wanglab/gogpt-training-data huggingface dataset:
Protein: Gonadotropin-releasing hormone receptor (GnRH receptor) (GnRH-R) (P30968)
Organism: Homo sapiens (Human)
Function: Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol-calcium second messenger system. Isoform 2 may act as an inhibitor of GnRH-R signaling.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Progonadoliberin-1
- Progonadoliberin-2
- Guanine nucleotide-binding protein G
- KiSS-1 receptor
- Metastasis-suppressor KiSS-1
- Guanine nucleotide-binding protein G
- Follitropin subunit beta
- Guanine nucleotide-binding protein subunit alpha-11
- Tachykinin-3
- Anosmin-1
Sequence:
MANSASPEQNQNHCSAINNSIPLMQGNLPTLTLSGKIRVTVTFFLFLLSATFNASFLLKLQKWTQKKEKGKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGELLCKVLSYLKLFSMYAPAFMMVVISLDRSLAITRPLALKSNSKVGQSMVGLAWILSSVFAGPQLYIFRMIHLADSSGQTKVFSQCVTHCSFSQWWHQAFYNFFTFSCLFIIPLFIMLICNAKIIFTLTRVLHQDPHELQLNQSKNNIPRARLKTLKMTVAFATSFTVCWTPYYVLGIWYWFDPEMLNRLSDPVNHFFFLFAFLNPCFDPLIYGYFSL
Protein: LD29223p (PAR-6) (Par-6, isoform B) (O97111)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cdc42 homolog
- Bazooka, isoform B
- Atypical protein kinase C
- Protein crumbs
- Patj homolog
- Lethal
- Protein PALS1
- Protein lin-7 homolog
- Inscuteable
- Ras-related protein Rac1
Sequence:
MSKNKINTTSATAASDTNLIEVKSKFDAEFRRWSFKRNEAEQSFDKFASLIEQLHKLTNIQFLILYIDPRDNDLLPINNDDNFGRALKTARPLLRVIVQRKDDLNEYSGFGTMKPRNLIGSILMGHTPVKTKAPSISIPHDFRQVSAIIDVDIVPETHRRVRLLKHGSDKPLGFYIRDGTSVRVTASGLEKQPGIFISRLVPGGLAESTGLLAVNDEVIEVNGIEVAGKTLDQVTDMMVANSSNLIITVKPANQRTLTSTHRGSFSRNSQLSSGSHHTNNTNTSDEIEHDDQDDIVDLTGVTLDESPTSTSAGNHNHQPPLSSSPSSHHQQAASNASTIMASDVKDGVLHL
Protein: RNA pseudouridine synthase 3, mitochondrial (EC 5.4.99.-) (RNA pseudouridylate synthase 3) (RNA-uridine isomerase 3) (Q5XET6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Protein Iojap-related
- Pseudouridine synthase family protein
- At4g38020 family protein)
- Short integuments 2, mitochondrial
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein mL43
Sequence:
MWKAKTCFRQIYLTVLIRRYSRVAPPPSSVIRVTNNVAHLGPPKQGPLPRQLISLPPFPGHPLPGKNAGADGDDGDSGGHVTAISWVKYYFEEIYDKAIQTHFTKGLVQMEFRGRRDASREKEDGAIPMRKIKHNEVMQIGDKIWLPVSIAEMRISKRYDTIPSGTLYPNADEIAYLQRLVRFKDSAIIVLNKPPKLPVKGNVPIHNSMDALAAAALSFGNDEGPRLVHRLDRETSGLLVMGRTKESIDYLHSVFSDYKGRNSSCKAWNKACEAMYQQYWALVIGSPKEKEGLISAPLSKVLLDDGKTDRVVLAQGSGFEASQDAITEYKVLGPKINGCSWVELRPITSRKHQLRVHCAEALGTPIVGDYKYGWFVHKRWKQMPQVDIEPTTGKPYKLRRPEGLDVQKGSVLSKVPLLHLHCREMVLPNIAKFLHVMNQQETEPLHTGIIDKPDLLRFVASMPSHMKISWNLMSSYLV
Protein: Thiamine pyrophosphokinase (TPK) (Thiamine kinase) (EC 2.7.6.2) (P35202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential protein, it is the only enzyme in yeast capable of synthesizing thiamine pyrophosphate (TPP).
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Constitutive acid phosphatase
- Repressible acid phosphatase
- Acid phosphatase PHO12
- Acid phosphatase PHO11
- Adenylate kinase
- GTP:AMP phosphotransferase, mitochondrial
- Probable acid phosphatase DIA3
Sequence:
MSEECIENPERIKIGTDLINIRNKMNLKELIHPNEDENSTLLILNQKIDIPRPLFYKIWKLHDLKVCADGAANRLYDYLDDDETLRIKYLPNYIIGDLDSLSEKVYKYYRKNKVTIIKQTTQYSTDFTKCVNLISLHFNSPEFRSLISNKDNLQSNHGIELEKGIHTLYNTMTESLVFSKVTPISLLALGGIGGRFDQTVHSITQLYTLSENASYFKLCYMTPTDLIFLIKKNGTLIEYDPQFRNTCIGNCGLLPIGEATLVKETRGLKWDVKNWPTSVVTGRVSSSNRFVGDNCCFIDTKDDIILNVEIFVDKLIDFL
Protein: Probable periplasmic serine endoprotease DegP-like (EC 3.4.21.107) (Protease Do) (Q57155)
Organism: Pseudomonas aeruginosa
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
Sequence:
MHTLKRCMAAMVALLALSLAMTARAELPDFTPLVEQASPAVVNISTRQKLPDRAMARGQLSIPDLEGLPPMFRDFLERSIPQVPRNPRGQQREAQSLGSGFIISNDGYILTNNHVVADADEILVRLSDRSEHKAKLIGADPRSDVAVLKIEAKNLPTLKLGDSNKLKVGEWVLAIGSPFGFDHSVTAGIVSAKGRSLPNESYVPFIQTDVAINPGNSGGPLLNLQGEVVGINSQIFTRSGGFMGLSFAIPIDVALNVADQLKKAGKVSRGWLGVVIQEVNKDLAESFGLDKPSGALVAQLVEDGPAAKGGLQVGDVILSLNGQSINESADLPHLVGNMKPGDKINLDVIRNGQRKSLSMAVGSLPDDDEEIASMGAPGAERSSNRLGVTVADLTAEQRKSLDIQGGVVIKEVQDGPAAVIGLRPGDVITHLDNKAVTSTKVFADVAKALPKNRSVSMRVLRQGRASFITFKLAE
Protein: Aminotransferase ALD1, chloroplastic (EC 2.6.1.-) (AGD2-like defense response protein 1) (Q9ZQI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aminotransferase involved in local and systemic acquired resistance (SAR) to the bacterial pathogen P.syringae. Required for salicylic acid (SA) and camalexin accumulation upon pathogen infection. Possesses aminotransferase activity in vitro and may generate amino-acid-derived defense signals in vivo. May be involved in ethylene-induced senescence signaling. Involved in the biosynthesis of pipecolate (Pip), a metabolite that orchestrates defense amplification, positive regulation of SA biosynthesis, and priming to guarantee effective local resistance induction and the establishment of SAR. Converts lysine to alpha-keto-epsilon-aminocaproate, which then can spontaneously cyclize to form delta-(1)-piperideine-2-carboxylate (P2C). P2C is converted to Pip by SARD4. May produce non-Pip metabolites that play roles in immunity. Involved in the synthesis of distinct metabolite signals that affect basal and early defenses, and later defense responses.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25372120}.
Interaction partners:
- Diaminopimelate epimerase, chloroplastic
- Probable flavin-containing monooxygenase 1
- Protein SAR DEFICIENT 4
- 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic
- Proline iminopeptidase
- Lipase-like PAD4
- Isochorismate synthase 1, chloroplastic
- LL-diaminopimelate aminotransferase, chloroplastic
- 4-substituted benzoates-glutamate ligase GH3.12
Sequence:
MVSLMFFSSASPLCSSPSKIPKASLDFEMKKLGGSTKLVRNVNLEKLKNNYLFPEINRRELEHIEKHPNVQLISLGTGDTTEPIPEQITSHMSNFAHGLSTVEGYRGYGLEQGNKTLRKAIAETFYRDLHVKSNEVFVSDGAQSDISRLQLLLGSNVTIAVQDPTFPAYIDSSVIIGQTGHFHEKTKKYQNVVYMPCGPNNSFFPDLAMTPRTDVIFFCSPNNPTGYVASRKQLHQLVDFAKTNGSIIIFDSAYAAFIEDGSPRSIYEIPGAREVAIEVSSFSKFAGFTGVRLGWSIIPDELLYSNGFPIINDFHRIVTTSFNGASNIAQAGGLACLSSGGLKEIRSVNNYYKENRKILMDTLVSLGLKVYGGVNAPYLWVHFKGSKSWDVFNEILENTHIITVPGSGFGPGGEEYLRISGFGRRDHIVEASKRLQNFFNTRTKHFTYLSSTSNTN
Protein: Ras-related protein RABC2a (AtRABC2a) (Ras-related protein Rab18B) (AtRab18B) (O49841)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:18703495}. Note=Colocalizes with peroxisome.
Interaction partners:
- Myosin-6
- Geranylgeranyl transferase type-2 subunit beta 1
- At3g14910
- Myosin-17
- Rab escort protein 1
- Rab3 GTPase-activating protein catalytic subunit
- Rab3 GTPase-activating protein catalytic subunit
- Myosin-13
Sequence:
MGSSSGQSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRGAQGIILVYDVTRRETFTNLVDVWGKEIELYSTNQECVRMLVGNKVDRESERGVSREEGIALAKELNCMFLECSARTRQNVEQCFEELALKIMEVPSLLEEGSSAVKRNILKQKPEHQTNTQSGCCS
Protein: Protein BREVIS RADIX (AtBRX) (Q17TI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulator of cell proliferation and elongation in the root and shoot. Regulates roots architecture and primary root protophloem differentiation. BRX, BAM3, and CLE45 act together to regulate the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem. Probable transcription regulator. Regulated by the auxin response factor ARF5. Polarly localized in vascular cells and subject to endocytic recycling. Required for CPD expression and for correct nuclear auxin response. Mediates cross-talk between the auxin and brassinosteroid pathways. BRX is a target for auxin-induced, proteasome-mediated degradation.
Subcellular location: Nucleus. Cell membrane {ECO:0000269|PubMed:28652362}; Peripheral membrane protein; Cytoplasmic side. Note=The translocation to the nucleus depends on the auxin concentration. Polar localization at the plasma membrane, rootward oriented, in developing root protophloem cells (PubMed:28652362). {ECO:0000269|PubMed:28652362}.
Interaction partners:
- CLAVATA3/ESR
- Auxin response factor 5
- Serine/threonine-protein kinase D6PK
- Protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE
- Type IV inositol polyphosphate 5-phosphatase 6
- Membrane-associated kinase regulator 5
- CLAVATA3/ESR
- Type IV inositol polyphosphate 5-phosphatase 7
- Shaggy-related protein kinase eta
- Protein NEN2
Sequence:
MFSCIACTKADGGEEVEHGARGGTTPNTKEAVKSLTIQIKDMALKFSGAYKQCKPCTGSSSSPLKKGHRSFPDYDNASEGVPYPFMGGSAGSTPAWDFTNSSHHPAGRLESKFTSIYGNDRESISAQSCDVVLDDDGPKEWMAQVEPGVHITFASLPTGGNDLKRIRFSREMFDKWQAQRWWGENYDKIVELYNVQRFNRQALQTPARSDDQSQRDSTYSKMDSARESKDWTPRHNFRPPGSVPHHFYGGSSNYGPGSYHGGPPMDAARTTTSSRDDPPSMSNASEMQAEWIEEDEPGVYITIRQLSDGTRELRRVRFSRERFGEVHAKTWWEQNRERIQTQYL
Protein: Probable thioesterase YBR096W (EC 2.3.1.-) (P38256)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MGVCTIFRWLFAAYLLSSYKSLPGAYFVRFYYYVIQNLFLPMFTGFETENIKKLEKNEYGCFSYTSLDTYASPFECDFYFHKSNSTYFAELDISRGNLMCKIFQKLMLNSKHYPYIPVANVFTNFLKEIKPFQKYSVSSRIICWDEKWIYVMSRFTIKKGTVLCSLSLTKYVLKDGRKTIKPKDALEYCGLYNEKVAKISEDNLKLLTERCGFHETVPLENLSQEYCSEI
Protein: F14O23.23 protein (Ubiquitin carboxyl-terminal hydrolase family protein) (Q9M9G1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein-tyrosine-phosphatase PTP1
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Senescence/dehydration-associated protein At4g35985
- Uncharacterized protein MHF15.4
- Calmodulin-lysine N-methyltransferase
- Peptide deformylase 1B, chloroplastic/mitochondrial
- Probable choline kinase 2
- Peptide deformylase 1A, chloroplastic/mitochondrial
- Probable LRR receptor-like serine/threonine-protein kinase At5g10290
Sequence:
MKSIFRSISIRRHSGHRTFADTSAVEDTYKFVRDRGLDHAVEREKNLRPLLSIKDLIRSEPAKSVPISVITSQKDSLRVPLRPIEFIRSFPSVFQEFLPGGIGIHPHISLTPEILNHDADEQLVYGSETYKQGLADRLLKLLMINRINKIPLEILDLLKWDLGLPKDYVETMVPEFPDYFRVIKSKLRGCSGELELVCWSNEHAVSVLEKKARTLRKGEYTKGSAIAFPMKFSNGFVVDKKMKKWIDDWQKLPYISPYENALHLSATSDESDKWAAAVLHEIMNLFVSKKVEKDAILHLGEFMGLRSRFKRVLHNHPGIFYLSSKLRTHTVVLRDGYKRGMLIESNELVTSRNRYMKLMNTVKKDNKAVSSSSKKEDKGKVEGEVCDTDAKAENDDISGSDVEDDRQGDFVDDDEDDDEVDQNQDLERGRRNSSPRSGRRSFGNSGSRDKAQSRRSKISLKTEKKRSRMY
Protein: Endochitinase (EC 3.2.1.14) (Allergen Pers a 1) (Allergen Prs a 1) (Chitin-binding avocado protein) (CBAP) (Class I chitinase) (PaI1) (allergen Pers a 1.0101) (P93680)
Organism: Persea americana (Avocado)
Function: Defense against chitin-containing fungal pathogens. Has in vitro antifungal activity against F.oxysporum inhibiting its growth and the branching of its hyphae. Has endochitinase activity, but no exochitinase or lysozyme activities.
Interaction partners:
Sequence:
MVYCTASLPLLLLLLVGLLAGEAFAEQCGRQAGGALCPGGLCCSQFGWCGSTSDYCGPTCQSQCGGVTPSPGGGVASLISQSVFNQMLKHRNDAACQAKGFYTYNAFIAAANSFNGFASVGDTATRKREIAAFLAQTSHETTGGWATAPDGPYAWGYCFLKEQGNPPDYCVPTAQWPCAPGKKYYGRGPIQISYNYNYGPAGRAIGYDLINNPDAVATDPVISFKTALWFWMTPQSPKPSCHNVITGRWTPSAADRAAGRLPGYGVITNIINGGIECGKGFNDKVADRIGFYKRYCDLLGVSYGSNLDCYNQRSFGVSTNPLAASS
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate decaprenyltransferase) (COQ2 homolog) (hCOQ2) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (Q96H96)
Organism: Homo sapiens (Human)
Function: Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis. Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-trans-decaprenyl diphosphate). The length of the polyprenyl side chain varies depending on the species, in humans, the side chain is comprised of 10 isoprenyls (decaprenyl) producing CoQ10 (also known as ubiquinone), whereas rodents predominantly generate CoQ9. However, this specificity is not complete, human tissues have low amounts of CoQ9 and rodent organs contain some CoQ10. Plays a central role in the biosynthesis of CoQ10. CoQ10 is a vital molecule that transports electrons from mitochondrial respiratory chain complexes. CoQs also function as cofactors for uncoupling protein and play a role as regulators of the extracellularly-induced ceramide-dependent apoptotic pathway. Regulates mitochondrial permeability transition pore (mPTP) opening and ROS production (pivotal events in cell death) in a tissue specific manner (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:27493029}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
Interaction partners:
- All trans-polyprenyl-diphosphate synthase PDSS1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Atypical kinase COQ8A, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- UbiA prenyltransferase domain-containing protein 1
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Atypical kinase COQ8B, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Sal-like protein 3
Sequence:
MLGSRAAGFARGLRAVALAWLPGWRGRSFALARAAGAPHGGDLQPPACPEPRGRQLSLSAAAVVDSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAAEPGCFPDWYMLSLFGTGAILMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYYSIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGALLGWSAIKGSCDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTKPWLSGFSVAMLGALSLVGVNSGQTAPYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFISNRTLGLIVFLGIVLGNLWKEKKTDKTKKGIENKIEN
Protein: Aftiphilin (Q6ULP2)
Organism: Homo sapiens (Human)
Function: Component of clathrin-coated vesicles. Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Co-localizes with AP1G1/AP-1 in the cytoplasm (PubMed:14665628, PubMed:15758025). Recruited to the perinuclear region by AP1G1/AP-1 (PubMed:15758025). {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}.
Interaction partners:
- Synergin gamma
- AP-1 complex subunit sigma-2
- Clathrin heavy chain 1
- AP-2 complex subunit beta
- Clathrin light chain A
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- AP-5 complex subunit mu-1
- AP-4 complex subunit epsilon-1
- AP-2 complex subunit alpha-1
Sequence:
MEPDIIRMYSSSPPPLDNGAEDDDDDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEEFVPSNHFMPIHEFSENVDSLTSFKSIKNGNDKDITAELSAPVKGQSDVLLSTTSKEIISSEMLATSIDGMERPGNLNKVVEQRQNVGTLESFSPGDFRTNMNVVHQNKQLESCNGEKPPCLEILTNGFAVLETVNPQGTDDLDNVADSKGRKPLSTHSTEYNLDSVPSPAEEFADFATFSKKERIQLEEIECAVLNDREALTIRENNKINRVNELNSVKEVALGRSLDNKGDTDGEDQVCVSEISIVTNRGFSVEKQGLPTLQQDEFLQSGVQSKAWSLVDSADNSEAIRREQCKTEEKLDLLTSKCAHLCMDSVKTSDDEVGSPKEESRKFTNFQSPNIDPTEENDLDDSLSVKNGDSSNDFVTCNDINEDDFGDFGDFGSASGSTPPFVTGTQDSMSDATFEESSEHFPHFSEPGDDFGEFGDINAVSCQEETILTKSDLKQTSDNLSEECQLARKSSGTGTEPVAKLKNGQEGEIGHFDSVPNIQDDCNGFQDSDDFADFSSAGPSQVVDWNAFEDEQKDSCSWAAFGDQQATESHHRKEAWQSHRTDENIDTPGTPKTHSVPSATSKGAVASGHLQESATSVQTALLNRLERIFEACFPSILVPDAEEEVTSLKHLLETSTLPIKTREALPESGELLDVWTELQDIHDAHGLRYQWGGSHSNKKLLSSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTATMSPDMNTCTSDQFQESLPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTTIPGVDPELYELTTSKLEISTSSLKVTDAFARLMSTVEKTSTSTRKPKREEHLSEEAIKVIAGLPDLTFMHAKVLMFPATLTPSTSSQEKADG
Protein: NDRG family member 4 (Protein NDRG4) (A0A0R4ICQ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- GINS complex subunit 3.
- Popeye domain-containing protein 1
- RING finger protein 207
- N-myc protein
Sequence:
MPECWDGEHDIETPYGMLHVVIRGAPKGNKPAILTYHDVGLNHKLCFNSFFQNEDMLEITKHFVVCHVDAPGQHIGAPQMPQGYQYPTMDQLAGMLPSVVQHFGFKSIVGIGVGAGAYILAKFALIFPDLVEGLVLLNIDPNGKGWIDWAATKLSGLTSTLPDTVLTHLFSQEELMSNTEVVQNYRQQINNTINQFNLQLFWNMYNSRRDLEMNRSGSVINAKTLRCPVMLVVGDNAPAEEGVVECNSKLDPTNTTFLKMADSGGMPQITQPGKLTEAFKYFLQGMGYIAYMKDRRMSGGPVPSASMTRLARSRTASLTSAGSVDGSRNRACTHSDSSEGVGQVSHTMEVSC
Protein: Kinesin-like protein KIF24 (Q5T7B8)
Organism: Homo sapiens (Human)
Function: Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells, leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin, possibly to suppress aberrant cilia formation. Following activation by NEK2 involved in disassembly of primary cilium during G2/M phase but does not disassemble fully formed ciliary axonemes. As cilium assembly and disassembly is proposed to coexist in a dynamic equilibrium may suppress nascent cilium assembly and, potentially, ciliar re-assembly in cells that have already disassembled their cilia ensuring the completion of cilium removal in the later stages of the cell cycle. Plays an important role in recruiting MPHOSPH9, a negative regulator of cilia formation to the distal end of mother centriole.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30375385}. Note=Primarily localizes to the mother centriole/basal body and is either absent at daughter centriole.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 97 kDa
- Serine/threonine-protein kinase Nek2
Sequence:
MASWLYECLCEAELAQYYSHFTALGLQKIDELAKITMKDYSKLGVHDMNDRKRLFQLIKIIKIMQEEDKAVSIPERHLQTSSLRIKSQELRSGPRRQLNFDSPADNKDRNASNDGFEMCSLSDFSANEQKSTYLKVLEHMLPDDSQYHTKTGILNATAGDSYVQTEISTSLFSPNYLSAILGDCDIPIIQRISHVSGYNYGIPHSCIRQNTSEKQNPWTEMEKIRVCVRKRPLGMREVRRGEINIITVEDKETLLVHEKKEAVDLTQYILQHVFYFDEVFGEACTNQDVYMKTTHPLIQHIFNGGNATCFAYGQTGAGKTYTMIGTHENPGLYALAAKDIFRQLEVSQPRKHLFVWISFYEIYCGQLYDLLNRRKRLFAREDSKHMVQIVGLQELQVDSVELLLEVILKGSKERSTGATGVNADSSRSHAVIQIQIKDSAKRTFGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELKKGIKCCTSVTSRNRTSGNSSPKRIQSSPGALSEDKCSPKKVKLGFQQSLTVAAPGSTRGKVHPLTSHPPNIPFTSAPKVSGKRGGSRGSPSQEWVIHASPVKGTVRSGHVAKKKPEESAPLCSEKNRMGNKTVLGWESRASGPGEGLVRGKLSTKCKKVQTVQPVQKQLVSRVELSFGNAHHRAEYSQDSQRGTPARPASEAWTNIPPHQKEREEHLRFYHQQFQQPPLLQQKLKYQPLKRSLRQYRPPEGQLTNETPPLFHSYSENHDGAQVEELDDSDFSEDSFSHISSQRATKQRNTLENSEDSFFLHQTWGQGPEKQVAERQQSLFSSPRTGDKKDLTKSWVDSRDPINHRRAALDHSCSPSKGPVDWSRENSTSSGPSPRDSLAEKPYCSQVDFIYRQERGGGSSFDLRKDASQSEVSGENEGNLPSPEEDGFTISLSHVAVPGSPDQRDTVTTPLREVSADGPIQVTSTVKNGHAVPGEDPRGQLGTHAEYASGLMSPLTMSLLENPDNEGSPPSEQLVQDGATHSLVAESTGGPVVSHTVPSGDQEAALPVSSATRHLWLSSSPPDNKPGGDLPALSPSPIRQHPADKLPSREADLGEACQSRETVLFSHEHMGSEQYDADAEETGLDGSWGFPGKPFTTIHMGVPHSGPTLTPRTGSSDVADQLWAQERKHPTRLGWQEFGLSTDPIKLPCNSENVTWLKPRPISRCLARPSSPLVPSCSPKTAGTLRQPTLEQAQQVVIRAHQEQLDEMAELGFKEETLMSQLASNDFEDFVTQLDEIMVLKSKCIQSLRSQLQLYLTCHGPTAAPEGTVPS
Protein: Endonuclease 8 2 (DNA glycosylase/AP lyase Nei 2) (EC 3.2.2.-) (DNA-(apurinic or apyrimidinic site) lyase Nei 2) (EC 4.2.99.18) (Endonuclease VIII 2) (P9WNC1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). Complements an E.coli nei nth double mutant.
Interaction partners:
- Probable ATP-dependent helicase Lhr
- Uncharacterized formamidopyrimidine-DNA glycosylase-like protein
- Ribonuclease 3
- Endonuclease III lyase)
- Endonuclease 8 1 lyase Nei 1)
- Protein RecA
- Adenine DNA glycosylase
- DNA polymerase I
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- Conserved protein
Sequence:
MPEGDTVWHTAATLRRHLAGRTLTRCDIRVPRFAAVDLTGEVVDEVISRGKHLFIRTGTASIHSHLQMDGSWRVGNRPVRVDHRARIILEANQQEQAIRVVGVDLGLLEVIDRHNDGAVVAHLGPDLLADDWDPQRAAANLIVAPDRPIAEALLDQRVLAGIGNVYCNELCFVSGVLPTAPVSAVADPRRLVTRARDMLWVNRFRWNRCTTGDTRAGRRLWVYGRAGQGCRRCGTLIAYDTTDERVRYWCPACQR
Protein: DUF1476 domain-containing protein (A1B602)
Organism: Paracoccus denitrificans (strain Pd 1222)
Interaction partners:
- ATP synthase gamma chain
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit c
- ATP synthase subunit delta
- ATP synthase epsilon chain
- ATP synthase subunit a
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Phosphoribosylformylglycinamidine synthase subunit PurS
Sequence:
MTTFDDRERAHEAKFAHDAELNFKAEARRNRLLGEWAAGLLGKTGDDARAYALTVVTSDFDEPGDEDVFRKLAADLEGKADEETIRAKMVELRATAREQIISEI
Protein: AFG2 interacting ribosome maturation factor (V9GYQ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTQDRPLLAVQEALKKCFPVVEEQQGLWQSALRDCQPLLSSLSNLAEQLQAAQNLRFEDVPALRAFPDLKERLRRKQLVAGDIVLDKLGERLAILLKVRDMVSSHVERVFQIYEQHADTVGIDAVLQPSAVSPSVADMLEWLQDIERHYRKSYLKRKYLLSSIQWGDLANIQALPKAWDRISKDEHQDLVQ
Protein: Transcription initiation factor IIB-2 (General transcription factor TFIIB-2) (AtTFIIB2) (Q9SS44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor IIF subunit alpha
- Transcription initiation factor IIA subunit 2
- DNA-directed RNA polymerase II subunit 4
- General transcription and DNA repair factor IIH subunit TFB2
- DNA-directed RNA polymerases II, IV and V subunit 11
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH subunit TFB4
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH helicase subunit XPD
- Transcription initiation factor TFIID subunit 1b
Sequence:
MSDAFCSDCKRHTEVVFDHSAGDTVCSECGLVLESHSIDETSEWRTFANESGDNDPVRVGGPTNPLLADGGLTTVISKPNGSSGDFLSSSLGRWQNRGSNPDRGLIVAFKTIATMADRLGLVATIKDRANEIYKRVEDQKSSRGRNQDALLAACLYIACRQEDKPRTVKEICSVANGATKKEIGRAKEYIVKQLGLETGQLVEMGTIHAGDFMRRFCSNLGMTNQTVKAAQESVQKSEEFDIRRSPISIAAAVIYIITQLSDEKKPLRDISVATGVAEGTIRNSYKDLYPHLSKIIPAWYAKEEDLKNLQSP