAKAAKYGAAGGLVPGGPGVRLPGAGIPGVGGIPGVGGIPGVGGPGIGGPGIVGGPGAVSPAAAAKAAAKAAKYGARGGVGIPTYGVGAGGFPGYGVGAGAGLGGASPAAAAAAAKAAKYGAGGAGALGGLVPGAVPGALPGAVPAVPGAGGVPGAGTPAAAAAAAAAKAAAKAGLGPGVGGVPGGVGVGGIPGGVGVGGVPGGVGPGGVTGIGAGPGGLGGAGSPAAAKSAAKAAAKAQYRAAAGLGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAGVPGFGAGAVPGSLAASKAAKYGAAGGLGGPGGLGGPGGLGGPGGLGGAGVPGRVAGAAPPAAAAAAAKAAAKAAQYGLGGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGLGAGGGVSPAAAAKAAKYGAAGLGGVLGARPFPGGGVAARPGFGLSPIYPGGGAGGLGVGGKPPKPYGGALGALGYQGGGCFGKSCGRKRK
Protein: Activity-dependent neuroprotector homeobox protein (Activity-dependent neuroprotective protein) (Q9Z103)
Organism: Mus musculus (Mouse)
Function: May be involved in transcriptional regulation. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation. Positively modulates WNT-beta-catenin/CTNN1B signaling, acting by regulating phosphorylation of, and thereby stabilizing, CTNNB1. May be required for neural induction and neuronal differentiation. May be involved in erythroid differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Chromosome {ECO:0000305|PubMed:23071114}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 4
- Chromodomain-helicase-DNA-binding protein 8
- Bromodomain PHD finger transcription factor
- Chromobox protein homolog 1
Sequence:
MFQLPVNNLGSLRKARKTVKKILSDIGLEYCKEHIEDFKQFEPNDFYLKNTTWEDVGLWDPSLTKNQDYRTKPFCCSACPFSSKFFSAYKSHFRNVHSEDFENRILLNCPYCTFNADKKTLETHIKIFHAPNSSAPSSSLSTFKDKNKNDGLKPKQADNVEQAVYYCKKCTYRDPLYEIVRKHIYREHFQHVAAPYIAKAGEKSLNGAVSLGTNAREECNIHCKRCLFMPKSYEALVQHVIEDHERIGYQVTAMIGHTNVVVPRAKPLMLIAPKPQDKKGMGLPPRISSLASGNVRSLPSQQMVNRLSIPKPNLNSTGVNMMSNVHLQQNNYGVKSVGQSYGVGQSVRLGLGGNAPVSIPQQSQSVKQLLPSGNGRSFGLGAEQRPPAAARYSLQTANTSLPPGQVKSPSVSQSQASRVLGQSSSKPPPAATGPPPSNHCATQKWKICTICNELFPENVYSVHFEKEHKAEKVPAVANYIMKIHNFTSKCLYCNRYLPTDTLLNHMLIHGLSCPYCRSTFNDVEKMAAHMRMVHIDEEMGPKTDSTLSFDLTLQQGSHTNIHLLVTTYNLRDAPAESVAYHAQNNAPVPPKPQPKVQEKADVPVKSSPQAAVPYKKDVGKTLCPLCFSILKGPISDALAHHLRERHQVIQTVHPVEKKLTYKCIHCLGVYTSNMTASTITLHLVHCRGVGKTQNGQDKTNAPSRLNQSPGLAPVKRTYEQMEFPLLKKRKLEEDADSPSCFEEKPEEPVVLALDPKGHEDDSYEARKSFLTKYFNKQPYPTRREIEKLAASLWLWKSDIASHFSNKRKKCVRDCEKYKPGVLLGFNMKELNKVKHEMDFDAEWLFENHDEKDSRVNASKTVDKKHNLGKEDDSFSDSFEHLEEESNGSGSPFDPVFEVEPKIPSDNLEEPVPKVIPEGALESEKLDQKEEEEEEEEEDGSKYETIHLTEEPAKLMHDASDSEVDQDDVVEWKDGASPSESGPGSQQISDFEDNTCEMKPGTWSDESSQSEDARSSKPAAKKKATVQDDTEQLKWKNSSYGKVEGFWSKDQSQWENASENAERLPNPQIEWQNSTIDSEDGEQFDSMTDGVADPMHGSLTGVKLSSQQA
Protein: Down syndrome cell adhesion molecule 1, isoform BW (A0A0B4K6Z8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQHYEEDIHKAFVIRGNSAILKCDIPSFVADFVNVISWHSDEKENFYPGTEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVGPKLTSGDDSRTVRIRQEDSVTLLCPAQAYPVPVYRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPRIIPFAFEEGPAQVGQYLTLHCSVPGGDLPLNIDWTLDGQAISEDLGITTSRVGRRGSVLTIEAVEASHAGNFTCHARNLAGHQQFTTPLNVYVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: TrbI protein (O24883)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Bifunctional DNA-directed RNA polymerase subunit beta-beta'
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein bL27
- Small ribosomal subunit protein bS18
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL14
Sequence:
MDNPKGIDGFTNLKEKDIATNENKLLRTITADKMIPAFLITPISSQIAGKVIAQVESDIFAHMGKAVLIPKGSKVIGYYSNNNKMGEYRLDIVWSRIITPHGINIMLTNAKGADIKGYNGLVGELIERNFQRYGVPLLLSTLTNGLLIGITSALNNRGNKEGATNFFGDYLLMQLMRQSGMGINQVVNQILRDKSKIAPIVVIREGSRVFISPNTDIFFPIPRENEVIAEFLK
Protein: tRNA (cytidine(32)-2'-O)-methyltransferase (EC 2.1.1.205) (2'-O-ribose RNA methyltransferase TRM7 homolog 1) (Q9VEP1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}.
Interaction partners:
- tRNA
- tRNA
- Pescadillo homolog
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein BOP1 homolog
- Probable ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- Probable rRNA-processing protein EBP2 homolog
- Nucleolar complex protein 2
- Ribosome biogenesis protein NSA2 homolog
Sequence:
MGKTSKDKRDIYYRQAKDEGWRARSAFKLLHVDEAYGILNGVQRAVDLCAAPGSWSQVLSRKLYDTCETDDEKSAVKIIAVDLQAMAPIRGILQLQGDITKQSTAEAIIGHFGGNEKAQLVVCDGAPDVTGVHEMDEYMQHQLLVAALSIATCVLETGGTFVAKIFKGNATSLLSSQMQIFFKKFDIYKPPSSRPSSIEAFVVCSDFCLPEGYIPQVINPARDDIRLLAQKTGSEVNRRLVPFIACGDLNGLSDPEEGKTSSSDESKSNLEYVYDAVMDDASYPLEFKEILKQVYDEQRHII
Protein: Protein LLP (Protein LAPS18-like) (B0FRH7)
Organism: Aplysia kurodai (Kuroda's sea hare)
Function: Acts as a transcriptional activator of C/EBP. Required for long-term synaptic facilitation at the sensory motor synapse. May function in noxious stimulus-facilitated memory formation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12759182, ECO:0000269|PubMed:16504946}.
Interaction partners:
Sequence:
MAKSIRSKHRRQMRNVKREHFAKKDLDRLKRLASKAQELDLDNVVTMKSAEEIKNKPSTSASDADKGMEVDNTKKVFKKKTQQNEDGHYPQWMNQRAVKKQKVKVAKLKTKKKIGKKIKW
Protein: BZIP domain-containing protein (A1ZAC2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein, isoform B
- AT25643p
- Protein dissatisfaction
- FI01017p
Sequence:
MHSPAQSPILDVTETVSMHSELDAELESKNNPSYSISIPQNLRLTGLGFPGMIGAKRSSETLPAFEYIAPPSHALQALEFPLMELNRVGVIGGGMFPGFVHRRVRGEKRPIPEAQKDAKYFERRKRNNEAAKRSRDARKIREDRIAFRAALLEQENSILRAQVLALRDELQTVRQLLGATTAGGMLSMARQV
Protein: Aquaporin PIP2-3 (Plasma membrane intrinsic protein 2-3) (AtPIP2;3) (Plasma membrane intrinsic protein 2c) (PIP2c) (RD28-PIP) (TMP2C) (Water stress-induced tonoplast intrinsic protein) (WSI-TIP) (P30302)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Water channel required to facilitate the transport of water across cell membrane; mercury-insensitive.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7846153}; Multi-pass membrane protein {ECO:0000269|PubMed:7846153}.
Interaction partners:
- Probable aquaporin PIP2-8
- Aquaporin SIP1-1
- Aquaporin PIP1-1
Sequence:
MAKDVEGPDGFQTRDYEDPPPTPFFDAEELTKWSLYRAVIAEFVATLLFLYVTVLTVIGYKIQSDTKAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLIRAVLYMVAQCLGAICGVGFVKAFQSSHYVNYGGGANFLADGYNTGTGLAAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIFNKSKPWDDHWIFWVGPFIGATIAAFYHQFVLRASGSKSLGSFRSAANV
Protein: Dipeptide transport system permease protein DppC (P0AEG1)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter DppABCDF involved in dipeptide transport. Responsible for the translocation of the substrate across the membrane (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
Interaction partners:
- Dipeptide transport ATP-binding protein DppD
- Dipeptide transport system permease protein DppB
- Dipeptide transport ATP-binding protein DppF
- Dipeptide-binding protein
- Oligopeptide transport ATP-binding protein OppD
- Putrescine export system ATP-binding protein SapD
- Oligopeptide transport ATP-binding protein OppF
- Glutathione transport system permease protein GsiC
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Nickel transport system permease protein NikB
Sequence:
MSQVTENKVISAPVPMTPLQEFWHYFKRNKGAVVGLVYVVIVLFIAIFANWIAPYNPAEQFRDALLAPPAWQEGGSMAHLLGTDDVGRDVLSRLMYGARLSLLVGCLVVVLSLIMGVILGLIAGYFGGLVDNIIMRVVDIMLALPSLLLALVLVAIFGPSIGNAALALTFVALPHYVRLTRAAVLVEVNRDYVTASRVAGAGAMRQMFINIFPNCLAPLIVQASLGFSNAILDMAALGFLGMGAQPPTPEWGTMLSDVLQFAQSAWWVVTFPGLAILLTVLAFNLMGDGLRDALDPKLKQ
Protein: L-aspartate oxidase (LASPO) (EC 1.4.3.16) (Quinolinate synthase B) (Q59767)
Organism: Rhodospirillum rubrum
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P10902}.
Interaction partners:
Sequence:
ILVDAQGRRFMTALDPAAELAPRDVVTRGVAAAIKAGKGAFLDARTALGAAFPQAFPTVYAACRASGIDPVRQPIPIAPAAHYHMGGVLTDSFGRTSIDGLWAVGEVACTGAHGANRLASNSLLEAVVFAARVAGDVGAAPLRRGWPPPAPPDLSPRPPPAEDAAAITRLRATMSARVGVIRDGQGLESALATIETIAAGARSPRLRAMTTAARLITAAALARRESRGAHFRADYPATDPAQSHRATAPFGPLRTVPPHPAQSLGEGLAAPPMETRS
Protein: Multiprotein Bridging Factor 1 (Multiprotein bridging factor 1, isoform B) (Multiprotein bridging factor 1, isoform C) (Multiprotein bridging factor 1, isoform D) (Q9XZ03)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDWDSVTVLRKKAPKSSTLKTESAVNQARRQGVAVDTQQKYGAGTNKQHVTTKNTAKLDRETEELRHDKIPLDVGKLIQQGRQSKGLSQKDLATKICEKQQVVTDYEAGRGIPNNLILGKMERVLGIKLRGKERGQPIAPPGKK
Protein: GA-binding protein subunit beta-1 (GABP subunit beta-1) (GABPB-1) (GABP subunit beta-2) (GABPB-2) (Nuclear respiratory factor 2) (Transcription factor E4TF1-47) (Transcription factor E4TF1-53) (Q06547)
Organism: Homo sapiens (Human)
Function: Transcription factor capable of interacting with purine rich repeats (GA repeats). Acts as a a master regulator of nuclear-encoded mitochondrial genes (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:7799916, ECO:0000305|PubMed:8441384}.
Interaction partners:
- GA-binding protein alpha chain
- Transcription factor A, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Dimethyladenosine transferase 1, mitochondrial
- Tubulin beta-2B chain
- Tubulin beta-3 chain
- Tubulin beta-2A chain
- Tubulin alpha-1A chain
- DNA-directed RNA polymerase, mitochondrial
- Caspase-2
Sequence:
MSLVDLGKKLLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNPESPDTVTIHAATPQFIIGPGGVVNLTGLVSSENSSKATDETGVSAVQFGNSSTSVLATLAALAEASAPLSNSSETPVVATEEVVTAESVDGAIQQVVSSGGQQVITIVTDGIQLGNLHSIPTSGIGQPIIVTMPDGQQVLTVPATDIAEETVISEEPPAKRQCIEIIENRVESAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRLQTNKEAV
Protein: Soluble NSF attachment protein 29 (P83351)
Organism: Caenorhabditis elegans
Function: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. Plays a role in the processing and secretion of the aspartic protease hrg-7 from the intestine.
Subcellular location: Synapse, synaptosome {ECO:0000250}.
Interaction partners:
- t-SNARE coiled-coil homology domain-containing protein
- V-SNARE coiled-coil homology domain-containing protein
- Putative syntaxin 6
- YKT6
- MRG domain-containing protein
- Alpha-soluble NSF attachment protein
- V-SNARE coiled-coil homology domain-containing protein
- Putative syntaxin-5
- t-SNARE coiled-coil homology domain-containing protein
- Syntaxin-1A homolog
Sequence:
MSRNPFDDDYRPSAASSTMPVKSYTTMGHYSGEDEADYYEREIEKTLQESLDSTERSRRHLENSEKIGTSTAQQLLEQREKLENTEKNLDEIHRTTQMTQRNLNSLKSFFGGMFKNKFTKKPQEPTETPTVPQSKSASRLSETATNLSSGGGSATFSGPSGQRTLTESSRSAIKGTRWEAMDNQIDENLDMMSANLRNLQRLGADLGKEVDSQNEMLDRIQYKAERNDGIVRDQDKQMQKILGTGASTSQTTAESLTPSMDTSTKMSLMMKATSLWK
Protein: At2g39210/T16B24.15 (Major facilitator superfamily protein) (Nodulin-like protein) (O80960)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- G-type lectin S-receptor-like serine/threonine-protein kinase At4g27290
- AT1G76160 protein
- tRNA-dihydrouridine synthase
- Protein DETOXIFICATION 8
- Protein DETOXIFICATION 2
- HAD superfamily, subfamily IIIB acid phosphatase
Sequence:
MVAASPGGSMKSLTIQILTGRWFMFFGSLLIMSTAGATYMFGIYSGDIKETLGYDQTTLNLLSFFKDLGANVGVLAGLLNEVTPPWFILLIGAILNFFGYFMIWLAVTERISKPQVWHMCLYICVGANSQSFANTGSLVTCVKNFPESRGVVLGILKGYVGLSGAIITQLYRAFYGEDTKELILMIGWLPAIVSFAFLRTIRIMKVKRQTNELKVFYNFLYISLGLATFLMVVIIINKLSGFTQSEFGGSAAVVIVLLLLPIIVVILEEKKLWKEKQVALNDPAPINVVTEKPKLDSSEFKDDDGEESKEVVEKVKTPSCWTTVFNPPERGDDYTILQALFSVDMLILFLATICGVGGTLTAIDNLGQIGNSLGYPKRSVSTFVSLVSIWNYYGRVVSGVVSEIFLIKYKFPRPLMLTMVLLLSCAGHLLIAFNVPGGLYVASVIIGFCFGAQWPLLFAIISEIFGLKYYSTLYNFGSVASPIGSYLLNVRVAGYLYDVEAGKQYKALGKTRVEGQDLNCIGTSCFKLSFIIIAAVTLFGVLVSMVLVIRTKKFYKSDIYKKFREKALAAEMEMAAPAAARSTVAKEDKDDVKGKVIGKGG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B0BD08)
Organism: Streptococcus pneumoniae
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMGQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQKPLPSVIAENPSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIPKVQAQTEHKSIKNPSQAVTEETYQPQAPKKHRFKMRYLILLASLVLVAASLIWILSRTPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAKKATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAKKVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP
Protein: Formimidoyltransferase-cyclodeaminase (Formiminotransferase-cyclodeaminase) (FTCD) [Includes: Glutamate formimidoyltransferase (EC 2.1.2.5) (Glutamate formiminotransferase) (Glutamate formyltransferase); Formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) (Formiminotetrahydrofolate cyclodeaminase)] (P53603)
Organism: Sus scrofa (Pig)
Function: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus {ECO:0000250|UniProtKB:Q9YH58}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O95954}. Note=More abundantly located around the mother centriole. {ECO:0000250|UniProtKB:O95954}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- 5-formyltetrahydrofolate cyclo-ligase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- methenyltetrahydrofolate cyclohydrolase
- Uncharacterized protein.
- Methionyl-tRNA formyltransferase, mitochondrial
- Serine hydroxymethyltransferase
- Methionine synthase
- Dihydrofolate reductase
Sequence:
MSQLVECVPNFSEGKNQEVIDAISRAVAQTPGCVLLDVDSGPSTNRTVYTFVGRPEDVVEGALNAARAAYQLIDMSRHHGEHPRMGALDVCPFIPVRGVTMDECVRCAQAFGQRLAEELGVPVYLYGEAARTAGRQSLPALRAGEYEALPEKLKQAEWAPDFGPSAFVPSWGATVAGARKFLLAFNINLLSTREQAHRIALDLREQGRGKDQPGRLKKVQAIGWYLDEKNLAQVSTNLLDFEVTGLHTVFEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFLLQDEHRIRLVVNRLGLDSLAPFKPKERIIEYLVPEAGPEQSLLHKPLRTFVREVGSRSAAPGAGSVAAATAAMGAALASMVGLMTYGRRQFEHLDATMRRLIPPFHAASAKLTSLVDADARAFEAYLKAMKLPKDTPEDKDRRAAALQEGLRQAVAVPLALAETVASLWPALQELALCGNLACRSDLQVAAKALETGVFGAYFNVLINLKDVTDDAFKAQVRQRISSLLQEAKTQAALVLDRLEARQA
Protein: Membralin-like protein At1g60995 (Q8GWG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RING/FYVE/PHD zinc finger superfamily protein
- Probable cyclic nucleotide-gated ion channel 20, chloroplastic
Sequence:
MDPEQTFIRVQERFSQILTPRIRGFLEYTYLFVAITLFCILVVMHANYVQQPGCSSELTGVELAEAELMQIKITSAGLWSRNDESTAADVPRVVAATDSLEVSKTDQESSTSEENTDDTFVKIDKEEPRSSFSVSAKENVRAAILRFLKKCYRRISFVLQHTARILRGVRKIWNIIGIPLNLDVPKLLHVLYMDKVNYYAVQWLESKTQEFEPTYLYTMEKGYFLLPDEAKSRHNIRTANVSISARHPCFGNRWQQLLINRVVGYDTIIMNSLQNSAGQGYLYNYQTREFYNLSYSQELPDGSAHFGDYLVTKCGVLMMSLFVFFTTTMSVSFTLRETQTRMLKFTVQLQHHAQHRLPTFQLIFVHVIESLVFVPIMIGILFFLFEFYDDQLLAFMVLVLVWLCELFTLISVRTPISMKFFPRFFLLYFLVFHIYFFSYAYGFSYLALMTTAAFMQHLILYFWNRFEVPALQRFLQSRQSHLQQHPDFHITSSTILASTLHITRLNRTTRNRTPSGPNHTTPNQNTETRSFTADGGGVGNPAQYQEQQEENEANTVPAEPNPQQAGAMSSFSSMLLWILGGASSEGLNSFLSMFRDVRDEDEAQVFADTSPPQNPHHDPLSVD
Protein: Alpha-fibrinogenase A3 (EC 3.4.21.-) (Snake venom serine protease) (SVSP) (Q9PRW2)
Organism: Crotalus atrox (Western diamondback rattlesnake)
Function: Snake venom serine protease that cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is less potent than A1 and A2 alpha-fibrinogenases.
Subcellular location: Secreted {ECO:0000269|PubMed:8024586}.
Interaction partners:
Sequence:
VIGGDECNINEHRSL
Protein: Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP 2) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent 2) (PPi-PFK 2) (Protein MATERNAL EFFECT EMBRYO ARREST 51) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 2) (F4JGR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- transaldolase
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
- Fructose-bisphosphate aldolase 2, chloroplastic
Sequence:
MASQLDLIGGDYIAGISINPPTNSRVTSVYSEVQASRIDHTLPLPSVFKTPFKIIDGPPSSSAGHPEEIEKLFPNLFGQPSALLVPNQSNEVSSDQKLKIGVVLSGGQAPGGHNVICGIFDYLQEYARGSSLFGFRGGPAGIMKGKYIELTSEFVYPYRNQGGFDMICSGRDKIETPEQFKQAEETVTKMDLDGLVVIGGDDSNTNACLLAEHFRAKNMKTLVIGCPKTIDGDLKSKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVFEKKLTLKNVTDNIVDVIYKRAENGYNYGVILVPEGLIDFIPEVQQLISELNEVLAEGNVDEEGQWKKNLKKETLEIFEFLPQTIQEQLMLERDPHGNVQVAKIETEKMLIQMVETELEKKKTEGTYEREFMGKSHFFGYEGRCGLPTNFDATYCYALGYGAGSLLQSGKTGLISSVGNLAAPVEEWTVGGTALTSLMDVERRHGKFKPVIKKAMVELEGAPFKKFASQREEWALKNRYISPGPIQFKGPGSDARNHTLMLELGAQA
Protein: Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha) (Q99NA5)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Aconitate hydratase, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Cytoplasmic aconitate hydratase
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MAGSAWVSKVSRLLGAFHNTKQVTRGFAGGVQTVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTQSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACFATIKDGKSLTKDLGGNSKCSDFTEEICRRVKDLD
Protein: Probable 2-oxoacid dependent dioxygenase (EC 1.14.-.-) (Q9SKK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the hydroxylation of but-3-enyl glucosinolate to 2-hydroxybut-3-enyl glucosinolate, which is toxic to insects, bacteria and nematodes, inhibits seed germination and produces bitter flavors.
Interaction partners:
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Cytochrome P450 81F4
- Cytochrome P450 81F1
- Flavin-containing monooxygenase FMO GS-OX5
- Probable 2-oxoglutarate-dependent dioxygenase AOP1
- Cytosolic sulfotransferase 18
- Cytosolic sulfotransferase 16
- Transcription factor MYB28
- 2-oxoglutarate-dependent dioxygenase AOP3
- Cytochrome P450 81F2
Sequence:
MAENYDRASELKAFDEMKIGVKGLVDAGVTKVPRIFHNPHVNVANPKPTSTVVMIPTIDLGGVFESTVVRESVVAKVKDAMEKFGFFQAINHGVPLDVMEKMINGIRRFHDQDPEVRKMFYTRDKTKKLKYHSNADLYESPAASWRDTLSCVMAPDVPKAQDLPEVCGEIMLEYSKEVMKLAELMFEILSEALGLSPNHLKEMDCAKGLWMLCHCFPPCPEPNRTFGGAQHTDRSFLTILLNDNNGGLQVLYDGYWIDVPPNPEALIFNVGDFLQLISNDKFVSMEHRILANGGEEPRISVACFFVHTFTSPSSRVYGPIKELLSELNPPKYRDTTSESSNHYVARKPNGNSSLDHLRI