wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-rhamnosidase (Q1HFU8)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MISLPLLALATGAVASASCWRNTSCTGPSKPSFPGPWDSNNFAPGSRLIQPKSILSLPDGTYISDYTSDSHPSITTEDAGLVFDFGLEVGGIVTIDYSSSVPNTTLGLAFTEAKDYIGRTSDNSNGGTGADGALATLLTEGEGSYTMPDSQLRGGFRYLALFIPSSSSSNASLTIQSITLELAFQPTWSNLRAYQGYFHSSDPVLNKAWYAGAYTLQTNSVPRTTCRVSVSSATGWNNNAVCGPGETLLLDGAKRDRWVWIGDMGVAVPSASVSTGDTESTKNALLAIWDNQTPSGLLPKAGPPYLRADSDTYHLWTIIGTYNYFLFTEDYDFLAGIWQKYVKALDYSLAKITPLGIMNATQTADWGRWNYGTLASSANMLLYRSLTTAAFLAPYAGDNPENYTDLASTLRSAIVTHLYDSAVGAFRDSPNSTLYPQDANSMALAFSFFSQSPLNCSSSFNLAEAARVSSYLESNWTPIGPEVPELPNNISPFISSIELEGHFASGHADRAIELIRMLWGWYLAHPNGTQSTVPEGYLVDGSWGYRGDRGYRNDPRYVSHAHGWSSGPTSTLTEYAVGLKITKPKGSEWSLRPASFGIQGFEEAQAGFTTGLGKFKAAFRVQGKRATVTWDTPAGTKGWVQLPGEEGSWVEGGMGSLTVKL
Protein: Small ribosomal subunit protein eS4 (40S ribosomal protein S4) (P41042)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein eL43
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein P2
- Small ribosomal subunit protein uS12
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein eL20
- 40S ribosomal protein S24
- Small ribosomal subunit protein eS19B
- Small ribosomal subunit protein eS10B
- Large ribosomal subunit protein uL10
Sequence:
MARGPKKHLKRLAAPKAWMLDKLGGVFAPRPSTGPHKLRESLPLLIFLRNRLKYALNGAEVTKIVMQRLVKVDGKVRTDPTYPAGYMDVITLEKTGEFFRLVYDVKGRFVIHRISAEEAKYKLCKVKKTQLGAKGVPFLVTHDGRTIRYPDPLIHANDSVQVDIASGKITDYIKFDSGNLCMITGGRNLGRVGTVVNRERHPGSFDIVHIKDSQGHVFATRLTNVFIIGKGNKPYISLPKGKGVKLSIAEERDKRLAAKTH
Protein: Ethylene-responsive transcription factor RAP2-2 (AtRAP2.2) (Protein RELATED TO APETALA2 2) (Q9LUM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in carotenoid biosynthesis regulation. Binds to the 5'-ATCTA-3' element present in the promoter of phytoene synthase (PSY) and phytoene desaturase (PDS). Involved in ethylene response and resistance to necrotrophic pathogens. Acts as a downstream regulator in the ethylene signaling pathway. Partially redundant with RAP2-12.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase SINAT2
- E3 ubiquitin-protein ligase PRT6
- Phytoene synthase 1, chloroplastic
- Arginyl-tRNA--protein transferase 2
- Pyruvate decarboxylase 1
- Plant cysteine oxidase 1
- Alcohol dehydrogenase class-P
- Sequence-specific DNA binding transcription factor
- Plant cysteine oxidase 4
- Pyruvate decarboxylase 2
Sequence:
MCGGAIISDFIPPPRSLRVTNEFIWPDLKNKVKASKKRSNKRSDFFDLDDDFEADFQGFKDDSAFDCEDDDDVFVNVKPFVFTATTKPVASAFVSTGIYLVGSAYAKKTVESAEQAEKSSKRKRKNQYRGIRQRPWGKWAAEIRDPRKGSREWLGTFDTAEEAARAYDAAARRIRGTKAKVNFPEEKNPSVVSQKRPSAKTNNLQKSVAKPNKSVTLVQQPTHLSQQYCNNSFDNSFGDMSFMEEKPQMYNNQFGLTNSFDAGGNNGYQYFSSDQGSNSFDCSEFGWSDHGPKTPEISSMLVNNNEASFVEETNAAKKLKPNSDESDDLMAYLDNALWDTPLEVEAMLGADAGAVTQEEENPVELWSLDEINFMLEGDF
Protein: Protein KRI1 homolog (A0A494C108)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHRTAMPEPRGSSQLRVNAAFAARYNRYREREELQRLKDRYGDRDSSSDSSSESDSSDERVEFDPQQERDFYKTLSLLKKKDPRIYQKDATFYNRTASSSDSEEDPEALEKQKKVRPMYLKDYERKVILEKAGKYVDEENSDGETSNHRLQETSSQSYVEEQKQLKESFRAFVEDSEDEDGAGEGGSSLLQKRAKTRQEKAQEEADYIEWLKGQKEIRNPDSLKELTHLKEYWNDPELDEGERFLRDYILNKRYEEEEEEEEDEEEMEEEEGVHGPPVQLAVDDSSDEGELFLKKQEDFEQKYNFRFEEPDSASVKTYPRSIASSVRRKDERRKEKREETRERKKREKAKKQEELKQLKNLKRKEILAKLEKLRKVTGNEMLGLEEGDLEDDFDPAQHDQLMQKCFGDEYYGAVEEEKPQFEEEEGLEDDWNWDTWDGPEQEGDWSQQELHCEDPNFNMDADYDPSQPRKKKREAPLTGKKKRKSPFAAAVGQEKPVFEPGDKTFEEYLDEYYRLDYEDIIDDLPCRFKYRTVVPCDFGLSTEEILAADDKELNRWCSLKKTCMYRSEQEELRDKRAYSQKAQNSWKKRQVFKSLCREEAETPAEATGKPQRDEAGPQRQLPALDGSLMGPESPPAQEEEAPVSPHKKPAPQKRRRAKKARLLGPTVMLGGCEFSRQRLQAFGLNPKRLHFRQLGRQRRKQQGPKNSS
Protein: V-type proton ATPase subunit B (V-ATPase subunit B) (Vacuolar proton pump subunit B) (Q76NU1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The B subunit is non-catalytic but combines with other subunits to form the catalytic complex. V-ATPase is responsible for energizing electrophoretic K(+)/2H(+) antiport by generating a transmembrane voltage of more than 200 mV (By similarity).
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Contractile vacuole membrane; Peripheral membrane protein; Cytoplasmic side. Note=Detected on macropinosomes and phagosomes, on contractile vacuoles, cytoplasmic cisternae and on the tubular extensions linking these vesicles.
Interaction partners:
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit F
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d
- V-type proton ATPase subunit C
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit E
- V-type proton ATPase subunit H
- V-type proton ATPase subunit G
Sequence:
MVGFEDHIAAITRNYQVNPRLDYRTVTAVNGPLVILDNIRGPKFSEIVTLTLGDGTQRKGQVLEIQGKRAVVQVFEGTIGIDAKHTRCEFSGDILKMPVSEDSLGRIFNGSGKPVDKGPNVLAEEYLDIQGQPINPSVRVYPQEMIQTGISAIDTMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSGKGVIDDHEDNFAIVFAAMGVNMETASFFKRDFEESGSMDRTALFLNLADHPTIERIITPRLALTTAEYLAYQCEKHVLVLLTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRIQGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFIDRQINNRQIYPPINVLPSLSRLMKSAIGDDMTRGDHSEVSNQMYANYAIGKDVQAMKAVVGEEALSSEDKLYLEFLERFESSFVGQNHYENRDIFNSLDLGWSLLRTFPSNLLKRITEKTIKQYYSRSSKGTVDSTN
Protein: Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit) (Q03147)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P50613}. Cytoplasm {ECO:0000250|UniProtKB:P50613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50613}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (By similarity). {ECO:0000250|UniProtKB:P50613}.
Interaction partners:
- CDK-activating kinase assembly factor MAT1
- Cyclin-H
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 3
- General transcription factor IIH subunit 1
- DNA-directed RNA polymerase II subunit RPB1
- General transcription factor IIH subunit 4
- TATA-box-binding protein
- General transcription factor IIH subunit 5
Sequence:
MAVDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGVPLQHIFIAAGDDLLELIQGLFLFNPCTRTTASQALKTKYFSNRPGPTPGCQLPRPNCPVEALKEPANPTVATKRKRAEALEQGILPKKLIF
Protein: DUF21 domain-containing protein At1g55930, chloroplastic (CBS domain-containing protein CBSDUFCH2) (Q84R21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELDLSVLGRSFIVTRRNSSITRPCIQSSNFSVRVLQRNKHRPLCFSTNPSNSSFIRFQKGCDFSHRCQFVVLSATGDHVGISQKHSDSTEKVDSIRILLKRGIVLGAVVCGVLFYGCGKVLASTSVVDVAFSKSILLLKNAWPKTSQVLKVLREQGLILAVLLGLSAFFSMAETSITTLWPWKVRELAEKEPENGVFRMLRSDVTRFLTTILIGTTVVNIAATALVTKAATAIFGEAGVSAATGVMTVAILLLTEITPKSVAVHNAQEVARIVVRPVAWLSLILYPVGRVVTYLSMGILKILGLKGRSEPYVTEDELKLMLRGAELSGAIEEEEQDMIENVLEIKDTHVREVMTPLVDVVAIDGSGSLVDFHNFWVTHQYSRVPVFEQRIDNIVGIAYAMDLLDYVPKGKLLESTTVVDMAHKPAFFVPDSMSVWNLLREFRIRKVHMAVVLNEYGGTIGIVTLEDVVEEIVGEIFDENDSKEEIQKKTGYIVMRAEGIYDVDANTSIDQLSEELNIKMAEGHQYETVSGFVCEAFGYIPKTGESVTVVLEKENWEENDEQDEGKHERQDQKEKHQIYRLEILAGNARKVSAVRFERVSDMDQVSEARDVKNMVPKFVRKWSSEEDSDGNLQAKNAVFDEHLIAETESMKKE
Protein: ATP-binding protein (P72163)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MGQIRVSGLGKAYKQYPNRWSRLFEWLVPFSPPRHHLHWILREVEFTIEPGEAVGIVGVNGAGKSTLLKMIAGTTQPTCGEIRVAGRVAALLELGMGFHPDFTGRQNVFMAGQLLGMQVEEIQALMPDIEAFAEIGEAIEQPVRTYSSGMQMRLAFSVATARRPDILIVDEALSVGDAYFQHKSFERIRSFRKAGTTLLIVSHDRSAIQSICDSAILLEQGRMAMRGRPEEVMDYYNALLAEREGQTVRQEMLADGQVRTISGTGEAAILDVRMVDQRQRALEVVEVGQAVTLEVEVEVRQDIERLILGFMIKDRLGQPMYGINTHRLDKALTDLKAGERITYRFAFDMRLGKGHYSVALSLSRLDSHLDRNFEWRDYGLVFHVINNRQEDFVGCSWLGAETHISRSGEAALDPTSAESTP
Protein: BILBO1 N-terminal domain-containing protein (Q38B39)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYPLLVCADLYGEKYNLEVRFPSKPTIEDLQKRIVTVFSTEMDSRRPEGYPEADFSIALVHIYDDKSQQWEKLLSDAQLHEYDQLYVFQPQTRWHMDVQKNLPPPTTPSKDHRTATPHSICKSPQSKGCDDVYSFSQNCEATVTAKTRLEEQRRRERVLREELFRVREETERLEREAALELSRKRLLKWQVMYTSTSHKETSGIYMASMCNYPPLGECLYTVDAPKPVSPGR
Protein: Uncharacterized protein YcdU (P75910)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Recombination-promoting nuclease RpnB
- Glyoxylate/hydroxypyruvate reductase A
Sequence:
MIPDYLTFIRFQDKRNLIYIYAIGLILIGFYWKNAGFTFPSEDIGVVSGILALVLYNFIFDLKAYWAYKCVTKNIDFSWFKKKQNHKIELFLTQPLVAGFLSLIMLSAMSWGLYQLLPSLYALFLISLLGPLVIFLLFRMIRTSYVKQVAISVAKKVKYKSLTRYVLLSVCISTVVNLLTISPLRNSDSFVTEGQWLTFKSIIALLILCGVVLAINLFFLRFSKRYAFLGRLFLQEIDLFFSSENALSTFFAKPLWLRLFILLVIEVMWITLVSVLATLVEWRIWFEAYFLLCYVPCLIYYFFYCRFLWHNDFMMACDMYFRWGHFNK
Protein: Calcium homeostasis modulator protein 3 (Protein A) (Q86XJ0)
Organism: Homo sapiens (Human)
Function: Pore-forming subunit of a voltage-gated ion channel, also permeable to larger molecules including ATP. Together with CALHM1, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs). CALHM1-CALHM3-mediated ATP released acts as a neurotransmitter to gustatory neurons in response to GPCR-mediated tastes, including sweet, bitter and umami substances.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:J3QMI4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium homeostasis modulator protein 1
Sequence:
MDKFRMLFQHFQSSSESVMNGICLLLAAVTVKLYSSFDFNCPCLVHYNALYGLGLLLTPPLALFLCGLLANRQSVVMVEEWRRPAGHRRKDPGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSSSVDPEKFLDFANMTPSQVQLFLAKVPCKEDELVRDSPARKAVSRYLRCLSQAIGWSVTLLLIIAAFLARCLRPCFDQTVFLQRRYWSNYVDLEQKLFDETCCEHARDFAHRCVLHFFASMRSELQARGLRRGNAGRRLELPAVPEPPEGLDSGSGKAHLRAISSREQVDRLLSTWYSSKPPLDLAASPGLCGGGLSHRAPTLALGTRLSQHTDV
Protein: Probable citrate synthase, mitochondrial (EC 2.3.3.16) (P34575)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Probable aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Bifunctional glyoxylate cycle protein
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Acetyl-coenzyme A synthetase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate carboxylase 1
- ATP-citrate synthase
- Probable ATP-citrate synthase
Sequence:
MSLSGMAIRRLITKGVIPVCQVAPLSTSAEGSTNLKEVLSKKIPAHNAKVKSFRTEHGSTVVQNVNIDMIYGGMRSMKGMVTETSVLDPEEGIRFRGYSIPECQKLLPKAKGGEEPLPEAIWWLLCTGDVPSEAQTAAITKEWNARADLPTHVVRMLDNFPDNLHPMAQFIAAIAALNNESKFAGAYARGVAKASYWEYAYEDSMDLLAKLPTVAAIIYRNLYRDGSAVSVIDPKKDWSANFSSMLGYDDPLFAELMRLYLVIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMAGLAGPLHGLANQEVLVFLNKIVGEIGFNYTEEQLKEWVWKHLKSGQVVPGYGHAVLRKTDPRYECQREFALKHLPNDDLFKLVSTLYKITPGILLEQGKAKNPWPNVDSHSGVLLQYFGMTEMSFYTVLFGVSRALGCLSQLIWARGMGLPLERPKSHSTDGLIKLALAAKK
Protein: Cadherin-related family member 5 (GP100) (Mu-protocadherin) (Q9JIK1)
Organism: Rattus norvegicus (Rat)
Function: Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR2 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9HBB8}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9HBB8}.
Interaction partners:
- Cadherin-related family member 2
- Cadherin-23
Sequence:
MGAPALLWPPLLLPLLTVLFGHLPGTLAQAQVCSANQTVFTMNENTTVSGPLADIFVPEDQYVTLGQLSTPNAFKVEGNKLFLIVTPDYEENSLLEAVLECKRGDTLVTQFRVFVAVLDINDNAPEFPFTIKEYNVSEDTRVNTIVIPETELKATDADKDDILVYTLQEVTPNASKFFSLVGINSPALKLDQTLDYYKSPNMTFRLLARDTREENVIPSHTATATVVLNVLPADLRTPWFLPCSFTDDYFCIQAQYHTVIPTGHKLPSPLILSPGPIYAVDGDQAINQPIVYSIMMGNTDDTFIINKDDGNLTMAKSIPSPMTFTLVVRAEQADMARYSVTQAVVEARDVTGNPLQFSQSLYFGTVVLGSEAGTAVKDKTFPSEILRIQAQYLGFPDLNSAVTYQVTNSSEFIMNKDILLTTVPMETERTIRIEVEANNTVTKDIATTIVEIQVSEREPPSTESPTPPEAGGTTGPSSNTTLETPSTSGTSQGPATTSSGGSAGPFPPAGTTLSPLTSAPTVPGGSPTLGISTSPQTATPGGDATQTPKPGTSQPMVPTPGASTSSQPATPSGSSTQTPKPGTSQPMVPTPGASTSSQPATPSGSSTQTPRPGTSQPMVPTPGASTSSQPATPSGSTQTPKPGTSQPTTTGPISGVGELGDGQRFSTVDMAVLGGVLGALLLLALIFLIILIHKHYRHRFTCCSGKAKEPQPSGYDNLTFLPDNKAKWSPTSNRKPEPGPEPVQPPLRPPSPMSSSPTPPSSMPPSPQPKASGSPKTVQAGDSPSAVRSILTKERRPEGEGGYKAVWFGKDIGAEADVVVLNEPTADVDSASASGSEGSDDDDDPDQKKSLRLGAVADNTYV
Protein: Beta-ketoacyl-[acyl-carrier-protein] synthase FabY (Beta-ketoacyl-ACP synthase) (KAS) (EC 2.3.1.180) (Beta-ketoacyl synthase KAS I/II domain-containing enzyme) (Q9HU15)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the initiation of the fatty acid biosynthesis. Catalyzes the condensation of acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis (FAS) primer beta-acetoacetyl-ACP. It can also use short-chain acyl-CoA as substrates, including butyryl-CoA, and hexanoyl-CoA, but does not use any of the longer chain acyl-CoA substrates.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- Biotin carboxylase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Biotin carboxylase
Sequence:
MSRLPVIVGFGGYNAAGRSSFHHGFRRMVIESMDPQARQETLAGLAVMMKLVKAEGGRYLAEDGTPLSPEDIERRYAERIFASTLVRRIEPQYLDPDAVHWHKVLELSPAEGQALTFKASPKQLPEPLPANWSIAPAEDGEVLVSIHERCEFKVDSYRALTVKSAGQLPTGFEPGELYNSRFHPRGLQMSVVAATDAIRSTGIDWKTIVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLGFNSMPTDFINAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEEGLRLIEGRDDVDFRRASRPFGENCGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYLTVAKAVASAVQIVGLDTVRHASFVHAHGSSTPANRVTESEILDRVASAFGIDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKVADDVHQQRLSISNRDMRQDKPLEVCFINSKGFGGNNASGVVLSPRIAEKMLRKRHGQAAFAAYVEKREQTRAAARAYDQRALQGDLEIIYNFGQDLIDEHAIEVSAEQVTVPGFSQPLVYKKDARFSDMLD
Protein: Histone deacetylase (EC 3.5.1.98) (E5RQ38)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
- Nuclear receptor corepressor 2
- Histone deacetylase 1
- Core histone macro-H2A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Histone H2A
- Core histone macro-H2A.1
- Histone H2A.Z
- Histone H2B type 1
- Histone H2B
- Histone H2B
Sequence:
MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDTKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASVLPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLSASNSLKDKQKCETQMLRQGVPLPGQYGSGIAASSSHAHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMEERATSKDSGTGKDSSACVEDTLGQVGAVKVKEEPVDSDEDAQMQEMECGEQAAFMQQTPLLESSHTRALSVHQARLAAAGIDGLEKHGLLSRTHSSPAPSMSPHPAADCPRQPASATGIAYDCLMLKHQCICGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLGDDSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEACINALLGNEPGSLEEDVLHQSVNTNAAASLQKTIEIQSKYWKSIKMVAVARGCALPASQLQEETETVSALASLTVDVEQPFAQEDGRTAGEPMEEEPAL
Protein: Calicin (Q13939)
Organism: Homo sapiens (Human)
Function: Possible morphogenetic cytoskeletal element in spermiogenic differentiation.
Subcellular location: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000269|PubMed:36527329, ECO:0000269|PubMed:36546111}.
Interaction partners:
- Cylicin-2
- Cylicin-1
Sequence:
MKLEFTEKNYNSFVLQNLNRQRKRKEYWDMALSVDNHVFFAHRNVLAAVSPLVRSLISSNDMKTADELFITIDTSYLSPVTVDQLLDYFYSGKVVISEQNVEELLRGAQYFNTPRLRVHCNDFLIKSICRANCLRYLFLAELFELKEVSDVAYSGIRDNFHYWASPEGSMHFMRCPPVIFGRLLRDENLHVLNEDQALSALINWVYFRKEDREKYFKKFFNYINLNAVSNKTLVFASNKLVGMENTSSHTTLIESVLMDRKQERPCSLLVYQRKGALLDSVVILGGQKAHGQFNDGVFAYIIQENLWMKLSDMPYRAAALSATSAGRYIYISGGTTEQISGLKTAWRYDMDDNSWTKLPDLPIGLVFHTMVTCGGTVYSVGGSIAPRRYVSNIYRYDERKEVWCLAGKMSIPMDGTAVITKGDRHLYIVTGRCLVKGYISRVGVVDCFDTSTGDVVQCITFPIEFNHRPLLSFQQDNILCVHSHRQSVEINLQKVKASKTTTSVPVLPNSCPLDVSHAICSIGDSKVFVCGGVTTASDVQTKDYTINPNAFLLDQKTGKWKTLAPPPEALDCPACCLAKLPCKILQRI
Protein: Denticleless protein homolog (Q6P1W0)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), KMT5A and SDE2. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis. May play a role in the regulation of the circadian clock (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NZJ0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Damage specific DNA binding protein 1.
- Sugar phosphate transporter domain-containing protein
- Chromatin licensing and DNA replication factor 1.
- Kelch-like protein 21
- DNL-type zinc finger
- Proliferating cell nuclear antigen
- Cell division cycle 45.
- Protein MCM10 homolog
- Ubiquitin-fold modifier conjugating enzyme 1.
- Origin recognition complex subunit 1
Sequence:
MLFRSVVNKPRLGCRQRGVPFTHPLQSLLQCYQCAKHDEHTSYGELGAAVPPFGCAFSTVPDMSHVLAVANEEGIVRLYDTECRDVQRLVVKEFMAHTNAVFDIAWVPGEHKLVTASGDQTAKLWDVKAGDLIGECKGHQCSLKSVAFSKFEKAVFSTGGRDGNIMVWDTRCNKKDGFYRQVNQITGAHNALDKQTPSKVKKRKPYVRGLAPSVDSQQSVTVVIFQDEHTIISAGAVDGIVKVWDLRKNYSAYRQDPVPAKLFPYPGNSTRKLGYSNLVLDPTGTNLFASCTDDNVYMFNATGLKTEPVSVFGGHQNSTFYIKTSVSPDGQFLLSGSSDHSAYIWQVSDPKVPPVTLTGHCQEVTSVAWCQSDFTKIATCSDDNTVRVWRLKRSSEDSAQSDKTETVGWACQKKCVPPSMAANLCTPGKPSMIPSSSLMSSPTPATCAPSYTGDLPMPSSTPVSALLPIPKLQTPQRLNGEGLGASPKQTSSSKISIKDWITRTPKSSTRADTKTPSPRKAFTPVEQYPSVSSTRVQMPYEKRAKRRLETSSEDVEHVCLDHCNCVMELEPGLKKAKLDLCSFSEKERDGSDDKCLRLSDLSRGFDQEFSPGPSTSFLINGTVNPPLSPLSELKSDLRDKENSSPEKNWLSALGHKFKSDKSSPQNKAASSPSSRNSTSKKHPTRNAPNSPVSVPTTPGSMRKICTYFFKKSE
Protein: Nuclear transport factor 2 domain protein, putative (AFU_orthologue AFUA_4G07835) (Q5B6G6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- mRNA export factor MEX67
- Nucleoporin NSP1
- Nuclear pore complex protein An-Nup57
- WD40 repeat protein poxJ
- Nuclear transport factor 2
- Nuclear pore complex protein An-Nup159
- Peptidase S59 domain-containing protein
- ATP-dependent RNA helicase sub2
- mRNA export factor GLE1
Sequence:
MAPTEDAYAKVSTEAATEFVQSFYPALQSNRATIASFYSSPPSTIVFNGNPVADGNAVQEIFVSQMPPTHYEVQSFDCQIINKQYPTATIGRQIDPRKDISILVVVSGYVRFGESRDLPQRGFSETFVLVPNPSSEGGKGKRRRDWLIQTQNFRLVV
Protein: Evasin P1074 (A0A0K8RDH6)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAFNMITFLQMAVFVVILFNINLHSASAGSKESSAHQSSDDSIKAEFCDAKCTMKTDGKWTQCHGGCFCVHVGNETEGRCMRLDGDYDYPSTQPEE
Protein: Transport protein particle (TRAPP) complex subunit TRS33, putative (Eurofung) (C8V0H5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2/Sedlin, putative
- Hypercellular protein A
- TMEM1 family protein, putative
- PutativeTRAPP
- Trafficking protein particle complex subunit
- GTP-binding protein ypt1
- Trafficking protein particle complex subunit 11 domain-containing protein
- DUF974 domain protein
Sequence:
MSFDAAGIHPIPSNSQDRLLSASCLDFLLIELVPMAERIAKDLAADERLLDDEETKETAFSRLESLGYRVGQGLAERFSRDRPRFTDNLDVIKFLCKDLWMTLFKKQIDNLKTNHRGVYVLTDNSFRPFAKMSMSSRNEALSRAQAYLWFPCGVIRGALSNLGIHTTVQAETTELPGATFQVKTINK