wanglab/gogpt-training-data huggingface dataset:
Protein: Doublesex- and mab-3-related transcription factor B1 (Q96MA1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
- C-terminal-binding protein 1
Sequence:
MADKMVRTPKCSRCRNHGFLVPVKGHAGKCRWKQCLCEKCYLISERQKIMAAQKVLKTQAAEEEQEAALCAQGPKQASGAAAAAPAPVPVPAASLRPLSPGTPSGDADPGPEGRAAACFFEQPPRGRNPGPRALQPVLGGRSHVEPSERAAVAMPSLAGPPFGAEAAGSGYPGPLDLRRPMRTVPGPLFTDFVRPLNINPDRALGPEYPGGSSMHPYCPFPLGYLDAPPGVPLQQGFRHVSRSQYQGGGLVSEPGGDFQPSYYLPPPPPPLPPLPPLPPQPQFLPPGYLSALHFLPPPPPPPPPSSFSLTVLFDTDKENTDDQDAEVLSGEPSQPSSQEQSD
Protein: Uncharacterized protein (Q57WG6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- tRNA/rRNA methyltransferase SpoU type domain-containing protein
- Ribosomal protein L9 domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L9 domain-containing protein
- Large ribosomal subunit protein mL43
- Uncharacterized protein
- Large ribosomal subunit protein uL23m
- Uncharacterized protein
- Large ribosomal subunit protein uL3m
Sequence:
MWHSSLRYVSFKRLPFGRRSTSGGVNFNKGLLTDRERGDPFTEPHAYRNKKSIAAISKVAKKQDILLREEKQRKELDKIQSGYVTERELHIGCDKPLGGNANEIARVIDEQALISPTPGEKCSTALRELMENEVDRRNHMMDKFGQPVGAREFHRLFKELRHADNEAETIERHQTRLVEEYGVYPSLRLDAYMLDDDTYFPEWVNALPYSIRDRVKFGSLGLTEKDEALRVTLGRMPLDRRRREWERLKKAKEYKAAKEETLTLAELRDARQGKRRFHWLQRKRQKRASILRRLALRKPDAFELWPSRVVDYSQRIAFIAQHVENGLDTKGQWPLDPEELARARVRRSKEEAERTFLMSAEEKRAHKKLSGRSGDGSIAEMLQSLEVPDKPFKRLSRKVYANRVNAIVHGDQDEYGRRYRKMETRSKRRMRPYASLGEIGLENELRKEPRINAKGLNNTDDEDWPRHTKSWGDGMPSMRYGS
Protein: Focal adhesion kinase targeting (FAT) domain-containing protein (G1NJW1)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MSSKIQPAPPEEYVPMVKEVGLALRTLLATVDESLPVLPASTHREIEMAQKLLNSDLAELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMISQSRPH
Protein: Glutaminase kidney isoform, mitochondrial (GLS) (EC 3.5.1.2) (K-glutaminase) (L-glutamine amidohydrolase) [Cleaved into: Glutaminase kidney isoform, mitochondrial 68 kDa chain; Glutaminase kidney isoform, mitochondrial 65 kDa chain] (P13264)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:1991024}. Cytoplasm, cytosol {ECO:0000269|PubMed:1991024}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68 and 65-kDa subunits. {ECO:0000269|PubMed:1991024}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 68 kDa chain]: Mitochondrion matrix {ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:7836378}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:7836378}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 65 kDa chain]: Mitochondrion matrix {ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:7836378}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:7836378}.
Interaction partners:
- Glutamine synthetase
- Glutamate dehydrogenase 1, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Amidophosphoribosyltransferase
- Glutamine--fructose-6-phosphate aminotransferase 2
- Glutamine--fructose-6-phosphate aminotransferase 1
- Carbamoyl-phosphate synthase, mitochondrial
- Multifunctional protein CAD
Sequence:
MMRLRGSAMLRELLLRPPAAVGGVLRRTQPLGTLCRRPRGGSRPAAGLVAAARLHPWWGGGGRAKGPGSGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKVKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKENQTVHKNLDGLL
Protein: Phosducin-like protein (PHLP) (Q13371)
Organism: Homo sapiens (Human)
Function: Acts as a positive regulator of hedgehog signaling and regulates ciliary function.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q9DBX2}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- T-complex protein 1 subunit eta
- 26S proteasome regulatory subunit 8
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
Sequence:
MTTLDDKLLGEKLQYYYSSSEDEDSDHEDKDRGRCAPASSSVPAEAELAGEGISVNTGPKGVINDWRRFKQLETEQREEQCREMERLIKKLSMTCRSHLDEEEEQQKQKDLQEKISGKMTLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAMNGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDLEAFLQEFGLLPEKEVLVLTSVRNSATCHSEDSDLEID
Protein: T-complex protein 1 subunit delta (TCP-1-delta) (A45) (CCT-delta) (P80315)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23807208}. Melanosome {ECO:0000250|UniProtKB:P50991}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta-2
- Chaperonin containing TCP1 subunit 8-like 1
- Cell division cycle protein 20 homolog
Sequence:
MPENVASRSGAPTAGPGSRGKSAYQDRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKGDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGTTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGLEILTDMSRPVQLSDRETLLNSATTSLNSKVVSQYSSLLSPMSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEGLVLTQKVANSGITRVEKAKIGLIQFCLSAPKTDMDNQIVVSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILRDALSDLALHFLNKMKIMVVKDVEREDIEFICKTIGTKPVAHIDQFTADMLGSAELAEEVSLNGSGKLFKITGCTSPGKTVTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGGAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLAENAGLNPISTVTELRNRHAQGEKTTGINVRKGGISNILEEMVVQPLLVSVSALTLATETVRSILKIDDVVNTR
Protein: Acid phosphatase PHOa (AFU_orthologue AFUA_1G03570) (Q5B5X5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Purple acid phosphatase
- 3-phytase
- Alkaline phosphatase
- Thiamine biosynthetic bifunctional enzyme, putative
- Riboflavin synthase
- Acid phosphatase
- Acid phosphatase, putative
- FAD synthase
- Riboflavin kinase
Sequence:
MKSSLVILLGAVASTVAQTATTTEPSLSDIAASAATIEPYSPVSNVEGLAFQRIFQVWFENIDYEDAAANENLQWLAKQGIVLSNFYAVTHPSQPNYCAAAGGDTFGMDHDDFLRIPANVSTVVDLLDTKYIAWAEYQEHMPYPGFEGFNYSNQETYADDYVRKHNPLILYDSVAENDMRRRQIKNFTHFDDDLASEKLPQWAFFTPNMTNDAHDTNITFAANWLRGWISPLLENDYFMNDTLILITFDEDKTFPKDNRIFSILLGGAVPENLHGTEDNTFYTHYSVIASVSANWGLPSLGRWDCGANILEIVANKTGYVNYKVDTTNLRLNQTYPGPLSNGDLSEYSPVWPNPLTEGDCSAGHGILDTVKETYAGTQPTYNYTSPFPYDSKSGYNEDVDATRKSS
Protein: Maltose regulon regulatory protein MalI (P18811)
Organism: Escherichia coli (strain K12)
Function: Repressor for the malX and malY genes. Also regulates its own expression. Binds maltose as an inducer.
Interaction partners:
- Protein MalY
- HTH-type transcriptional regulator EbgR
- 7alpha-hydroxysteroid dehydrogenase
- HTH-type transcriptional regulator UidR
Sequence:
MATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNAAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLHGGKDGEQLAQRFSLLLNQGVDGVVIAGAAGSSDDLRRMAEEKAIPVIFASRASYLDDVDTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSDWVLECTSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLKAGRQSGESGVDRYFEQQVSLAAFTDATPTTLDDIPVTWASTPARELGITLADRMMQKITHEETHSRNLIIPARLIAAK
Protein: GON-4-like protein (Q21216)
Organism: Caenorhabditis elegans
Interaction partners:
- Nicotinic receptor-associated protein 1
- HAT C-terminal dimerisation domain-containing protein
- Forkhead transcription factor fkh-6
- F-box C protein
Sequence:
MEDTAEENNESIDDQPSTSTATDPNQTRETEKEKGDDEMFRLLQATDEILENKAKSMNLSSLNVRSILHHLIKYPSTIDVLLGIRENDDLPSVRNMRSRKKPDDSGASSTVNTPKKFGALRIEDRGPKSFLDLEYEEDDEYDDDYIEENDTSTRNKLNAGSEEDEENDDEEEIEDEGEDEDDEEQDELEEDGEHEITGSEACTSGQNDTMHALLFDETSEDVQNEEDYVLNMTLNDTRAESVAPIPTLDNVDDDGFYRDFVTGINRTEKDNDNLEVLDTEDDPDDEDYNVCADDGLNVEDWDETRQDKTTQIPRHELKALMIDTLLAEKEIPLNAFPEEAINGEEHRKSQKVKDAEVYERINTSISSSSESCSLLKDSLATFRPQELQQLNMQLEQHVQLLTQLVVTCHHDVNLSHVRNSSQLMMNELDDIRQQKIYPTVFDVRNLDAAIESCHDINAFDAVDESFLKYAENTEGYGGIALRPEAAVVLSRSNAIRYPALLPSRQPFFIETPIPFLSEEDLMLAVALLQFAHLPRRGEKEMIDRYTAIQQHCLPARSSYKIRTHLKSMRRSDKNPIHQIMQAAEKGVCKLVLPLKSWQESDTPICQWPPASQPGWYRRFQETFNVTEERKILRKHVSTMVLTPVKNKDRQDQEASEATFESGEEGEDDEFVNMGTAPDGRKIIMGREHIEDLVHQLIKQNEISPSKRRKNPTPMKLSTMIQLEEAEKRIADSQKNSCGGQTISALSNVSGDSNVDNNGTHEKELMPSTSSIDSLESINNQETSKFPRPLPMSDQPTLNTSCHITTTTCSVSYEDVDVGTLKKSYVEITASKYETNSNSCFSYPIPPTPGRRSPDDFDDYFMDLESNSLMWPQTPYAVTDENPQTPRGFSASESSEPIDFSSLGKATSLDTEEIVFQSTSCQRPMGYCSDFGEFSNSSSLPEEIPVPSHQRTPQESAIEDDSSMPGLDMVPLYEEDVEECIIEDIEEEEAPIKQGLVNSRPPLRFKKEVKAGITNLAPSRKRTRIEREAMGSVGLDDEQLHDKQKENIMRKVIEDVNQRLFMHTDTYQRFKEAITDENLTDFEKVTRTIIILANHPELLNLVLLNAPPEAVISDLQCDHNYQSYKVAIEMIMDIERYITAAKLKEPSLKGLFRYIQSFLEDKPNMTDEQATKRFYELFGQDRPLWKKLESRFWCLPYKARPRLENYEYIDLTGLETMSKREKRDWNSIPPRFETVDDIDQVMGSVYRASKNEPPSNLVVKCGEFCIRNDDETYTQLEITERLWTRKDDISLLTSYNEALKTIPNFTVSQMPSLISDLSFGEKSIIARLQYLLTELKSLD
Protein: Uncharacterized protein (F4JCB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQQIEKRSLLCSFLSVFHLIHLQALLLEMAELRSGVLFKLLEEMGVGKVRRDVDHRPVLLQIRCIIPVLAAGGLWPNKGFFLRITDSTHSIYVSLPREENDLVLYDKLQIGQLIFVEKLEFAYPVPMIKGIRPTPGRRACTGDPIDLIPKERIEKFCVGLSDIEENYDHQVKKPRRTRWNNSSVSELNFTDLGLSKNLSSVMEEKDDTESMISSCSSSFSSAARRRSWIGSADNRKRRDSLDPSMIKNHDHDTKHVSRARSSSATSPSLSIRSYGGIEEKSSSRTRRRDVVVSPSPRWSKSLSYGSRSNKSKNLLPPKSNTFESSDPISRKRSWTETEILWDSLPPKVVNLGKEILRQRDTAIRAASQALLEASAAERLLKCLRSYSELSDRRNQHQENQQPPIQDFLSFQDELSKSRLIIQSLSTEKTEHCNANIVKTGDERREKATQWIKSALATDLKLVSLSASKPTQSPGRKGLTLIAQESDNREGNASESNSRLGEIKERLSRASSELRNWLKEEGRSWYLNRVEKYLDEISNGTKWREMRSEEVGETMYQIKRVSDWLDTIVKGEEDEEEKMVMMMMSESETEACGRVRNKIYRILLKHVETTSLLSHQRSTSLMSHHQQQQHEQHLFQKTMSL
Protein: Ribosomal lysine N-methyltransferase 1 (EC 2.1.1.-) (Q08961)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosomal lysine N-methyltransferase 2
- Protein BCP1
- Ribosomal lysine N-methyltransferase 3
- Ribosomal lysine N-methyltransferase 5
- Ribosomal lysine N-methyltransferase 4
- Protein arginine N-methyltransferase 2
- Protein-lysine N-methyltransferase EFM4
- Cytochrome c lysine N-methyltransferase 1
- Large ribosomal subunit protein uL14A
- Histidine protein methyltransferase 1
Sequence:
MSSDALKALLQWGASFGVIVPEELKFLYTDLKGIICVCEKDIDNPSIKIPPEIVISRNLPMKFFGLSESTKNINGWLKLFFAKIKFDRDNDTIVDNVRVNDKFKPYLDALPSRLNSPLVWNPSELKRLSSTNIGNSIHEKFEGIFKEWFELVSSSDMFDLERVADDVQTFHNLDELTYEALYEKILKITELQRPTIWYSFPAFLWSHLIFISRAFPEYVLNRNCPDNSIVLLPIVDLLNHDYRSKVKWYPENGWFCYEKIGTASQSRELSNNYGGKGNEELLSGYGFVLEDNIFDSVALKVKLPLDVVSTILETEPSLKLPLLSDYTTYAFENKDCVQQEKKATRSATDYINGVTYFINIQNEQCLEPLLDLFTYLSKAEEEDLHDLRARLQGIQMLRNALQSKLNSITGPPATDDSYAIDPYRVYCADVYTKGQKQILKEALTRLKKLEKTMLSENKHQLLTMSKILKNDPAFAETELPSLFSNEDGEEVIFESTYDLLILWILLKTKKNSYPTKYEWVGQQYTNFKQTAYISDDAKAFHTAYFEKQDDVDLAEVDHAIQFVVDNSFTRTSSTTEETILVRK
Protein: 48 related 2, isoform C (A0A0B4LIA7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRNQLPDSSSSPPISHLPFHNFDDDLINDLPSCIYAGQHQGGGATGGGGGSGGGGGSSGLRLSSNNLRHIQQHYMQHSGENLLDSSTNPMGVHNSGGGAPLMCNSPSASSSGGGCGNAGSATPGGAGGPNPGYGSVGAATASSYKMQRQAANVRERKRIQRSAPTGSINSAFDELRVHVPTFPYEKRLSKIDTLRLAIAYISLLREVLQTDYDPLTYVEKCLRGEIKADRANWNTSDLTARLSWINWENLGVHPGRRTLLTSLALSSEPMCGAHCGMP
Protein: Selenoprotein P (SeP) (P49908)
Organism: Homo sapiens (Human)
Function: Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.
Subcellular location: Secreted {ECO:0000269|PubMed:8142465}. Note=Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium. {ECO:0000250|UniProtKB:P70274}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit C-like protein
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit E
- Glutathione peroxidase 3
- Eukaryotic translation initiation factor 3 subunit J
Sequence:
MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASUYLCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSUCCHCRHLIFEKTGSAITUQCKENLPSLCSUQGLRAEENITESCQURLPPAAUQISQQLIPTEASASURUKNQAKKUEUPSN
Protein: SIX homeobox 3 (A0A0G2JWI0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVFRSPLDLYSSHFLLPNFADSHHCSLLLASSGGGSGAGGGGGAGGGGGGGGGNRAGGGGAGGAGGGGGGGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSILSPPTMAKAVKSHGTAGQSWMRRLC
Protein: Ghiberti (Q8IQC4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine palmitoyltransferase 1
- serine C-palmitoyltransferase
- Serine palmitoyltransferase small subunit B
- Serine palmitoyltransferase small subunit B
Sequence:
MLDNLVEFASYWWFRYLMVTELYMVEKWERITIHVIFMVLFCVFWYFNYSVLLSLAGLIGPTSASIADIIPGVQGHGLKVT
Protein: NADPH:quinone oxidoreductase (EC 1.6.5.2) (Q9LK88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}.
Interaction partners:
- AT4g29480/F17A13_300
- Nitroreductase family protein
- Wall-associated receptor kinase 3
- Bifunctional riboflavin kinase/FMN phosphatase
- FAD synthetase 1, chloroplastic
- Leucine-rich repeat receptor-like protein kinase PXL1
Sequence:
MEAVTAIKPLIRVAALSGSLRKTSFHTGLLRAAIDLTKESVPGLQIEYIDISPLPLINTDLEVNGTYPPVVEAFRQKILEADSILFASPEYNFSVSAPLKNALDWASRPPNVWADKPAAIISTGGGFGGGRSQYHLRQIGVFLDLHFINKPEFTLNAFQPPQKFDAEGNLVDEVTKERLKQVLLSLQAFTLRLQGK
Protein: Lipase member M (EC 3.1.1.-) (Lipase-like abhydrolase domain-containing protein 3) (Q5VYY2)
Organism: Homo sapiens (Human)
Function: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MLETLSRQWIVSHRMEMWLLILVAYMFQRNVNSVHMPTKAVDPEAFMNISEIIQHQGYPCEEYEVATEDGYILSVNRIPRGLVQPKKTGSRPVVLLQHGLVGGASNWISNLPNNSLGFILADAGFDVWMGNSRGNAWSRKHKTLSIDQDEFWAFSYDEMARFDLPAVINFILQKTGQEKIYYVGYSQGTTMGFIAFSTMPELAQKIKMYFALAPIATVKHAKSPGTKFLLLPDMMIKGLFGKKEFLYQTRFLRQLVIYLCGQVILDQICSNIMLLLGGFNTNNMNMSRASVYAAHTLAGTSVQNILHWSQAVNSGELRAFDWGSETKNLEKCNQPTPVRYRVRDMTVPTAMWTGGQDWLSNPEDVKMLLSEVTNLIYHKNIPEWAHVDFIWGLDAPHRMYNEIIHLMQQEETNLSQGRCEAVL
Protein: Abelson interacting protein, isoform C (Abelson interacting protein, isoform E) (A0A0B4KH51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLTETPMASENIMDELASLIRTEIPDGRQSLRDSYTNLERVADYCEDTYYRADNKKAALEATKNYTTQSLASVAYQINTLAYSYMQLLELQAQQLGEMESQMNHIAQTVHIHKEKVARREIGVLTANKVSSRQFKIVAPINPEKPIKYVRKPIDYSMLDEIGHGINSAQHSQVRQKHRGSSHGSVQSLLPPSVGPPPTTKPPTPPQMSRAGNTGTLGKSVSNTGTLGKSSREYRTPPVVNPPQVPSHYAPNYPIGHPKRMSTASSTMTTTTTGGGAAGNERAAGYSALPMPPSQQIATHVNLPSAGMMQSLPPPPPTTYDDRSSMPPPPSPLTVSQHEMTEQSHIGMHTLGRNINRNHFSLNFARPGSQSPPLPPPPPPEDEHQDFGRPRTSTGPQLAPIVPEDQNLPGWVPKNFIEKVVAIYDYYADKDDELSFQESSVLYVLKKNDDGWWEGVMDGVTGLFPGNYVEPCV
Protein: Mitochondrial inner membrane magnesium transporter mrs2 (RNA-splicing protein mrs2) (P87149)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High-conductance magnesium-selective channel that mediates the influx of magnesium into the mitochondrial matrix. Essential for the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing. It also suppresses a variety of mitochondrial intron mutations and its absence may disturb the assembly of mitochondrial membrane complexes.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q01926}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01926}.
Interaction partners:
- Uncharacterized mitochondrial carrier C8C9.12c
- Putative metal ion transporter C17A12.14
- Uncharacterized Rab geranylgeranyltransferase C15C4.03
Sequence:
MVLIVGFNLRTSIASFSPICRSLFLFPKYRSRIIRPVVLLEKPFDKHFYATDSNPLITGFPETSKNCPPSVAATKNRLLMNCTEFDDHGNVRVISGDFKKMDLCKQNGLLPRDLRKLNTSINSIVPVILVREGSILINLLHIRALIKANSVLLFDVYGSQHSHSQSQFIYELEGRLKQKSSDFGWLPYEMRALETILVSVVNTLDSELHVLHNLVSDLLADFELDINQERLRTLLIFSKRLSGFLKKATLIRDVLDELLEQDQDLAGMYLTERLKTGKPRDLDKHDEVELLLETYCKQVDEIVQQTDNLVGNIRSTEEICNIMLDANRNSLMLLGLKLSAMTLGLGFGAVVASLYGMNLQNGLENHPYAFYITTGSIFAFAAFLSSLGILKIRRLKRIQMALYHRCNLPISLDPRSLRPPYL
Protein: Cystatin cpi-1 (Cysele1) (G5EDZ9)
Organism: Caenorhabditis elegans
Function: Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation.
Interaction partners:
- SCP domain-containing protein
- Transthyretin-like family protein
- TIL domain-containing protein
- Reelin domain-containing protein
Sequence:
MRFILLIALVFAVLDGINCQIAGGLSDVNASEYTGAAWNSVPEINSKNNGQNYMVPIKVVKAQVQVVAGTNTVLEVLVGESTCPRQGSVQASQVTAANCPLKSGGKRELYKVSIWEKPWENFKQTKAEKIRGVKPDEKI
Protein: Centrosomal protein of 135 kDa (Cep135) (Centrosomal protein 4) (Q66GS9)
Organism: Homo sapiens (Human)
Function: Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:32060285, ECO:0000269|PubMed:32946374}. Note=During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles.
Interaction partners:
- Spindle assembly abnormal protein 6 homolog
- Centrosomal P4.1-associated protein
- Serine/threonine-protein kinase PLK4
- Centrosomal protein of 152 kDa
- Centriolar coiled-coil protein of 110 kDa
- SCL-interrupting locus protein
- Centrosomal protein of 295 kDa
- Serine/threonine-protein kinase PLK1
- Centlein
- WD repeat-containing protein WRAP73
Sequence:
MTTAVERKYINIRKRLDQLGYRQTLTVECLPLVEKLFSDLVHTTESLRQSKLSAVKAEKESANFDFVLEPYKLENARLSRENNELYLELMKLREHSDQHVKELKTSLKKCARETADLKFLNNQYAHKLKLLEKESKAKNERIQQLQEKNLHAVVQTPGGKKRSIAFRRQRMQIDEPVPPSEVSSYPVPQPDDPYIADLLQVADNRIQELQQEVHQLQEKLAMMESGVRDYSKQIELREREIERLSVALDGGRSPDVLSLESRNKTNEKLIAHLNIQVDFLQQANKDLEKRIRELMETKETVTSEVVNLSNKNEKLCQELTEIDQLAQQLERHKEEVLETADKELGEAKKEIKRKLSEMQDLEETMAKLQLELNLCQKEKERLSDELLVKSDLETVVHQLEQEKQRLSKKVESFAVTERQLTLEVERMRLEHGIKRRDRSPSRLDTFLKGIEEERDYYKKELERLQHIIQRRSCSTSYSAREKSSIFRTPEKGDYNSEIHQITRERDELQRMLERFEKYMEDIQSNVKLLTAERDKLSVLYNEAQEELSALRKESTQTTAPHNIVSLMEKEKELALSDLRRIMAEKEALREKLEHIEEVSLFGKSELEKTIEHLTCVNHQLESEKYELKSKVLIMKETIESLENKLKVQAQKFSHVAGDSSHQKTEVNSLRIVNEQLQRSVDDYQHRLSIKRGELESAQAQIKILEEKIDELNLKMTSQDEEAHVMKKTIGVIDKEKDFLQETVDEKTEKIANLQENLANKEKAVAQMKIMISECESSVNQLKETLVNRDREINSLRRQLDAAHKELDEVGRSREIAFKENRRLQDDLATMARENQEISLELEAAVQEKEEMKSRVHKYITEVSRWESLMAAKEKENQDLLDRFQMLHNRAEDWEVKAHQAEGESSSVRLELLSIDTERRHLRERVELLEKEIQEHINAHHAYESQISSMAKAMSRLEEELRHQEDEKATVLNDLSSLRELCIKLDSGKDIMTQQLNSKNLEFERVVVELENVKSESDLLKKQLSNERHTVKNLESLLATNRDKEFHSHLTSHEKDTEIQLLKEKLTLSESKLTSQSRENTMLRAKVAQLQTDYDALKRQISTERYERERAIQEMRRHGLATPPLSSTLRSPSHSPEHRNV
Protein: Protocadherin 9 (A0A8I5ZK96)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLRDFYLLAALIACLRLDSAIAQELIYTIREELPENVPIGNIPKDLNISHINAATGTSASLVYRLVSKAGDAPLVKVSSSTGEIFTTSNRIDREKLCAGASYAEENECFFELEVVILPNDFFRLIKIKIIVKDTNDNAPMFPSPVINISIPENTLINSRFPIPSATDPDTGFNGVQHYELLNGQSVFGLDIVETPEGEKWPQLIVQQNLDREQKDTYVMKIKVEDGGTPQKSSTAILQVTVSDVNDNRPVFKEGQVEVHIPENAPVGTSVIQLHATDADIGSNAEIRYIFGAQVAPATKRLFALNNTTGLITVQRSLDREETAIHKVTVLASDGSSTPARATVTINVTDVNDNPPNIDLRYIISPINGTVYLSEKDPVNTKIALITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPKALHTLVLVFLYVNDTAGNASYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQSIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQCNSHSKNDLIPVTHQKCPSSTGFHIRENEESHSESQRRVTFHLPDGSQESCSDSGLGDHEPVGSGTLISHPLPLVQPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFSNGSHMADIPLANLKSYKQAGGTIESPKEHQL