wanglab/gogpt-training-data huggingface dataset:
Protein: Zyg eleven-related protein 1 (zyg-11-related protein) (Q2WF59)
Organism: Caenorhabditis elegans
Function: Acts as target recruitment subunit in the E3 ubiquitin ligase complex zer-1-cul-2-elc-1.
Interaction partners:
- Cullin-2
- Elongin-C
- Leucine-Rich Repeat protein
- von Hippel-Lindau tumor suppressor homolog
- RNA polymerase II transcription factor SIII p18 subunit
- RING-box protein 1
- Sex-determining protein fem-1
- Protein zer-1 homolog
- Early embryogenesis protein zyg-11
- TIR domain-containing protein
Sequence:
MSHTADIPLEAPTLLKLASSSVQSQINNDEYMETVILPVPLSQELFARFRNKWNIHNHGPAPVEHLGPPTDEPRPDQGNIDMIKQVFRIWSDSTRLPLEKLNLTGATVDDQIFVDLLHAHAHSITELDLTNVTGVTDLSNAYLYARSTHFPMLTSIRMTSMDLVTGHQPRRKNGIASTEFRALFMLGEEALAEARGQMERDGLRSPLSPSSQPSSIQSDHQSLDALVPCDSPVEPPLITARAPNVKRLFLPRCPAKRTTIDEEEQNTHVILTKILSPLQQLEVLDLSYWSKTDDMRCLQPLSNTLTCLILYDVPDLYHAVPNICHMTELRILDVSQSNRDSGLYPHPVTTLNKLIVSLKYLTHLDISSTNLATQPSSHDNPARYRESVRTDICGLQSLVRPLKYLGLFNCESASHVREIPAEVVSGDANEDQVITSLQMYKDRAGLLQNVLNESYQLYRFGNSNPLTRHTEALHLVLEAMHRHLADSTLQIAGSASLFYIIRKVDMNRDTKRRVVSALLSGMEVHMEEQVMVRNCCLSLCQFEIPQDILFDYSRLAVLLVSVLQHHNADNLTQRIVVFLLNSMACHVEGDQKVQVGSYGAIEMILDQIARKHTANVCDDVMEVGWSFLWNITDETPVNCELFLNANGLDLFQKCYEAFKTERELVRNMMGLIGNIAEVDELRSQLMKDDYVKIFCALLESQEESIEISYNSAGVLAHMVSDGEEVWKQMTVCRNEVMQRIVEATSSWKLATRRFINYRSFRPILRLLPLYHAYASQHWAVWALANLTTTDGEKYCAYVRDEGGVPLLEELVSNAITTTDIRTLANTVLENIRNVENKRNPKSIPADLAHSSNSPTFVPSYVSDVEEEDEGDVEADEEVQDFVNVDFDDYALPMEY
Protein: Uracil phosphoribosyltransferase (EC 2.4.2.9) (UMP pyrophosphorylase) (UPRTase) (P0A8F0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Interaction partners:
- Uridine kinase
- Cytosine deaminase
- Uridylate kinase
- Orotidine 5'-phosphate decarboxylase
- Thymidine phosphorylase
- Uridine phosphorylase
- Uracil permease
- 5'/3'-nucleotidase SurE
- Pyrimidine 5'-nucleotidase YjjG
- Pyrimidine/purine nucleoside phosphorylase
Sequence:
MKIVEVKHPLVKHKLGLMREQDISTKRFRELASEVGSLLTYEATADLETEKVTIEGWNGPVEIDQIKGKKITVVPILRAGLGMMDGVLENVPSARISVVGMYRNEETLEPVPYFQKLVSNIDERMALIVDPMLATGGSVIATIDLLKKAGCSSIKVLVLVAAPEGIAALEKAHPDVELYTASIDQGLNEHGYIIPGLGDAGDKIFGTK
Protein: mannose-6-phosphate isomerase (EC 5.3.1.8) (O05898)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable phosphomannomutase PmmA
- Conserved protein
- Probable phosphomannomutase PmmB
- Glutamine--fructose-6-phosphate aminotransferase
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase isozyme 2
- ATP-dependent 6-phosphofructokinase
- Fructose-1,6-bisphosphatase class 2
- Mannose-1-phosphate guanylyltransferase
Sequence:
MELLRGALRTYAWGSRTAIAEFTGRPVPAAHPEAELWFGAHPGDPAWLQTPHGQTSLLEALVADPEGQLGSASRARFGDVLPFLVKVLAADEPLSLQAHPSAEQAVEGYLREERMGIPVSSPVRNYRDTSHKPELLVALQPFEALAGFREAARTTELLRALAVSDLDPFIDLLSEGSDADGLRALFTTWITAPQPDIDVLVPAVLDGAIQYVSSGATEFGAEAKTVLELGERYPGDAGVLAALLLNRISLAPGEAIFLPAGNLHAYVRGFGVEVMANSDNVLRGGLTPKHVDVPELLRVLDFAPTPKARLRPPIRREGLGLVFETPTDEFAATLLVLDGDHLGHEVDASSGHDGPQILLCTEGSATVHGKCGSLTLQRGTAAWVAADDGPIRLTAGQPAKLFRATVGL
Protein: Mitochondrial nicotinamide adenine dinucleotide transporter SLC25A52 (Mitochondrial NAD(+) transporter SLC25A52) (Mitochondrial carrier triple repeat protein 2) (Solute carrier family 25 member 52) (Q3SY17)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane carrier protein that mediates the import of NAD(+) into mitochondria. Compared to SLC25A51, SLC25A52-mediated transport is not essential for the import of NAD(+) in mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:32906142}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIDSEAHEKRPPILTSSKQDISPHITNVGEMKHYLCGCCAAFNNVAITYPIQKVLFRQQLYGIKTRDAVLQLRRDGFRNLYRGILPPLMQKTTTLALMFGLYEDLSCLLRKHVRAPEFATHGVAAVLAGTAEAIFTPLERVQTLLQNHKHHDKFTNTYQAFKALKCHGIGEYYRGLVPILFRNGLSNVLFFGLRGPIKEHLPTATTHSAHLVNDFIGGGLLGAMLGFLCFPINVVKTRLQSQIGGEFQSFPKVFQKIWLERDRKLINLFRGAHLNYHRSLISWGIINATYEFLLKFI
Protein: Uncharacterized RNA-binding protein C644.16 (Q9P6P7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA 3'-end-processing protein rna14
- Uncharacterized protein C4G9.04c
- Poly
- Polyadenylate-binding protein 2
- Endoribonuclease ysh1
- Cleavage factor two protein 2
- Uncharacterized RNA-binding protein C660.15
- mRNA 3'-end-processing protein yth1
- Protein cft1
- mRNA cleavage and polyadenylation factor clp1
Sequence:
MNPSCVVYVGNIPYEMAEEQVIDIFKQSGPVKSFQLVIDPESGQPKGYGFCEYHDPATAASAVRNLNNYDAGTRRLRVDFPTADQIRRLDKLLGPSRYGYYPQSYANQSYTYGNNFGSYPPTQPSTQPLPQSYGYPSYPPAGYRGGSARPSGVLANDEVYRVLAQLAPNEIDYMLSAIKALCLEAPEQAAQLFETNPQLSYAVFQAMLMKRYTSESVVADLLIPAGVNLPGAQEPNRGYFSPMHTYSSAVPGPISVPSAPYGRASSTIAEVSPMYGSHAAPYASTPSAAVGSSRGSTPASATVPISPARGFPTTSAYNPAPPAYGMANPAYGSTGIRSSSIPSSGSIRSPSLTTTSAQATTNATNNITTTTAAQDENATKAALIAQLMALTDDQINVLPPDQKERILQIRQALPSSYKTESK
Protein: Auxin-responsive GH3 family protein (T26J12.7 protein) (O49301)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Two-component response regulator ARR16
- Serine/threonine-protein kinase SRK2F
- Two-component response regulator ARR17
- Serine/threonine-protein kinase SRK2J
- Probable inactive receptor-like kinase BSK12
- Serine/threonine-protein kinase SRK2H
Sequence:
MSLTSDLSEKSSDKMKVLEDLTSNVTQIQDNVLEEILTLNANTNYLQKFFLGSFDKESFKKNVPVVTYEDVKPYIERVVNGEPSNVISARPITGFVLSTGTSGGAQKMMPWNEKYLDNLTFMYDLRMHIISNNVKDVEKGKAMMFYFTKLESITPSGLPARVASSSYLKSNYFKNRPSNWYYSYTSPDEVTLCPDNKQNLYCHLLCGLVQRNEVTRMGSIFASVMVRAIKFLEDSWEELCSNIRSGQLSEWITDIGCRDSVSLVLGGPHPEAADTIEQICNQKCWKGIITRLWPKAKYIETIVTGSMVQYVPTLNYYSNNMLPLISTIYASSETQFGLNLNPMCKPEDVSYTFMPNVSYFEFIPVDGDKNDVVDLADVKLGCCYEAVVTNFSGLYRIRVGDILVVTGFHNKAPQFRFIRRDNVVLSIDLDKTNEDDLFKAVNNAKLTLDSSHLMLIDFTSYADISTIPGHYVVYWEVKNKNEDKKSKKHIELKEETFSECCLLMEDSLDSVYKICRFKEESVGPLEIKVVRQGTFDSLMDYFISQGASIGQYKTPRCIKSGKALEVLEENVVATFFST
Protein: Transcription factor SOX-30 (Q8CGW4)
Organism: Mus musculus (Mouse)
Function: Acts as both a transcriptional activator and repressor. Binds to the DNA sequence 5'-ACAAT-3' and shows a preference for guanine residues surrounding this core motif. Binds to its own promoter and activates its own transcription. Required to activate the expression of postmeiotic genes involved in spermiogenesis. Binds to the promoter region of CTNNB1 and represses its transcription which leads to inhibition of Wnt signaling. Also inhibits Wnt signaling by binding to the CTNNB1 protein, preventing interaction of CTNNB1 with TCF7L2/TCF4 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:29848638, ECO:0000269|PubMed:29866902}. Cytoplasm {ECO:0000250|UniProtKB:O94993}. Note=Enriched at the chromocenter. {ECO:0000269|PubMed:29848638}.
Interaction partners:
Sequence:
MERARPEPPPPPPPPPRQPPRPTPPRPLRPAPPAQPVEAATFRAAAAERSQSPSAQATAAMAAVASSCGEAAAAGAQAAGTRRLLQVKPEQVLLLPPGGPGVPPAPDEGAAAAAAAAAAAASSAQARLLQLRPELLLLPPQSAADGGPCRPELHPMQPRTLLVKAEKQELGAGLDLSVGSRRTTEAGPRASRAAKLDGTGKALDGRRSDEKKAKLEAEEAPRDALKGGEGKSLLAIGEGVIKTEEPDRPRDDCRLGTEATSNGLVHSSKEAILAQPPSAFGPHQQDLRFPLTLHTVPPGARIQFQGPPPSELIRLSKVPLTPVPIKMQSLLEPSVKIETKDVPLTVLPSDAGIPDTPFSKDRNGHVKRPMNAFMVWARIHRPALAKANPAANNAEISVQLGLEWNKLSEEQKKPYYDEAQKIKEKHREEFPGWVYQPRPGKRKRFPLSVSNVFSGTTQNIISTNPTTIYPYRSPTYSVVIPGLQNTITHPVGEAPPAIQLPTPAVQRPSPITLFQPSVSSTGPVAVPPPSLTPRPSLPPQRFSGPSQTDIHRLPSGSSRSVKRSTPGSLESTTRIPAGASTAHARFATSPIQPPKEYASVSTCPRSTPIPPATPIPHSHVYQPPPLGHPATLFGTPPRFSFHHPYFLPGPHYFPSSTCPYSRPPFGYGNFPSSMPECLGYYEDRYQKHEAIFSALNRDYPFRDYPDEHTHSEDSRSCESMDGPPYYSSHGHGGEEYLNAMPTLDIGALENVFTAPASAPSGVQQVNVTDSDEEEEEKVLRNL
Protein: Tubulin polymerization-promoting protein family member 3 (Q9CRB6)
Organism: Mus musculus (Mouse)
Function: Regulator of microtubule dynamic that has microtubule bundling activity (By similarity). Required for embryo implantation; possibly by regulating beta-catenin. Also required for decidualization via regulation of beta-catenin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BW30}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BW30}.
Interaction partners:
Sequence:
MAASTDIAGLEESFRKFAIHGDPKASGQEMNGKNWAKLCKDCKVADGKAVTGTDVDIVFSKVKAKSARVINYEEFKKALEELATKRFKGKSKEEAFDAICQLIAGKEPANIGVTKAKTGGAVDRLTDTSKYTGSHKERFDESGKGKGIAGRQDILDDSGYVSAYKNAGTYDAKVKK
Protein: Prefoldin chaperone subunit family protein (F4K498)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Outer envelope membrane protein 7
Sequence:
MAKKKVSRNSNGASNEQQQIQNQSVPVTSQKSTKLSRESSMEDHDSSEEKFQNLKSLNAILLKQTMEKRQQIESLFQAKDSLEIELVRSGKEKTLLREELCGSSDENFMLKIEMDLLMGFVEGRVKEMGVEVDWLFKEKSDRETEIRDLKREANGLIRKLESEREEFSRVCDERDLVKSGFDLQSEEMNLLKESVVRLEMREVSLGEEVGRLKCENGRLVKERKKREEVIERGNRERSELVESLEEKVREIDVLKREIEGVVKEKMEVEMVRRDQREMIVELEKKLGDMNEIVESLTKEREGLRGQVVGLEKSLDEVTEEAKARAEQINELVKEKTVKESELEGLMVENNSIKKEIEMAMVQFSDKEKLVEQLLREKNELVQRVVNQEAEIVELSKLAGEQKHAVAQLRKDYNDQIKNGEKLNCNVSQLKDALALVEVERDNAGKALDEEKRNMVALKEKVVALEKTNEATGKELEKIKAERGRLIKEKKELENRSESLRNEKAILQKDIVELKRATGVLKTELESAGTNAKQSLTMLKSVSSLVCGIENKKDEKKRGKGMDSYSVQLEAIKKAFKNKESMVEEMKKELAKMKHSVEDAHKKKSFWTLVSSVTSLLMAASVAYAASLK
Protein: Bacterial microcompartment shell protein PduU (Bacterial microcompartment protein homohexamer) (BMC-H) (Propanediol utilization protein PduU) (P0A1D1)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2. Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, may selectively transport specific metabolites. Proteins such as this one with circularly permuted BMC domains may play a key role in conferring heterogeneity and flexibility in this BMC (Probable).
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:27063436}. Note=The N- and C-terminii are on the convex side of the hexamer, probably inside the BMC (Probable) (PubMed:18786396). Modeling suggests the beta-barrel is on the exterior of the BMC where it interacts with PduV (Probable). {ECO:0000269|PubMed:18786396, ECO:0000305, ECO:0000305|PubMed:25646976}.
Interaction partners:
- Bacterial microcompartment shell protein PduT
- Bacterial microcompartment shell protein PduK
- Bacterial microcompartment shell vertex protein PduN
- Propanediol utilization protein PduV
- Bacterial microcompartment shell protein PduB
- Bacterial microcompartment shell protein PduJ
- Bacterial microcompartment shell protein PduA
- Bacterial microcompartment assembly protein PduM
- Propanediol dehydratase large subunit
- Propanal dehydrogenase
Sequence:
MERQPTTDRMIQEYVPGKQVTLAHLIANPGKDLFKKLGLQDAVSAIGILTITPSEASIIACDIATKSGAVEIGFLDRFTGAVVLTGDVSAVEYALKQVTRTLGEMMQFTTCSITRT
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQ78)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Protein kinase C-like 1
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MSQQVGASIRRKLVIVGDGACGKTCLLIVFSKGQFPEVYVPTVFENYVADVEVDGRRVELALWDTAGQEDYDRLRPLSYPDSNVVLICFSIDLPDSLENVQEKWIAEVLHFCQGVPIILVGCKVDLRNDPQTLEQLRAEGLQPVATADGQNVADQIGATGYYECSAKTGYGVREVFEAATRASLMGKQKNTGKKNKKNSGEKKKRKCVLL
Protein: ABC transporter G family member 40 (ABC transporter ABCG.40) (AtABCG40) (Pleiotropic drug resistance protein 12) (Q9M9E1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity abscisic acid (ABA) transporter that mediates the import of ABA, with a preference for (+)-ABA, through the plasma membrane, especially in guard cells, and is involved in the intercellular and intracellular ABA signaling pathways leading, for example, to stomatal closure, thus conferring drought tolerance. Together with ABCG30, import into the embryo the ABA delivered from the endosperm via ABCG25 and ABCG31-mediated export to suppress radicle extension and subsequent embryonic growth. May be a general defense protein (By similarity). Functions as a pump to exclude Pb(2+) ions and/or Pb(2+)-containing toxic compounds from the cytoplasm. Contributes to Pb(2+) ions resistance. Confers some resistance to the terpene sclareol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15923333, ECO:0000269|PubMed:20133880}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 50
- Protein NRT1/ PTR FAMILY 4.6
- ABC transporter C family member 2
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- ABC transporter C family member 1
- Protein LEAD-SENSITIVE 1
- Feruloyl CoA ortho-hydroxylase 1
Sequence:
MEGTSFHQASNSMRRNSSVWKKDSGREIFSRSSREEDDEEALRWAALEKLPTFDRLRKGILTASHAGGPINEIDIQKLGFQDTKKLLERLIKVGDDEHEKLLWKLKKRIDRVGIDLPTIEVRFDHLKVEAEVHVGGRALPTFVNFISNFADKFLNTLHLVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIGEMTVRETFAYAARFQGVGSRYDMLTELARREKEANIKPDPDIDIFMKAMSTAGEKTNVMTDYILKILGLEVCADTMVGDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPAPETFNLFDDIILIAEGEIIYEGPRDHVVEFFETMGFKCPPRKGVADFLQEVTSKKDQMQYWARRDEPYRFIRVREFAEAFQSFHVGRRIGDELALPFDKTKSHPAALTTKKYGVGIKELVKTSFSREYLLMKRNSFVYYFKFGQLLVMAFLTMTLFFRTEMQKKTEVDGSLYTGALFFILMMLMFNGMSELSMTIAKLPVFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDPNVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAILANEFFGHSWSRAVENSSETLGVTFLKSRGFLPHAYWYWIGTGALLGFVVLFNFGFTLALTFLNSLGKPQAVIAEEPASDETELQSARSEGVVEAGANKKRGMVLPFEPHSITFDNVVYSVDMPQEMIEQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEIYVGPLGHESTHLINYFESIQGINKITEGYNPATWMLEVSTTSQEAALGVDFAQVYKNSELYKRNKELIKELSQPAPGSKDLYFPTQYSQSFLTQCMASLWKQHWSYWRNPPYTAVRFLFTIGIALMFGTMFWDLGGKTKTRQDLSNAMGSMYTAVLFLGLQNAASVQPVVNVERTVFYREQAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIASVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIASQFGDITEPMADSNMSVKQFIREFYGYREGFLGVVAAMNVIFPLLFAVIFAIGIKSFNFQKR
Protein: Klra18 protein (Q2M2N3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MTEQKDTFSAVRFHKSSGLQNEMRLKETRKPRKAGLRVCSVPWQFIVIALGILISLRLVIVAVLMTNIFQYGQQKHELQEFLKHHNNCSIMQSDINLKDELLKNKSIECNLLESINRDQNRLYNKTKTVLDSLQHTGRGVKVYWFCYGMKCYYFIMDRKPWSRCKQSCQNSSLTLLKIDNEDELFLQLVVPSDSCWIGLSYDNKKKDWAWIDNRPSKLALNTTKYNIRDGGCMFLSKTRLDNNYCDQSFICICGKRLDKFPH
Protein: MutL homolog 3 (Q68FG1)
Organism: Mus musculus (Mouse)
Interaction partners:
- DNA mismatch repair protein Mlh1
- DNA mismatch repair protein Msh2
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein Msh3
- Mismatch repair endonuclease PMS2
- DNA ligase 4
- DNA repair protein XRCC4
- TP53-binding protein 1
- MutS protein homolog 4
- E3 ubiquitin-protein ligase RNF168
Sequence:
MIRCLSDDVKTKLRSGLAISSLGQCVEELTLNSIDAEATCVAIRVNMETFQVQVIDNGLGMAGDDVEKVGNRYFTSKCHSVRDLENPAFYGFRGEALASIADMAGAVEISSKKNTTLKTFVKMFQNGKALATHEADLTRPSVGTTVTVYNLFYQFPVRRKSMDPRLEFEKVRQRVEALSLMHPSISFSLRNDVSGSMVLQLPKTKDICSRFCQIYGLGKSQKLREIRFKYKEFEFSGYISSEAHYNKNMQFLFVNRRLVLRTKLHKLIDFLLRKESIICRPKNGSASRQMNSSPRHRSASELHGIYVINVQCPFCEYDVCIEPAKTLIEFQSWDTVLICIQEGVKRFLKQEKLFVELSGEDIKEFNEDNGFSLFGTTLQTHVSTHEKCDQSSFREACNKILDSYEMFNLQSKAVKRIATLENKTRQNPGDSETIRKKTVGSLYTDASDGPCYSKSVESVLQDSNNSAYLEPRVSEEEVAKTSHSGENEKWKKSFLENKTSGRIHETSPKMFSSPIQMHHLLEEREADLEMQTISSTVNVMAANIPQNNDIPSQLEKWKDAPEVGCQPLPFETTLLRVRGTQRKKERRKKEPSSRGRVNVFSYGQVKLCSTGFITHVVQSEHAKSTETEHSFKNYARPGPVSAQETFGKRTHHAIETPDSSDLTSTLSKESSQPPNKRFCRTNTGYGTENKPVATDDNLALFQESCKESHTDRLLPDASSFPWCRYVSDGCRKIDKRGSFKQVVRRKLSLRSQVGSLEKFKRQYGKVSSSLDTEKDNNTEVRTHLDPQNEPDVLLKDKSHLDMSDGCEITTVEHSETCQPLSPILYPEKILFSKEDRLEQMPHLRESPITLEELSHCNRKADVEKSAASLASKLSKLKDSEKEMQTVGMTGHTSELPDSNPSWKDNSQCTRLDLDFCELLKNKLEKIESDMLPMADSATEDGPINKNSELHPNNTTDDTEKPETPLLFPCNDSKISRDSDVLIRTSEQPTGNPDSVGKVIMSQVEDGIGSQGGVCPQGDESKARSCSKNEPNAHCMDWQQHFDVTLGRMVYINRMTGLSTFVAPTDDLHTACTKDLTTVAVDVLLGNDAVDAAAAAVSEPLQSLFSEWSNPVFARYPEVAVDVSSGQAESLAVKIHNVLYPYRFTKEMIHSVKVLQQVDNKFIACLMSTRMDEDGRTGGNLLVLVDQHAAHERIRLEQLITDSYEKQDPQSAGRKKLLSSTIIPPLAITVSEEQRRLLRSYHKHLEDLGLELLFPDASDSLILVGKVPLCFVEREASELRRGRSTVTKSIVEELIREQVELLQTTGGIQGTLPLTVQKVLASQACHGAIKFNDRLSLEESCRLIEALSLSQLPFQCAHGRPSMLPLADLDHLEQEKQVKPNLAKLRKMVRAWHLFGKTEQNLQQPIRPCEPP
Protein: CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) (O51522)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Interaction partners:
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL13
- Nucleoside diphosphate kinase
- UvrABC system protein A
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
Sequence:
MKKNLKILVITGGVISGIGKGVTSASIARLFRYDFRVTPIKCDGYLNTDPGTINPVEHGEVFVLDDGGEVDMDFGHYERFLNLNAKSSWNITMGKIYKKILENERKGKYLGRTVQLIPHVTDEIKSTIFQIASSENSDMLIIEIGGTVGDMENILFIETVRQIRQEIGSGNISFIHLTYVPSPAGINEQKSKPTQQSVKTLNKAGIFPDLIIARSSQVLTDQIRKKVAMFCNVESTSIIDNVDVSTIYEIPISFYKQGVHEILSSKLNIKVDPKIEELSKLVGVIKSNFFVPKKIINIAICGKYAELDDSYASIRESLVHVAAHLDLLIKSTLIDSNDLNESCLKEFDGIIVPGGFGGKGYEGKIMAIKYARENNIPFLGICLGLQLAVIEFARNVCGILDADTEENLARDKPLKSPVIHLLPEQKGIKDKGATMRLGGYPVILKKNTIAFKLYGQDRIIERFRHRYEVNNDYIDLFAKNGLIVSGFSSDFKMAKLIEIPENKFFVACQFHPELITRIENPAKLFLGLIKACI
Protein: Beta-1,4-galactosyltransferase (Beta-1,4-GalTase) (EC 2.4.1.-) (A0A384NY44)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU368121}. Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}.
Interaction partners:
Sequence:
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
Protein: Tyrosine-protein kinase Fer (EC 2.7.10.2) (Proto-oncogene c-Fer) (p94-Fer) (P70451)
Organism: Mus musculus (Mouse)
Function: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus. Cytoplasm, cell cortex {ECO:0000250}. Note=Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts (By similarity). Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (PubMed:11339827). {ECO:0000250, ECO:0000269|PubMed:11339827}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus.
Interaction partners:
- Catenin beta-1
- Catenin delta-1
- Tyrosine-protein kinase Yes
Sequence:
MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKESTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDDYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQQMLLHKEAAVLELEKRIEESFETCEKKSDIVLLLGQKQALEELKQSVQQLRCTEAKCAAQKALLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIKSPKSVLGSSTQVCDVISVGERPLAEHDWYHGAIPRIEAQELLKQQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDHHFNTKQVITKKSGVVLLNPIPKDKKWVLNHEDVSLGELLGKGNFGEVYKGTLKDKTPVAIKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVPGGDFLTFLRKRKDELKLKQLVRFSLDVAAGMLYLESKNCIHRDLAARNCLVGENNTLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQNCPEEVFTIMMKCWDYKPENRPKFNDLHKELTVIKKMIT
Protein: Gap junction protein (Q503F4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Phosphoinositide phospholipase C.
- PI-PLC X domain-containing protein 1
- PI-PLC X domain-containing protein 1
- Phosphatidylinositol-specific phospholipase C, X domain-containing 2.
Sequence:
MSWGALYAQLGGVNKHSTSLGKIWLSVLFIFRICILVIAAETVWGDEQSDFTCNTQQPGCKNVCYDHFFPVSHIRFWCLQLIFVSTPALLVAMHVAYRKRNMKKKSILAKRGGNGKGDDLESLKNRRLPITGPLWWTYTSSLFFRLLFEAGFMYALYYVYDGFQMARLVKCEQWPCPNKVDCFISRPTEKTVFTIFMVGSSAICIVLNVAELAYLIVKALLRCSARAKGRRSFVHQEKMSTEKAHLQNEKNARLLSSASDSSSNKTV
Protein: Nuclear receptor 2C2-associated protein (TR4 orphan receptor-associated 16 kDa protein) (Q86WQ0)
Organism: Homo sapiens (Human)
Function: May act as a repressor of NR2C2-mediated transactivation by suppressing the binding between NR2C2/TR4 and the TR4-response element in target genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:12486131}.
Interaction partners:
- Nuclear receptor subfamily 2 group C member 2
Sequence:
MTHSLVCPETVSRVSSVLNRNTRQFGKKHLFDQDEETCWNSDQGPSQWVTLEFPQLIRVSQLQIQFQGGFSSRRGCLEGSQGTQALHKIVDFYPEDNNSLQTFPIPAAEVDRLKVTFEDATDFFGRVVIYHLRVLGEKV