wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) (Enoylpyruvate transferase) (UDP-N-acetylglucosamine enolpyruvyl transferase) (EPT) (O51428)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
Interaction partners:
- UDP-N-acetylenolpyruvoylglucosamine reductase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylmuramyl-tripeptide synthetase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramate--L-alanine ligase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- D-alanine--D-alanine ligase
- DNA gyrase subunit B
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MHSYIVEGGYKIGGQITASGNKNAALPCILAALLTDEEVILENIPNINDVKVVLDILNDIGADIAREGNTLKIKVLNIVKTEIDSSFTDLIRASILLLGPFVSRFGKIDMALPGGDVIGKRRLDTHFYGLCKLGAKLSTKDRRIVLKANKLVGAEMFLDEASVTATENIIMAAVLAEGNTVIMNAACEPHVQDLCNMLNSMGANILGIGSNVLEIKGVKKLSGTVFRIGADFMQVGSLISLAALTGGELEIKKADPQHFRLIRHVYSRLGINFEYDRENVYVRNKQELKVKLDFGGHIPKIDDGPWPAFPTDLMSIIVVTATQVEGTVLVFEKMFESRMFFVDKLIKMGARIVLCDPHRVVVTGKSSLKGNVLSSPDVRAGMSLLIAAFVAEGRSEIQNVYQIERGYEDVVNKLINLGAKIKKVKSQ
Protein: 5-formyltetrahydrofolate cyclo-ligase (5-FCL) (EC 6.3.3.2) (5,10-methenyltetrahydrofolate synthetase) (MTHFS) (P0AC28)
Organism: Escherichia coli (strain K12)
Function: Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10-methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).
Interaction partners:
- Bifunctional protein FolD
- Phosphoribosylglycinamide formyltransferase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Serine hydroxymethyltransferase
Sequence:
MIRQRRRALTPEQQQEMGQQAATRMMTYPPVVMAHTVAVFLSFDGELDTQPLIEQLWRAGKRVYLPVLHPFSAGNLLFLNYHPQSELVMNRLKIHEPKLDVRDVLPLSRLDVLITPLVAFDEYGQRLGMGGGFYDRTLQNWQHYKTQPVGYAHDCQLVEKLPVEEWDIPLPAVVTPSKVWEW
Protein: Serine/threonine-protein kinase PLK (EC 2.7.11.21) (Polo-like kinase) (Q4KMI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSAAIAKPSAKPSAHVDPKSAPLKEIPDVLVDPRTMKRYMRGRFLGKGGFAKCYEITDMDTKEVFAGKVVPKSMLLKPHQKEKMSTEIAIHKSLDNPHVVGFHGFFEDDDFVYVVLEICRRRSLLELHKRRKAVTEPEARYFMRQTIQGVQYLHNNRVIHRDLKLGNLFLNDDMDVKIGDFGLATKIEFDGERKKTLCGTPNYIAPEVLCKKGHSFEVDIWSLGCILYTLLVGKPPFETSCLKETYIRIKKNEYSVPRHINPVASALIRRMLHADPTLRPSVAELLTDEFFTSGYAPMRLPTSCLTVPPRFSIAPSSLDPALLRKPLSSLNKGTDSPIEEMGKMDQPQREDLQQRDGPEQPDTHLTDMLQQLAVVNAAKPSDRDFIRQEEAEDPACIPVFWISKWVDYSDKYGLGYQLSDNSVGVLFNDSTRLIMCADGDSLQYIDRNSLESYLSVRSYPSALSKKITLLKYFRNYMSEHLLKAGANITPREGDELTRLPYLRHWFRTKSAIVLHLSNGTVQINFFQDHTKLILCPLMGAVTYINEKREFYTYKMTLIEEFGCCKELASRLRYARNMVEKLMACKSSTTAATSAR
Protein: Splicing regulator sde2 (Silencing defective protein 2) (Telomere maintenance protein SDE2) (O14113)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in pre-mRNA splicing by facilitating excision of introns featuring relatively long (>21 nucleotides) spacing between the branchpoint and 3'-splice site (ss). Recruits cactin to the spliceosome which may enable folding of RNA between the branchpoint and 3'-ss, to guide the splice site towards the spliceosome's catalytic center. Required for proper chromatin organization by assisting splicing of components involved in genomic stability and telomere organization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28947618}. Nucleus {ECO:0000269|PubMed:28947618}. Note=The unprocessed form localizes to the nucleus. Following cleavage in the nucleus, the C-terminal sde2 remains nuclear, whereas the N-terminal UBL appears to disperse throghout the cell. {ECO:0000269|PubMed:28947618}.
Interaction partners:
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-processing factor 17
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor cwf10
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor cwf15
- Pre-mRNA-splicing factor cwf17
- Pre-mRNA-splicing factor cwf5
Sequence:
MECKTVFLNGDFLKNSVNVNLNRLATVETLLRHVLGDSYETVLERAYLTHQSRIVHPDIQLCKLEGKSTSAHLNLTLCTRVLGGKGGFGSQLRAAGGRMSKKRNEQENQDSCRDLDGNRLGTIRQAKELSEYLAKKPAETRAKKEAKKQKLNKVLAADSSSSRFDDHEYLEDLEQSVSNVRDAFQNSLLYRRGSTSASSFSSGSNGATTDEPAEKEARNNNSSINSWSRRMQASESSNEAEGEDSESQTSKSLYEWDDPLYGL
Protein: Protein NEL (93 kDa protein) (Q90827)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Transmembrane protein 117
- Protein phosphatase 4 regulatory subunit 4.
Sequence:
MESGCGLGTLCLLLCLGPVVGFGVDPSLQIDVLSELGLPGYAAGVRQVPGLHNGSKAFLFPDTSRSVKASPETAEIFFQKLRNKYEFTILVTLKQAHLNSGVIFSIHHLDHRYLELESSGHRNEIRLHYRTGSHRSHTEVFPYILADDKWHRLSLAISASHLILHVDCNKIYERVVEKPFMDLPVGTTFWLGQRNNAHGYFKGIMQDVQLLVMPQGFISQCPDLNRTCPTCNDFHGLVQKIMELQDILAKTSAKLSQAEQRMNKLDQCYCERTCTMKGMTYREFESWTDGCKNCTCMNGTVQCEALICSLSDCPPNSALSYVDGKCCKECQSVCIFEGRTYFEGQRETVYSSSGDCVLFECKDHKMQRIPKDSCATLNCPESQQIPLSHSCCKICKGHDFCTEGHNCMEHSVCRNLDDRAVCSCRDGFRALREDNAYCEDVDECAEGQHYCRENTMCVNTPGSFMCICKTGYIRIDDYSCTEHDECVTNQHNCDENALCFNTVGGHNCVCKLGYTGNGTVCKAFCKDGCRNGGACIASNVCACPQGFTGPSCETDIDECSDGFVQCDSRANCINLPGWYHCECRDGYHDNGMFSPSGESCEDIDECATGRHSCANDTVCFNLDGGYDCRCPHGKNCTGDCIHEDKIKHNGQIWVLENDRCSVCSCQSGYVMCRRMVCDCENPTVDLFCCPECDPRLSSQCLHQSGELSYNSGDSWIQNCQQCRCLQGEVDCWPLPCPEVDCEFSVLPENECCPRCVTDPCQADTIRNDITKTCLDETNVVRFTGSSWIKHGTECTLCQCKNGHVCCSVDPQCLQEL
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (F4I456)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transducin family protein / WD-40 repeat family protein
- AT4G30480 protein
- Outer envelope protein 64, mitochondrial
- Topless-related protein 3
- Chaperone DnaJ-domain superfamily protein
- E3 ubiquitin-protein ligase RMA
- Expressed protein
- Chaperone DnaJ-domain superfamily protein
- Topless-related protein 4
- Transcriptional corepressor LEUNIG_HOMOLOG
Sequence:
MALWMDAGATPTTEKEKADLEAISALKESTAIEFKEEGNECVRKGKKHYSEAIDCYTKAISQGVLSDSETSILFSNRSHVNLLLGNYRRALTDAEESMRLSPHNVKAVYRAAKASMSLDLLNEAKSYCEKGIENDPSNEDMKKLLKLVNSKKQEKEQHEAQASQAVVEAKACLSAIENRGVKIGKAMYRELTGLKKPMLDKNNILHWPVLLLYAEAMTSDFVEDFCETDMFATHLDMMFSEDSPPLPWDKNNEYSRDVIELYYEASSGTPLPRSRVLQYLLEGTKGSQAETTGEEDTSATKTPSYLKGSSGMVKVNERRTLHDVLKEPKFVIPEIPVFYIVSKRSKFYKDFTAGKWTPPN
Protein: 5'-deoxynucleotidase hdd1 (EC 3.1.3.89) (P87242)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNAAKSLSIVPFLDCLSRLKTTPRTGWLYHGIEKPESIADHMYRMGILTMLCNDPSINKERCLKIAVVHDMAESIVGDITPHENVSKEEKHRMESEAMVSITQQLIPLNLSLQAEEIKELFLEYESASTPEAKFVKDIDKFEMIAQMFEYERKFNGEKDLSQFTWAGKLIQHPLVKGWLNDVLQEREQFWASVRQKKL
Protein: Cullin 4B (A0A669KAX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFPTGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQVKYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA
Protein: Cytochrome c oxidase assembly protein COX19 (hCOX19) (Q49B96)
Organism: Homo sapiens (Human)
Function: Required for the transduction of an SCO1-dependent redox signal from the mitochondrion to ATP7A to regulate cellular copper homeostasis. May be required for the assembly of mitochondrial cytochrome c oxidase (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16212937, ECO:0000269|PubMed:23345593, ECO:0000269|PubMed:23676665}. Mitochondrion intermembrane space {ECO:0000269|PubMed:23345593, ECO:0000269|PubMed:23676665}. Mitochondrion {ECO:0000269|PubMed:23345593, ECO:0000269|PubMed:23676665}. Note=Partitions between mitochondria and the cytosol in a copper-dependent manner. Enriched in the cytosol when intracellular copper concentrations are elevated. {ECO:0000269|PubMed:23345593}.
Interaction partners:
- Cytochrome c oxidase copper chaperone
- Bifunctional coenzyme A synthase
- Cytochrome c oxidase assembly protein COX11
- Mitochondrial intermembrane space import and assembly protein 40
- Cytochrome c oxidase assembly factor 6 homolog
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 7
- Cytochrome c
- Cytochrome c oxidase assembly factor 5
- FAD-linked sulfhydryl oxidase ALR
- Cytochrome c oxidase assembly factor 4 homolog, mitochondrial
Sequence:
MSTAMNFGTKSFQPRPPDKGSFPLDHLGECKSFKEKFMKCLHNNNFENALCRKESKEYLECRMERKLMLQEPLEKLGFGDLTSGKSEAKK
Protein: CG5012 (Q2XYH0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LRQISRQVQLHRMYSAAAPAAAVSGAEKLVPPAPEGAAKPPNPKLDSIVNNIAALNLLEVAELSTLLKQKLNLPETAFAPQFAAGPARAAPAEDEEEAAPKKVQTSFKVKLVKFDEKQKVALIKEVKNLLEGMNLVQAKKFVESAPTIVKEDIPKEEAEKLKEALSKAG
Protein: LD46604p (Myosin phosphatase targeting subunit 75D, isoform A) (Myosin phosphatase targeting subunit 75D, isoform C) (Myosin phosphatase targeting subunit 75D, isoform D) (Q8SY34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase beta isoform
- Myosin regulatory light chain sqh
- Serine/threonine-protein phosphatase alpha-1 isoform
Sequence:
MIKGILIQRKSQEDASYTKQLKMEHADLVAEMQTVESLPTHERLQLARLRRAQQLKLSRQKDKEWAKLQRAKGNTASGGSGTGSLGNGLMNGNGDTTHHFRHANGSGTLSGRRHISFENSVVLLEAASRNDMPEVAALLQHGITPDAANEDGLTAMHQACIDNNVEMLQLLLEYGANVDAQDSDKWTPLHAAATCGHLELVRILIRHGANLLAVNTDGNMPYDLCDDEKTLDFIEGEMAQRGVTQELIDETRSSTERIMLRDLMELARTGGDLEEPDYQCATPLHIAAANGYVRVVEFLLEQHVNVDAMDKDLWTPVHAAACWGHLEVLEMLAQCGADLNVRNKDDETPSDICEDPEIRERIEQLKTEQESKRLAEAQRRRVRRSQSNNTRAQSVRRTSLRDKTLTTKKDAVEETRLRLQAQEATDSEAPSSAGDPLTNGYGYGNNNGEKRPSTGSSNGQPLPHSKSADALDNATAALSANATHSYPSRRPPDGRENDELLRLKAAGAAGEMQRATSAAAVILTEKGTAASAEAVQIQSSKEAANGKINVQVTVLVDTNSTHHHQQHQQQQQQQQQHHHQQHVLLLQQHQQLQQHQQQQQQQQQQQHVALDGYSATLANLKKQRSLSRTANVLNTFELSSQTASNAHPIAAANATTTNGSVLGAGGSSSNNNNNLSTSNNNNNGSAPISTQPTLGHMGAGSVLSDFEGSSPAGSSLNKFSGITGDVVTDSTSSSRRCCVLM
Protein: Stanniocalcin-2 (STC-2) (Stanniocalcin-related protein) (STC-related protein) (STCRP) (O76061)
Organism: Homo sapiens (Human)
Function: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pappalysin-1
- Biorientation of chromosomes in cell division protein 1
- Biorientation of chromosomes in cell division protein 1-like 2
- Sodium-dependent phosphate transport protein 2A
Sequence:
MCAERLGQFMTLALVLATFDPARGTDATNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIRGLHGICMTFLHNAGKFDAQGKSFIKDALKCKAHALRHRFGCISRKCPAIREMVSQLQRECYLKHDLCAAAQENTRVIVEMIHFKDLLLHEPYVDLVNLLLTCGEEVKEAITHSVQVQCEQNWGSLCSILSFCTSAIQKPPTAPPERQPQVDRTKLSRAHHGEAGHHLPEPSSRETGRGAKGERGSKSHPNAHARGRVGGLGAQGPSGSSEWEDEQSEYSDIRR
Protein: Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.19) (Protein glycosylation B) (Q5HTX9)
Organism: Campylobacter jejuni (strain RM1221)
Function: Oligosaccharyltransferase that catalyzes the transfer of a preassembled heptasaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains, affording a beta-linked glycan to the asparagine side chain of target proteins.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:B9KDD4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:B9KDD4}.
Interaction partners:
Sequence:
MLKKEYLKNPYLVLFAMIILAYVFSVLCRFYWIWWASEFNEYFFNNQLMIISNDGYAFAEGARDMIAGFHQPNDLSYYGSSLSTLTYWLYKITPFSFESIILYMSTFLSSLVVIPIILLANEYKRPLMGFVAALLASVANSYYNRTMSGYYDTDMLVIVLPMFILFFMVRMILKKDFFSLIALPLFIGIYLWWYPSSYTLNVALIGLFLIYTLIFHRKEKIFYIAVILSSLTLSNIAWFYQSAIIVILFALFALEQKRLNFMIIGILGSATLIFLILSGGVDPILYQLKFYIFRNDESANLTQGFMYFNVNQTIQEVENVDFSEFMRRISGSEIVFLFSLFGFVWLLRKHKSMIMALPILVLGFLALKGGLRFTIYSVPVMALGFGFLLSEFKAILVKKYSQLTSNVCIVFATILTLAPVFIHIYNYKAPTVFSQNEASLLNQLKNIANREDYVVTWWDYGYPVRYYSDVKTLVDGGKHLGKDNFFPSFALSKDEQAAANMARLSVEYTEKSFYAPQNDILKSDILQAMMKDYNQSNVDLFLASLSKPDFKIDTPKTRDIYLYMPARMSLIFSTVASFSFINLDTGVLDKPFTFSTAYPLDVKNGEIYLSNGVVLSDDFRSFKIGDNVVSVNSIVEINSIKQGEYKITPIDDKAQFYIFYLKDSAIPYAQFILMDKTMFNSAYVQMFFLGNYDKNLFDLVINSRDAKVFKLKI
Protein: LuxR family transcriptional regulator (PhzR) (Quorum-sensing control repressor) (Quorum-sensing transcriptional repressor QscR) (Regulatory protein SdiA) (Q9RMS5)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MHDEREGYLEILSRITTEEEFFSLVLEICGNYGFEFFSFGARAPFPLTAPKYHFLSNYPGEWKSRYISEDYTSIDPIVRHGLLEYTPLIWNGEDFQENRFFWEEALHHGIRHGWSIPVRGKYGLISMLSLVRSSESIAATEILEKESFLLWITSMLQATFGDLLAPRIVPESNVRLTARETEMLKWTAVGKTYGEIGLILSIDQRTVKFHIVNAMRKLNSSNKAEATMKAYAIGLLN
Protein: Platelet glycoprotein V (GPV) (Glycoprotein 5) (CD antigen CD42d) (P40197)
Organism: Homo sapiens (Human)
Function: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein IX
- von Willebrand factor
- Platelet glycoprotein Ib beta chain
- CD151 antigen
- Platelet glycoprotein 4
- Platelet glycoprotein Ib alpha chain
- Platelet glycoprotein VI
- Thioredoxin
- GTP-binding protein 1
- Sialoadhesin
Sequence:
MLRGTLLCAVLGLLRAQPFPCPPACKCVFRDAAQCSGGDVARISALGLPTNLTHILLFGMGRGVLQSQSFSGMTVLQRLMISDSHISAVAPGTFSDLIKLKTLRLSRNKITHLPGALLDKMVLLEQLFLDHNALRGIDQNMFQKLVNLQELALNQNQLDFLPASLFTNLENLKLLDLSGNNLTHLPKGLLGAQAKLERLLLHSNRLVSLDSGLLNSLGALTELQFHRNHIRSIAPGAFDRLPNLSSLTLSRNHLAFLPSALFLHSHNLTLLTLFENPLAELPGVLFGEMGGLQELWLNRTQLRTLPAAAFRNLSRLRYLGVTLSPRLSALPQGAFQGLGELQVLALHSNGLTALPDGLLRGLGKLRQVSLRRNRLRALPRALFRNLSSLESVQLDHNQLETLPGDVFGALPRLTEVLLGHNSWRCDCGLGPFLGWLRQHLGLVGGEEPPRCAGPGAHAGLPLWALPGGDAECPGPRGPPPRPAADSSSEAPVHPALAPNSSEPWVWAQPVTTGKGQDHSPFWGFYFLLLAVQAMITVIIVFAMIKIGQLFRKLIRERALG
Protein: Protein APCDD1 (Adenomatosis polyposis coli down-regulated 1 protein homolog) (Protein primglo) (xPgo) (Q66KI8)
Organism: Xenopus laevis (African clawed frog)
Function: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGIPCFYSSLISCLFSIITLVDVGQSSALTLSDSRLHPQSLEKSPWREFQCQHMLKHLHNGARVTVQMPPNIEGHWVSMGCEVRSGPEFITRSYRFYNNNTFKAYQHYYGNNHCTIPTYTLVIRGKIRLRQASWIIRGGTEADYQLHNVQIIPHSETVAEKLTWLVNHTCAGFVPGDMPWEPGISYDLWREEGGFKCTKALNFAMHELQLIRVEKQYMHHNLDHLVEELFLGDIHTDPSQRMYYRPSSYQPPLQNAKNHNQNCVACRIILRSDEHHPPILPAKADLPVGLNGEWVSQRCEVRPEVLFLTRHFIFNDNNHTWEGFYYHYSDPICKHPSFTIYAKGRYSRGVYSSKVMGGTEFVFKVNHMKVTPMDFATASLLNVFNGDECGAEGSWKVGVEQDVTHTNGCVALGIKLPHTEYELFRMEQDNRGRYLLYNGQRPSDGSSPARPEKRATSYQVPLVQCTSVSLNPEGAHDGQHKSQSRNSAAGHIFLYLFSNLFLLFICTLLHLEILS
Protein: Mitochondrial tRNA methylthiotransferase CDK5RAP1 (EC 2.8.4.3) (CDK5 activator-binding protein C42) (CDK5 regulatory subunit-associated protein 1) (mt-tRNA-2-methylthio-N6-dimethylallyladenosine synthase) (mt-tRNA-N6-(dimethylallyl)adenosine(37) methylthiotransferase) (Q8BTW8)
Organism: Mus musculus (Mouse)
Function: Methylthiotransferase that catalyzes the conversion of N6-(dimethylallyl)adenosine (i(6)A) to 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 (adjacent to the 3'-end of the anticodon) of four mitochondrial DNA-encoded tRNAs (Ser(UCN), Phe, Tyr and Trp). Essential for efficient and highly accurate protein translation by the ribosome. Specifically inhibits CDK5 activation by CDK5R1 (By similarity). Essential for efficient mitochondrial protein synthesis and respiratory chain.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25738458}.
Interaction partners:
- Exosome complex component RRP40
- Exosome complex component RRP46
- tRNA dimethylallyltransferase
- Cyclin-dependent kinase 5
- Mitochondrial tRNA-specific 2-thiouridylase 1
- Transmembrane and coiled-coil domain-containing protein 4
- Pre-mRNA-processing factor 40 homolog B
Sequence:
MHPLRCVLQVQRLSAPFTSMCWVLLRTCRAQSSVSSTPCPSPEAKSSEAQKDFSSRLATGPTFQHFLRSASVPQEKPSSPEVEDPPPYLSGDELLGRQRKVYLETYGCQMNVNDTEIAWSILQKSGYLRTSNLQEADVILLVTCSIREKAEQTIWNRLHQLKVLKTKRPRSRVPLRIGILGCMAERLKGEILNREKMVDLLAGPDAYRDLPRLLAVVESGQQAANVLLSLDETYADIMPVQTSPSATSAFVSIMRGCDNMCSYCIVPFTRGRERSRPVASILDEVRKLSEQGLKEVTLLGQNVNSFRDNSEVQFNNAGSANLSRGFTTNYKPKQGGLRFSHLLDQVSRIDPEMRIRFTSPHPKDFPDEVLQLIRERHNICKQIHLPAQSGSSRVLDAMRRGYSREAYVALVHHVRETIPGVSLSSDFITGFCGETEDDHRQTVSLLREVQYNTGFLFAYSMRQKTRAYHRLKDDVPEEVKLRRLEELITVFREEASKANKTSVGCSQLVLVEGFSKRSTTDLCGRNDANLKVIFPDAEVEDITNPGLKVRAQPGDYVLVKITSASSQTLKGHILCRTTMKDSLTYCTT
Protein: DNA helicase (EC 3.6.4.12) (Q38E36)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM3
- DNA helicase
- Minichromosome maintenance
- DNA replication licensing factor MCM6
- Cell division cycle 45
- Origin recognition complex subunit 1
- DNA polymerase epsilon catalytic subunit
- Protein MCM10 homolog
Sequence:
MQLRSFFVECCEPPQCMTELLSGEALPTRNLWTLDVDCMKLLAACPSVADLLFYHTTTLMDALRKICAEVCAKAGRHLNPSDLSPRLSHLPTVGTPPPSLPPQRGILVSVCGSIVRMNTKKVVPLVRKLKCFKCLETVELTSSPFDRSTKLKPHCANKECKGEELQQIGQVWMDYAECRLQQRHSESGRLPRTLLITLEDDLSKKCTVGQLVEVIGILFPKWRNTYPNALPIIEPTIWALNVNVMDSYRDGGSFNASAAAKRRHNGQVEESAFTPESFYSSFGKDKFGRGSALVNSVCPHLAGLFAPRMAVILATLGGTSTVGKTRMHVRSTIHCLFVGDSSTGKSQLLRCAALLAPRSTSTTGMGSTSAGLTVAASKEQGEWVLEPGALVLSDGGVCVIDELRTVSVGDRASLHEAMEQQTISVAKAGMVTKLRTCCSVISACNPPTRQNGTEIGVGGPLLSRFDFVFLLWDTPSPETDDRIATHILNYSQAGRLPDSVLSLDDVGRYLRWVHAHYSQNGGPLLTDGASRLIKAYYEMQQRRGAVPNLADCVPITIRLLESLVRVTQAYAKLHLERVCTEMDAAFTVFLFEQSAYSLKCPLEVLGPDVYTSSKCLEEYFLDLSPKGVEKQRTILQAITDTFSSCSSTLDSETTLENVPQDLAAGEWLSKLRAPHEKTPSPDRLVGKRSNSDSGTLEAALRSVKRLVAEVRTPREEPQTVICYPADSLSQLSAPPVSLPPARTPNRLRDAKEIMRSLSFNA
Protein: Transcription factor 12 (TCF-12) (DNA-binding protein HTF4) (E-box-binding protein) (Salivary-specific cAMP response element-binding protein alpha) (SCBP-alpha) (Transcription factor HTF-4) (P51514)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis.
Subcellular location: Nucleus.
Interaction partners:
- TAL bHLH transcription factor 1, erythroid differentiation factor
- Achaete-scute homolog 1
- Myogenin
- Rhombotin-2
- RUNX1 partner transcriptional co-repressor 1
- Myoblast determination protein 1
- LIM domain binding 1
- Runt-related transcription factor 1
- Cyclic AMP-responsive element-binding protein 1
- Twist-related protein 1
Sequence:
MNPQQQRMAAIGTDKELSDLLDFSAMFSPPVNSGKTRPTTLGSSQFSGSGMDERGGTTSWGTSGQPSPSYDSSRGFTDSPHYSDHLNDSRLGTHEGLSPTPFMNSNLIGKTSERGSFSLYSRDSGLSGCQSSLLRQDLGLGSPAQLSSSGKPGTPYYSFSATSSRRRPLHDSVALDPLQAKKVRKVPPGLPSSVYAPSPNSDDFNRESPSYPSPKPPTSMFASTFFMQDGTHSSSDLWSSSNGMSQPGFGGILGTSTSHMSQSSSYGSLHSHDRLSYPPHSVSPTDINTSLPPMSSFHRGSTSSSPYVAASHTPPINGSDSILGTRGNAAGSSQTGDALGKALASIYSPDHTSSSFPSNPSTPVGSPSPLTAGTSQWPRAGGQAPSSPSYENSLHSLKNRVEQQLHEHLQDAMSFLKDVCEQSRMEDRLDRLDDAIHVLRNHAVGPSTSLPTSHSDIHSLLGPSHNAPIGNLNSNYGGSSLVTNSRSASMVGTHREDSVSLNGNHSVLSSTVAASNTELNHKTPESFRGGVQNQSGSVVPTEIKTENKEKDENLHEPPSSDDMKSDDESSQKDIKVSSRGRTSSTNEDEDLNPEQKIEREKERRMANNARERLRVRDINEAFKELGRMCQLHLKSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSAASAEPPTTLPGTHPGLSETTNPMGHL
Protein: C2 calcium/lipid-binding region-containing protein (Q55BH2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MDKFKDKLKVQSPSSNKEDIKISYVVKIVKVTGLPKSSYSPLLVSWKRGSKKENSGEVKTIPRDGEGVVDHTINLNATITKTPKGFLEKSIQFTVKEEKLGKKPVSLGSVSVNLAQYAESKTEKTHPFPIQDKSKVVCNLYLSIQSSWLKVNGKSMVKAEGNQKEILQELGKQKISHEGTDYFLQTEQDMSEPDQTDFGHDSDNEDEDHVDFDDDSNDKSNVSTLSRKSSSGSVEKGESSSSSSTTIANGHNRTNSSNSVGSNTTTTTTTTSNYVPPALIKEESEEKDLNAMTADLKIKKYKKQLKTLKSELEKSKSQFSTLSKDRDEKVEEIKRMIDDMENIKDRSKSVGNGVIADYNNQIEQLNSKLTAGNKDIENLKIQLQRERNQSSQDSNQVTVLQNQLLTINSQLDTIRNENTTLNNQIRQLETQLRESSSNKPEELQNALATVQNLHLELNQLRSQLATTTEENRSQFIQLEQERLKSNSTESNVNRVEQEKLNLQQRLEHYERTIHLQLEDFEKEKLKISAELGDLKTKLLNYEKLESELNELKSKQPTIPENNNDNDKELIEARDEILQLKEKLNEKEDSIKSTNDQLIEIKDKLIIKETALIELQDQFEQLKKQDNKELLEARDQIVELKDRLTQKEESFKETENKLEDRAIEISELRDKLAEKESILTDREEQLDQLKQSIENQSSTTPIISDQQELLEARDEIVQLKDKLTAKEDSIKDIDNQLIELKDRLTAKELLFKETEDQLYEKSNEISILQDKISNLEESNNNNNSNNSNSSINELQLKLKEFELNTLDKNQSYEERIEKLELQLKEKQLEVQSLQLEIHNNVKEGDSNDRLLKLEEQYKELQEKFDKVKNKKNTLKVLCSNYKLNIEQLEQKQSTLESSAIANQDGLSDEIDQLKSKLIHQTNENEIIQDENNQLKLQLTSYQDDSISKQNIIKDYQEIISKLEQEKEDLIENNKNNKKNSDNSDGHDDSGDDDDRSAEIEEFKEKIQYQKEKIKALKEDLESKSDEWIDIKIKMEEIIGGKQDEIEKLQQQLQQKESLSSLALPVSKDDNNQSNQILEEEIDQLKSQIKQLQQENLAISSEKQFKVQHLQQELEQLRQVNSASASPRSSIGGGGSGIDNLDDLRKEMEENKNIETSIYWSELDFDRNNIPFCGTNVWAIIDGIGGLGKSQNIRLLNKIVISLEKSFLRSGNDCKFIAYWFSTCCYLLSKCHQAGYTQESANPMKSGIEINVNSFVTPAPEIGGSFIRDLQALNLSIYSKLLSVTEIKLERVLIPSVYLPDSIILEAQKSPIKSSSSSSSTSPLGRTSGSLPFNNTGANSINNLLYILDGIIQFLKEGRIFDSVSNQFLNQIFYFMNAQITNHLLNNPKVCTTTQGLEVKMGVSRLKEWCSATPYKSASQQLDSSLEASNLLVIDKNVFVDIEAIKSIFQKLNLHQIKQLLQSFTPDSLSPDTIPTVLRKALDSNWRQSIDINSLPLLIDQSKKFKI
Protein: Queuine tRNA-ribosyltransferase accessory subunit 2 (Queuine tRNA-ribosyltransferase domain-containing protein 1) (O14096)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosducin-like protein C2A9.09
- Queuine tRNA-ribosyltransferase catalytic subunit
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
Sequence:
MAISSLSSPSGARVSSVTVKNKVLKTPCFFLPTSRGTVPHLTPDNVEEFDIPALYVGLEDCLDRLEASPILTNEGTIKKWIAAPSVQPTLLAPRRTSPLPSVSAGQSHINIVTASGAKKLTNDLYIKAVLKLCPELVIPLNDTPTSPPGVKRKPKIVERSVNWTTELLLALKATDAFNTTKVFFPVPDLDTQYLTPIFQFFQENQLANNIAGLAFSNNVNPLPADLVGLPRLSIQKFESPLEILKCIQRGIDIIVPDMITQATDAGVALTFSFPPPSKDVLNSKIELGLDMWDERFATDMEPLQSGCVCKTCRRYKRAYVRHLLQARELVAWILLQLHNVYAFTAFFQGIRASIQEGNFDEDVRKFEEIYMTSFPASHGFGPRKRGYQMDLTNVQPVENKPAWISMKSPLEKEIANEYEALKVTERKEDTQDYNEPELHNR