wanglab/gogpt-training-data huggingface dataset:
Protein: HTH-type transcriptional regulator KdgR (P76268)
Organism: Escherichia coli (strain K12)
Function: Transcriptional repressor that negatively regulates the expression of kdgT, kdgK and kdgA, which encode proteins involved in transport and catabolism of 2-keto-3-deoxygluconate (KDG). Also represses expression of eda, which encodes the Entner-Doudoroff aldolase, by binding to its P2 promoter region.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 2-keto-3-deoxygluconate permease
- 2-dehydro-3-deoxygluconokinase
- Ribosomal RNA small subunit methyltransferase B
Sequence:
MANADLDKQPDSVSSVLKVFGILQALGEEREIGITELSQRVMMSKSTVYRFLQTMKTLGYVAQEGESEKYSLTLKLFELGARALQNVDLIRSADIQMRELSRLTKETIHLGALDEDSIVYIHKIDSMYNLRMYSRIGRRNPLYSTAIGKVLLAWRDRDEVKQILEGVEYKRSTERTITSTEALLPVLDQVREQGYGEDNEEQEEGLRCIAVPVFDRFGVVIAGLSISFPTLRFSEERLQEYVAMLHTAARKISAQMGYHDYPF
Protein: Selenide, water dikinase (EC 2.7.9.3) (Selenium donor protein) (Selenophosphate synthase) (Q94497)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Synthesizes selenophosphate from selenide and ATP.
Interaction partners:
- O-phosphoseryl-tRNA
- Probable cysteine desulfurase, mitochondrial
- Thioredoxin reductase
- Small ribosomal subunit protein eS24
- Molybdenum cofactor sulfurase
- Prokaryotic-type class I peptide chain release factors domain-containing protein
- Tr-type G domain-containing protein
Sequence:
MSISIKDKKEELLCRLTDFTKLKGUGCKVPQAELLSLLDGIGEGIGYDCSISQTKFPDIVMIQTTDFFFPLVDDPYFQGKIACANVLSDLYSFGIEDCDNMLMLLACSTDMTAEQRQWSSKLMIQGFNDQAICAGSKVSGGQTVKNPWPIVGGVATSILKTNEFIKPVNAVPGDVLVLTKPLGTQVCVNFHQWLSKPERWEKINTITNAEECEQVFNYATLSMARLNRVGARLMKKYNAHAATDVTGFGILGHSTNLAQNQLLPIRFEIHTLPIIKHMKKLEDHLNHPFKLLKGTSAETSGGLLISMSRENAEAFCKEIYEIEKQPAWIIGDVIDQSSNYDRSKNTSIILENPKIIEVEPNTNF
Protein: Keratin, type II cuticular Hb3 (Hair keratin K2.10) (Keratin-83) (K83) (Type II hair keratin Hb3) (Type-II keratin Kb23) (P78385)
Organism: Homo sapiens (Human)
Interaction partners:
- Desmoglein-4
- Keratin-associated protein 3-3
Sequence:
MTCGFNSIGCGFRPGNFSCVSACGPRPSRCCITAAPYRGISCYRGLTGGFGSHSVCGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRECCQSNLEPLFAGYIETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRILQSHISDTSVVVKLDNSRDLNMDCIVAEIKAQYDDIATRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRLCEGVEAVNVCVSSSRGGVVCGDLCVSGSRPVTGSVCSAPCNGNLVVSTGLCKPCGQLNTTCGGGSCGQGRH
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta) (RNA polymerase subunit beta) (P0C501)
Organism: Oryza sativa (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MLRNGNEGMSTIPGFSQIQFEGFCRFINQGLAEELEKFPTIKDPDHEISFQLFAKGYQLLEPSIKERDAVYESLTYSSELYVSARLIFGFDVQKQTISIGNIPIMNSLGTFIINGIYRIVINQILLSPGIYYRSELDHKGISIYTGTIISDWGGRSELAIDKKERIWARVSRKQKISILVLSSAMGSNLKEILDNVSYPEIFLSFPNAKEKKRIESKEKAILEFYQQFACVGGDLVFSESLCEELQKKFFQQKCELGRIGRRNMNRRLNLDIPQNSTFLLPRDVLAATDHLIGMKFETGILDDDDMNHLKNKRIRSVADLLQDQFGLALGRLQHAVQKTIRRVFIRQSKPTPQTLVTPTSTSILLITTYETFFGTYPLSQVFDQTNPLTQTVHGRKVSCLGPGGLTGRTASFRSRDIHPSHYGRICPIDTSEGINVGLTGSLAIHARIDHWWGSVESPFYEISEKAKKKKERQVVYLSPNRDEYYMIAAGNSLSLNRGIQEEQVVPARYRQEFLTIAWEQIHVRSIFPFQYFSIGGSLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQTALDSRVSVIAEREGKIISTNSHKILLSSSGKTISIPLVTHRRSNKNTCMHQKPRVPRGKSIKKGQILAEGAATVGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTDTTSQGSAEKITKEIPHLEEHLLRNLDRNGVVKLGSWVETGDILVGKLTPQIASESSYIAEAGLLRAIFGLEVSTSKETSLKLPIGGRGRVIDVKWIQRDPLDIMVRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGTPVDMVFNPLGVPSRMNVGQIFESSLGLAGDLLKKHYRIAPFDERYEQEASRKLVFSELYEASKQTKNPWVFEPEYPGKSRIFDGRTGDPFEQPVLIGKSYILKLIHQVDEKIHGRSTGPYSLVTQQPVRGRAKQGGQRIGEMEVWALEGFGVAHILQEILTYKSDHLIARQEILNATIWGKRVPNHEDPPESFRVLVRELRSLALELNHFLVSQKNFQVNREEV
Protein: Sun domain-containing protein 1 (Q20924)
Organism: Caenorhabditis elegans
Function: Involved in centrosome attachment to the nucleus. Required for zyg-12 localization to the nuclear envelope. Together with pot-1, it is required to anchor telomeres to the nuclear envelope in embryos.
Subcellular location: Nucleus membrane {ECO:0000305|PubMed:14697201}; Single-pass membrane protein {ECO:0000305|PubMed:14697201}. Nucleus envelope {ECO:0000269|PubMed:24297748}.
Interaction partners:
- Zygote defective protein 12
- Nuclear migration and anchoring protein unc-84
- Transmembrane protein 201 homolog
- Serine/threonine-protein kinase plk-2
- Lamin-1
- C2H2-type domain-containing protein
- Nuclear migration protein unc-83
- HORMA domain-containing protein
- C2H2-type domain-containing protein
- HORMA domain-containing protein
Sequence:
MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYKEITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFHQTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTPEKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVLSPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQEQFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA
Protein: Putative allantoin permease (Allantoin transport protein) (Allantoin transporter) (P75712)
Organism: Escherichia coli (strain K12)
Function: Uptake of allantoin into the cell.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Allantoinase
- Putative purine permease YbbY
- Allantoate amidohydrolase
- (S)-ureidoglycine aminohydrolase (UGHY) (UGlyAH)
- Glycerate 3-kinase
- Uncharacterized fimbrial-like protein SfmH
- Uncharacterized protein YggM
- Type 1 fimbrin D-mannose specific adhesin
- Hydroxypyruvate isomerase
Sequence:
MEHQRKLFQQRGYSEDLLPKTQSQRTWKTFNYFTLWMGSVHNVPNYVMVGGFFILGLSTFSIMLAIILSAFFIAAVMVLNGAAGSKYGVPFAMILRASYGVRGALFPGLLRGGIAAIMWFGLQCYAGSLACLILIGKIWPGFLTLGGDFTLLGLSLPGLITFLIFWLVNVGIGFGGGKVLNKFTAILNPCIYIVFGGMAIWAISLVGIGPIFDYIPSGIQKAENGGFLFLVVINAVVAVWAAPAVSASDFTQNAHSFREQALGQTLGLVVAYILFAVAGVCIIAGASIHYGADTWNVLDIVQRWDSLFASFFAVLVILMTTISTNATGNIIPAGYQIAAIAPTKLTYKNGVLIASIISLLICPWKLMENQDSIYLFLDIIGGMLGPVIGVMMAHYFVVMRGQINLDELYTAPGDYKYYDNGFNLTAFSVTLVAVILSLGGKFIHFMEPLSRVSWFVGVIVAFAAYALLKKRTTAEKTGEQKTIG
Protein: Bilobe protein, conserved (Q38BU4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPLPSTLPSPAPPSPPVATSKLDLDINGLQKILQQIDESFHASDDDVDRRLRLQHLERQQVALQQLCDAALQQQDGQAVPPALDNSTDVRPITYKVLDTDVVSTPRSIDAFNPSHNTRETLQSIARKTETCLRSPHAPLVAPPRLLSPSRVTSMPHMGAGTTAQGEVKTPDHAGVATAKIFPLRSPELPPTYHDGAAVQEDRDLVESFLGDGRAKAQHPYAVEEGGVHRVRGSTGGWQQRGIHTLRGVRSCRLMAPRMSSGTDRTASPEHFDIGEDEKLIRQLIGRNETRVKGSTNRNNHCFQTAPTKGENVAAHSCGTEGQIHRHSTVPSASGRQPAQGDAHPTSTSMAHNPHKEDCAARNGHWVRGKSVKELTQKMECLARHLVKCMRDRLQLQYRVDRLEGMLDVANTEVGRLRRTLEQREEGTLTESAWRATINAKERELRVCEDEIRRLRILVEQQVTRQGCGLARQNEAAALQQAKADLECMMQELGVAHMRRREMEEEFERTKQALDAAESHIQMLDKRLAQAERAAALARVWDVSGDLNVQVGDVPSAPASTALQKGLPEAKLKLQANVGNVDSWTHDAQREIARLTAHIENLALKHAESDRHAELRLSNARKESDVLRRQCNELRVEVRSHEVQIETLRRDRVAVGLREGQLRQQLLDLRDDAVLLADLLQATTKNAKGMLQILGTDDVEHRQSKAAVERFVAGVLCDFDALGRFFGALQCIDIGESRCQMEERVSVSEATAARRDFVLKAVEDAMERPSQGFGPATLSSSKPPCVETLQAAHESHRPSVAADCILATGTRPPEDRKPPTTSSTPSPAHPVLRWVADQNISLEGVTAPDEGNQPQNGAKMAESRASVMEGCTGRNLEQQSSNDFYALSGTNTDTEPKISLFPTTSWPSPQGARRGSPPSRLSDQAESHVLIQDSARSRISTGISFLSKAPDGSGTVASEGIPHLQQPLSHSMVSSQSHMVEETSDERSSGPMLSVVAATTRHVDTLSAQAVANRVDDVDLKGVTLELLRAEDRTSVKVHPAVSWNTGAENSAEKDGVGGEQTDLNDVPVTEVMRHLQPRDDSPENRKQTPPRLMPHYVVTHASSTATATREERSGAPVGRRPAVQQAADPAPLRRAVVGGGRDGRGRGRAVALAEPQRPTAARPGAALLPSVNDVGPEPRNNTVTATMVSGEAGTAHRHHLPVGTEFLSLRQPALANAQSKPKD
Protein: DNA damage-binding protein 2 (DDB p48 subunit) (DDBb) (Damage-specific DNA-binding protein 2) (UV-damaged DNA-binding protein 2) (UV-DDB 2) (Q92466)
Organism: Homo sapiens (Human)
Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR.
Subcellular location: Nucleus {ECO:0000269|PubMed:10777490, ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11705987, ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16713579, ECO:0000269|PubMed:17635991, ECO:0000269|PubMed:18593899}. Chromosome {ECO:0000269|PubMed:32789493}. Note=Accumulates at sites of DNA damage following UV irradiation. {ECO:0000269|PubMed:32789493}.
Interaction partners:
- Cullin-4A
- DNA damage-binding protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
- DNA repair protein complementing XP-A cells
- Ubiquitin carboxyl-terminal hydrolase 24
- DNA repair protein complementing XP-C cells
- DET1 homolog
- Denticleless protein homolog
- Cellular tumor antigen p53
Sequence:
MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDGARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHFQHLTPIKAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDVFDGNSGKMMCQLYDPESSGISSLNEFNPMGDTLASAMGYHILIWSQEEARTRK
Protein: Mitoferrin-1 (Mitochondrial iron transporter 1) (Protein frascati) (Solute carrier family 25 member 37) (Q287T7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:16511496}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family B member 10, mitochondrial
- Ferrochelatase
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Frataxin.
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- STEAP family member 3, metalloreductase.
- ATP-binding cassette sub-family B member 6
- Asparaginyl-tRNA synthetase 2
- Glutaredoxin-related protein 5, mitochondrial
- Coproporphyrinogen oxidase.
Sequence:
MELRTDAVLASLEMSEPVKNDEDYESLPAHASLGTHMTAGAVAGILEHTVMYPVDSVKTRMQSLQPDPKAQYRSVYGALKRIVRTEGLLRPLRGLNITVLGAGPAHALYFACYERIKRSLSDVIQNGGNSHIANGVAGSVATVLHDAVMNPAEVVKQRMQMYNSPYRSLYDCVLMVSRKEGLAAFYRSYSTQLTMNIPFQAVHFITYEFMQEHFNPHRQYRPETHIISGAAAGAVSAAVTTPLDVCKTLLNTQENVALSSAHVSGHLSGMVNALRTVYRLGGVPAFFKGIQARVIYQMPSTAIAWSVYEFFKYFLTQHESHVQEVSHKTSPT
Protein: Evasin P467 (L7M8Z8)
Organism: Rhipicephalus pulchellus (Yellow backed tick) (Dermacentor pulchellus)
Function: Salivary chemokine-binding protein which binds to host chemokines CCL1, CCL2, CCL3 and CCL5.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MALKACITVIAVVYVVQVVRGAEKSLDSDSSGEDYELWTQGCPFLVAENRTGFGTTVSCQHNCNGAIEKVPEGEPCYTIGEDGLGRMKLNLPYNCSLGECSGGVCVPNGRSDVCFKRTWEENNKAMA
Protein: Peptidoglycan-recognition protein SC1a (EC 3.5.1.28) (C0HK98)
Organism: Drosophila melanogaster (Fruit fly)
Function: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Gram-negative bacteria-binding protein 1
- Modular serine protease
- Peptidoglycan-recognition protein SA
- Peptidoglycan-recognition protein SC2
Sequence:
MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG
Protein: Protein rogdi homolog (Q4V7D2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000269|PubMed:29150638}. Cell projection, axon {ECO:0000269|PubMed:29150638}. Perikaryon {ECO:0000269|PubMed:29150638}. Cell projection, dendrite {ECO:0000269|PubMed:29150638}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:29150638}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000269|PubMed:29150638}.
Interaction partners:
- DmX-like protein 1
- Dmx-like 2
- S-phase kinase-associated protein 1
- WD repeat-containing protein 7
Sequence:
MATAMAASAAERAVLEEEFRWLLHAEVHAVLRQLQDILKEASLRFTLPGPSTEGPAKQENFILGSCGTDQVKGVLTLQGDALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFKTGAEVLKLMDAVMLQLTRARNRLTTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHTLQPTSTKNFRPAGGAVLHSPGAMFEWGSQRLEVSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSSRPF
Protein: Ephrin B3 (A5HTT2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
Protein: Phosphatidylinositol 4-phosphate 5-kinase its3 (EC 2.7.1.68) (1-phosphatidylinositol 4-phosphate kinase) (Diphosphoinositide kinase) (PIP5K) (PtdIns(4)P-5-kinase) (O13853)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved, together with the calcineurin ppb1, in cytokinesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10950958, ECO:0000269|PubMed:33172987, ECO:0000269|PubMed:39239853, ECO:0000269|PubMed:9873063}; Peripheral membrane protein {ECO:0000269|PubMed:9873063}. Note=Also localizes to the cell division site. {ECO:0000269|PubMed:33172987, ECO:0000269|PubMed:39239853, ECO:0000269|PubMed:9873063}.
Interaction partners:
- Phosphatidylinositol 4-kinase pik1
- Probable protein transport protein Sec61 subunit gamma
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Inositol-1,4,5-trisphosphate 5-phosphatase 1
- Phosphatidylinositol 4-kinase lsb6
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
- Uncharacterized protein C19F5.03
- Uncharacterized protein C3C7.01c
Sequence:
MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS
Protein: Ciliary microtubule inner protein 4 (Testis-expressed protein 33) (O43247)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9D9J2}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9D9J2}.
Interaction partners:
Sequence:
MELGHGAGTTTFTRAHLNDKEGQQDLDPWKAAYSSLDTSKFKNQGLSSPQPLPLGASAQGSSLGQCHLKEIPPPPPTAASRDSLGMDPQSRSLKNAGSRSSSRENRATSGEGAQPCQGTDDGPSLGAQDQRSTPTNQKGSIIPNNIRHKFGSNVVDQLVSEEQAQKAIDEVFEGQKRASSWPSRTQNPVEISSVFSDYYDLGYNMRSNLFRGAAEETKSLMKASYTPEVIEKSVRDLEHWHGRKTDDLGRWHQKNAMNLNLQKALEEKYGENSKSKSSKY
Protein: Coiled-coil domain-containing protein 83 (Q8IWF9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENSGKANKKDTHDGPPKEIKLPTSEALLDYQCQIKEDAVEQFMFQIKTLRKKNQKYHERNSRLKEEQIWHIRHLLKELSEEKAEGLPVVTREDVEEAMKEKWKFERDQEKNLRDMRMQISNAEKLFLEKLSEKEYWEEYKNVGSERHAKLITSLQNDINTVKENAEKMSEHYKITLEDTRKKIIKETLLQLDQKKEWATQNAVKLIDKGSYLEIWENDWLKKEVAIHRKEVEELKNAIHELEAENLVLIDQLSNCRLVDLKIPRRLYLTQAAGLEVPPEEMSLELPETHIEEKSELQPTEVESRDLMSSSDESTILHLSHENSIEDLQYVKIDKEENSGTEFGDTDMKYLLYEDEKDFKDYVNLGPLGVKLMSVESKKMPIHFQEKEIPVKLYKDVRSPESHITYKMMKSFL
Protein: Putative lipoate-protein ligase A (EC 6.3.1.20) (O13629)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Lipoyl synthase, mitochondrial
- Putative glycine cleavage system H protein, mitochondrial
- Probable octanoyltransferase
- Probable pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Pyridoxamine 5'-phosphate oxidase C1952.08c homolog
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Sequence:
MLEAVTNPKSSLATFSKQLNGLLQAKVVVCKSVNPYFNLALENYLYENSTAKHCLLLYTNSPSVIIGRNQNPWVEANVKLCRDNFVNIIRRKSGGGTVFHDFGNLNYSVLMNREEFSHTENASIMIQALRNLGVHARLNQRHDIVLAQSQRKISGSAYKISRNRCYHHGTMLLNSDLEGVREYLRSPSTGILSKGVSSTRSPVSNTKLLKAEFIKQVISCFLLHKSHSTTTKPLSKPRASSKRLYDIEPKSVITLEQNDLLGVPSILKAVNELQSWEWTFGQTPSFKQHLESTELSVSMDISVVHGRLEKVIFSTPNATLEHELSSIPWTGLCYESGFANTFLISGIHSKEAISILKWISDSI
Protein: Putative diacyglycerol O-acyltransferase Rv3371 (EC 2.3.1.20) (Putative triacylglycerol synthase Rv3371) (P9WKA9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis.
Interaction partners:
- Triacylglycerol lipase
- Diacylglycerol kinase
- Possible triacylglycerol synthase
- Possible multi-functional enzyme with acyl-CoA-reductase activity AcrA1
- Trehalose-phosphate phosphatase
Sequence:
MAQLTALDAGFLKSRDPERHPGLAIGAVAVVNGAAPSYDQLKTVLTERIKSIPRCTQVLATEWIDYPGFDLTQHVRRVALPRPGDEAELFRAIALALERPLDPDRPLWECWIIEGLNGNRWAILIKIHHCMAGAMSAAHLLARLCDDADGSAFANNVDIKQIPPYGDARSWAETLWRMSVSIAGAVCTAAARAVSWPAVTSPAGPVTTRRRYQAVRVPRDAVDAVCHKFGVTANDVALAAITEGFRTVLLHRGQQPRADSLRTLEKTDGSSAMLPYLPVEYDDPVRRLRTVHNRSQQSGRRQPDSLSDYTPLMLCAKMIHALARLPQQGIVTLATSAPRPRHQLRLMGQKMDQVLPIPPTALQLSTGIAVLSYGDELVFGITADYDAASEMQQLVNGIELGVARLVALSDDSVLLFTKDRRKRSSRALPSAARRGRPSVPTARARH
Protein: Serine hydroxymethyltransferase, mitochondrial (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Serine methylase) (Q9CZN7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis (By similarity). Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate (By similarity). Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism: thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (By similarity). Also required for mitochondrial translation by producing 5,10-methylenetetrahydrofolate; 5,10-methylenetetrahydrofolate providing methyl donors to produce the taurinomethyluridine base at the wobble position of some mitochondrial tRNAs. Associates with mitochondrial DNA (By similarity). In addition to its role in mitochondria, also plays a role in the deubiquitination of target proteins as component of the BRISC complex: required for IFNAR1 deubiquitination by the BRISC complex (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P34897}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:P34897}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P34897}. Cytoplasm {ECO:0000250|UniProtKB:P34897}. Nucleus {ECO:0000250|UniProtKB:P34897}. Note=Mainly localizes in the mitochondrion. Also found in the cytoplasm and nucleus as part of the BRISC complex. {ECO:0000250|UniProtKB:P34897}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Glycine dehydrogenase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Phosphoserine phosphatase
- Dihydrofolate reductase
- Methylenetetrahydrofolate reductase
Sequence:
MVSFSLLRTTRPLQRCGQLVCMAARAQHSKVAQTQAGEAAGGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPQTGLIDYDQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVRAHLLADMAHISGLVAAKVIPSPFKYADVVTTTTHKTLRGARSGLIFYRKGVRTVDPKTGKEIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLRNAQAMADALLKRGYSLVSGGTDTHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKRKTAKLQDFKSFLLKDPETSQRLANLRQQVEQFARGFPMPGFDER
Protein: T-lymphocyte activation antigen CD86 (Activation B7-2 antigen) (Early T-cell costimulatory molecule 1) (ETC-1) (CD antigen CD86) (P42082)
Organism: Mus musculus (Mouse)
Function: Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Also involved in the regulation of B cells function, plays a role in regulating the level of IgG(1) produced. Upon CD40 engagement, activates NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- T-cell-specific surface glycoprotein CD28
- T-lymphocyte activation antigen CD80
- Cytotoxic T-lymphocyte protein 4
- CD40 ligand
- Programmed cell death protein 1
- Inducible T-cell costimulator
- CD27 antigen
- Tumor necrosis factor receptor superfamily member 4
- CD276 antigen
- Programmed cell death 1 ligand 1
Sequence:
MDPRCTMGLAILIFVTVLLISDAVSVETQAYFNGTAYLPCPFTKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSVNAKYLGRTSFDRNNWTLRLHNVQIKDMGSYDCFIQKKPPTGSIILQQTLTELSVIANFSEPEIKLAQNVTGNSGINLTCTSKQGHPKPKKMYFLITNSTNEYGDNMQISQDNVTELFSISNSLSLSFPDGVWHMTVVCVLETESMKISSKPLNFTQEFPSPQTYWKEITASVTVALLLVMLLIIVCHKKPNQPSRPSNTASKLERDSNADRETINLKELEPQIASAKPNAE