wanglab/gogpt-training-data huggingface dataset:
Protein: Disintegrin and metalloproteinase domain-containing protein 20 (ADAM 20) (EC 3.4.24.-) (O43506)
Organism: Homo sapiens (Human)
Function: May be involved in sperm maturation and/or fertilization.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
- Disintegrin and metalloproteinase domain-containing protein 30
- Disintegrin and metalloproteinase domain-containing protein 21
Sequence:
MAVGEPLVHIRVTLLLLWFGMFLSISGHSQARPSQYFTSPEVVIPLKVISRGRGAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGYVEGVPESLVALSTCSGGFLGMLQINDLVYEIKPISVSATFEHLVYKIDSDDTQFPPMRCGLTEEKIAHQMELQLSYNFTLKQSSFVGWWTHQRFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPYPGNIFRLKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQDGISCNVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGVIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAIPDIGEVKDGTVCGPEKICIRKKCASMVHLSQACQPKTCNMRGICNNKQHCHCNHEWAPPYCKDKGYGGSADSGPPPKNNMEGLNVMGKLRYLSLLCLLPLVAFLLFCLHVLFKKRTKSKEDEEG
Protein: Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (mVDAC1) (Voltage-dependent anion-selective channel protein 5) (VDAC-5) (mVDAC5) (Q60932)
Organism: Mus musculus (Mouse)
Function: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol (By similarity). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. May mediate ATP export from cells (By similarity).
Subcellular location: [Isoform Mt-VDAC1]: Mitochondrion outer membrane {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}.; SUBCELLULAR LOCATION: [Isoform Pl-VDAC1]: Cell membrane {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}. Membrane raft {ECO:0000269|PubMed:25168729}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000250|UniProtKB:Q9Z2L0}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Stress-70 protein, mitochondrial
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Translocator protein
- Bcl-2-like protein 1
- Steroidogenic acute regulatory protein, mitochondrial
- Non-selective voltage-gated ion channel VDAC2
- ADP/ATP translocase 2
- Hexokinase-2
- Superoxide dismutase
Sequence:
MCSFFLVLLLWQNMAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVNGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETSKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQVDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA
Protein: Anamorsin homolog (Fe-S cluster assembly protein DRE2 homolog) (Q9V3Y2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}.
Interaction partners:
- LD40224p
- NADPH-dependent diflavin oxidoreductase 1
- GEO02273p1
- Glutaredoxin-related protein 5, mitochondrial
- BolA-like protein DDB_G0274169
- GH14121p
- MIP18 family protein galla-2
- Lipoyl synthase, mitochondrial
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- MMS19 nucleotide excision repair protein
Sequence:
MENFKGLQKSLYIWTDSADLDKRVEQLKAATGGDVALENVHRLSFSSYANSSFDLIVIECAQLTDSYVKLLHMLKPSGKLHLVSYIGPAASLLQEIKLSGFINCREDSPDALTAEKPGYETGSSARLSFAKKNASAVNVWKISGDDEELIDEEELLDEEDKQKPDPAGLRVCSTTGKRKACKNCSCGLAEELETEKQSQKATENAKSSCGNCYLGDAFRCSTCPYLGMPAFKPGEKVQLADNLLKSDI
Protein: Protein RecA (Recombinase A) (P0A452)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs (By similarity). It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similarity). Required for DNA transformation; protects transforming DNA from degradation, possibly in combination with DprA. Present at 15,000-30,000 monomers per competent cell.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- DNA processing protein DprA
- Putative competence-damage inducible protein
- Single-stranded DNA-binding protein
- DNA repair protein RadA
- DNA polymerase IV
- Single-stranded-DNA-specific exonuclease RecJ
- ATP-dependent DNA helicase RecG
- Regulatory protein RecX
- DNA-directed RNA polymerase subunit beta
Sequence:
MAKKPKKLEEISKKFGAEREKALNDALKLIEKDFGKGSIMRLGERAEQKVQVMSSGSLALDIALGSGGYPKGRIIEIYGPESSGKTTVALHAVAQAQKEGGIAAFIDAEHALDPAYAAALGVNIDELLLSQPDSGEQGLEIAGKLIDSGAVDLVVVDSVAALVPRAEIDGDIGDSHVGLQARMMSQAMRKLGASINKTKTIAIFINQLREKVGVMFGNPETTPGGRALKFYASVRLDVRGNTQIKGTGDQKETNVGKETKIKVVKNKVAPPFKEAVVEIMYGEGISKTGELLKIASDLDIIKKAGAWYSYKDEKIGQGSENAKKYLAEHPEIFDEIDKQVRSKFGLIDGEEVSEQDTENKKDEPKKEEAVNEEVPLDLGDELEIEIEE
Protein: DnaJ protein ERDJ3B (Chaperone protein dnaJ 19) (AtDjB19) (AtJ19) (Endoplasmic reticulum dnaJ domain-containing protein 3B) (AtERdj3B) (Protein SCJ1 homolog ERDJ3B) (Q9LZK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates protein folding in the endoplasmic reticulum (ER) lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305|PubMed:18718935}.
Interaction partners:
- Stromal cell-derived factor 2-like protein
- DnaJ protein P58IPK homolog
- Heat shock 70 kDa protein BIP3
- Heat shock 70 kDa protein BIP1
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Calreticulin-3
- UDP-glucose:glycoprotein glucosyltransferase
- bZIP transcription factor 28
Sequence:
MAIRWSELCIVLFALSYAICVLAGKSYYDVLQVPKGASDEQIKRAYRKLALKYHPDKNQGNEEATRKFAEINNAYEVLSDEEKREIYNKYGEEGLKQFSANGGRGGGGGGMNMQDIFSSFFGGGSMEEEEKVVKGDDVIVELEATLEDLYMGGSMKVWREKNVIKPAPGKRKCNCRNEVYHRQIGPGMFQQMTEQVCDKCPNVKYEREGYFVTVDIEKGMKDGEEVSFYEDGEPILDGDPGDLKFRIRTAPHARFRRDGNDLHMNVNITLVEALVGFEKSFKHLDDHEVDISSKGITKPKEVKKFKGEGMPLHYSTKKGNLFVTFEVLFPSSLTDDQKKKIKEVFA
Protein: Leucine-rich repeat receptor-like protein kinase PEPR2 (EC 2.7.11.1) (Elicitor peptide 1 receptor 2) (PEP1 receptor 2) (Q9FZ59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a receptor for PEP defense peptides. Unlike typical immune receptors, senses an endogenous elicitor that potentiates PAMP-inducible plant responses (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Precursor of elicitor peptide 1
- Elicitor peptide 3
- Elicitor peptide 2
- Elongation factor Tu, chloroplastic
- CLAVATA3/ESR
- PAMP-induced secreted peptide 1
- Elicitor peptide 7
- Elongation factor Tu
Sequence:
MRNLGLLEITLLCSLFVYFRIDSVSSLNSDGLALLSLLKHFDKVPLEVASTWKENTSETTPCNNNWFGVICDLSGNVVETLNLSASGLSGQLGSEIGELKSLVTLDLSLNSFSGLLPSTLGNCTSLEYLDLSNNDFSGEVPDIFGSLQNLTFLYLDRNNLSGLIPASVGGLIELVDLRMSYNNLSGTIPELLGNCSKLEYLALNNNKLNGSLPASLYLLENLGELFVSNNSLGGRLHFGSSNCKKLVSLDLSFNDFQGGVPPEIGNCSSLHSLVMVKCNLTGTIPSSMGMLRKVSVIDLSDNRLSGNIPQELGNCSSLETLKLNDNQLQGEIPPALSKLKKLQSLELFFNKLSGEIPIGIWKIQSLTQMLVYNNTLTGELPVEVTQLKHLKKLTLFNNGFYGDIPMSLGLNRSLEEVDLLGNRFTGEIPPHLCHGQKLRLFILGSNQLHGKIPASIRQCKTLERVRLEDNKLSGVLPEFPESLSLSYVNLGSNSFEGSIPRSLGSCKNLLTIDLSQNKLTGLIPPELGNLQSLGLLNLSHNYLEGPLPSQLSGCARLLYFDVGSNSLNGSIPSSFRSWKSLSTLVLSDNNFLGAIPQFLAELDRLSDLRIARNAFGGKIPSSVGLLKSLRYGLDLSANVFTGEIPTTLGALINLERLNISNNKLTGPLSVLQSLKSLNQVDVSYNQFTGPIPVNLLSNSSKFSGNPDLCIQASYSVSAIIRKEFKSCKGQVKLSTWKIALIAAGSSLSVLALLFALFLVLCRCKRGTKTEDANILAEEGLSLLLNKVLAATDNLDDKYIIGRGAHGVVYRASLGSGEEYAVKKLIFAEHIRANQNMKREIETIGLVRHRNLIRLERFWMRKEDGLMLYQYMPNGSLHDVLHRGNQGEAVLDWSARFNIALGISHGLAYLHHDCHPPIIHRDIKPENILMDSDMEPHIGDFGLARILDDSTVSTATVTGTTGYIAPENAYKTVRSKESDVYSYGVVLLELVTGKRALDRSFPEDINIVSWVRSVLSSYEDEDDTAGPIVDPKLVDELLDTKLREQAIQVTDLALRCTDKRPENRPSMRDVVKDLTDLESFVRSTSGSVH
Protein: Cyclin-Y (Cyclin fold protein 1) (Q8BGU5)
Organism: Mus musculus (Mouse)
Function: Positive regulatory subunit of the cyclin-dependent kinase CDK14/PFTK1. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway (By similarity). Recruits CDK16 to the plasma membrane (By similarity). Positive regulatory subunit of the cyclin-dependent kinase CDK16.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 14
- Cyclin-dependent kinase 16
- Cyclin-dependent kinase 15
Sequence:
MGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNMEFNPSDHPRASTIFLSKSQTDVREKRKSLFINHHPPGQTSRKYSSCSTIFLDDSTVSQPNLKYTIKCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLSRERAHKLEAISRLCEDKYKDLRKPMRKRSASADNLILPRWSPAIIS
Protein: Rhino (Q49BK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTSGMSKMDQKKGKNIKKTARKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIHSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPNWKFPEITKPFGVNRGLDLDEILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK
Protein: Geranylgeranyl pyrophosphate synthase, chloroplastic (GGPP synthase) (GGPS) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranyltranstransferase) (EC 2.5.1.10) (P80042)
Organism: Capsicum annuum (Capsicum pepper)
Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:1303794}.
Interaction partners:
Sequence:
MRSMNLVDLWAQQACLVFNQTLSYKSFNGFMKIPLKNSKINPKLNKKRPFSPLTVSAIATTKEDERIEAAQTEEPFNFKIYVTEKAISVNKALDEAIIVKEPHVIHEAMRYSLLAGGKRVRPMLCLAACELVGGNQENAMAAACAVEMIHTMSLIHDDLPCMDNDDLRRGKPTNHKIYGEDVAVLAGDSLLAFAFEHIVNSTAGVTPSRIVGAVAELAKSIGTEGLVAGQVADIKCTGNASVSLETLEFIHVHKTAALLESSVVLGAILGGGTNVEVEKLRRFARCIGLLFQVVDDILDVTKSSEELGKTAGKDLVVDKTTYPKLLGLEKAKEFAAELNREAKQQLEGFDSRKAAPLIALADYIAYRDN
Protein: Centrosomal protein POC5 (Protein of centriole 5) (hPOC5) (Q8NA72)
Organism: Homo sapiens (Human)
Function: Essential for the assembly of the distal half of centrioles, required for centriole elongation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:37934472}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19349582, ECO:0000269|PubMed:32110738, ECO:0000269|PubMed:32946374, ECO:0000269|PubMed:37934472}. Note=Localized to the distal portion of centrioles. Localizes to the inner scaffold in the central region of centrioles. {ECO:0000269|PubMed:32110738, ECO:0000269|PubMed:37934472}.
Interaction partners:
- POC1 centriolar protein homolog B
- Centrin-2
- Centrin-3
- Protein FAM161A
- Centrin-1
- WD repeat-containing protein 90
- Spindle assembly abnormal protein 6 homolog
- WD repeat-containing protein 53
- Centrosomal protein of 135 kDa
- Centrosomal protein of 120 kDa
Sequence:
MSSDEEKYSLPVVQNDSSRGSSVSSNLQEEYEELLHYAIVTPNIEPCASQSSHPKGELVPDVRISTIHDILHSQGNNSEVRETAIEVGKGCDFHISSHSKTDESSPVLSPRKPSHPVMDFFSSHLLADSSSPATNSSHTDAHEILVSDFLVSDENLQKMENVLDLWSSGLKTNIISELSKWRLNFIDWHRMEMRKEKEKHAAHLKQLCNQINELKELQKTFEISIGRKDEVISSLSHAIGKQKEKIELMRTFFHWRIGHVRARQDVYEGKLADQYYQRTLLKKVWKVWRSVVQKQWKDVVERACQARAEEVCIQISNDYEAKVAMLSGALENAKAEIQRMQHEKEHFEDSMKKAFMRGVCALNLEAMTIFQNRNDAGIDSTNNKKEEYGPGVQGKEHSAHLDPSAPPMPLPVTSPLLPSPPAAVGGASATAVPSAASMTSTRAASASSVHVPVSALGAGSAATAASEEMYVPRVVTSAQQKAGRTITARITGRCDFASKNRISSSLAIMGVSPPMSSVVVEKHHPVTVQTIPQATAAKYPRTIHPESSTSASRSLGTRSAHTQSLTSVHSIKVVD
Protein: ATP-citrate synthase alpha chain protein 3 (ATP-citrate synthase A-3) (EC 2.3.3.8) (ATP-citrate lyase A-3) (Citrate cleavage enzyme A-3) (O80526)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- ATP-citrate synthase beta chain protein 1
- ATP-citrate synthase beta chain protein 2
- Citrate synthase 2, peroxisomal
- Citrate synthase 3, peroxisomal
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Citrate synthase 4, mitochondrial
- Citrate synthase 5, mitochondrial
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Citrate synthase 1, peroxisomal
- Aconitate hydratase 2, mitochondrial
Sequence:
MARKKIREYDSKRLLKEHLKRLANIDLQIRSAQVTESTDFTELTNQESWLSSTKLVVKPDMLFGKRGKSGLVALKLDLAEVADFVKARLGTEVEMEGCKAPITTFIVEPFVPHDQEYYLSIVSDRLGCTISFSECGGIEIEENWDKVKTIFLPAEKSMTLEVCAPLIATLPLEVRAKIGNFIMGAFAVFQDLDFSFMEMNPFTLVDGEPFPLDMRGELDDTAAFKNFNKWGDIEFPLPFGRVLSSTENFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYARVVIDCATTDPDGRKRALLIGGGIANFTDVAATFNGIIRALREKETRLKASRMHIYVRRGGPNYQTGLARMRALGEELGVPLEVYGPEATMTGICKRAIDCIMLPDA
Protein: Vomeronasal type-2 receptor 1 (Putative pheromone receptor V2R1) (V2Rx) (O70410)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASRQISLALGFLAFLWAVLGAQNKTEEVQCRLMAKFNLSGYVDAKNHSLVIAGLFPIHSRIIPVDEAILEPVSPMCEGFNFRGFRWMKTMIHTIKEINERKDILPNHTLGYQIFDSCYTISKAMESSLVFLTGQEEFKPNFRNSTGSTLAALVGSGGSSLSVAASRILGLYYMPQVGYTSSCSILSDKFQFPSYLRVLPSDNLQSEAIVNLIKHFGWVWVGAIAADDDYGKYGVKTFKEKMESANLCVAFSETIPKVYSNEKMQKAVKAVKTSTAKVIVLYTSDIDLSLFVLEMIHHNITDRTWIATEAWITSALIAKPEYFPYFGGTIGFATPRSVIPGLKEFLYDVHPNKDPNDVLTIEFWQTAFNCTWPNSSVPYNVDHRVNMTGKEDRLYDMSDQLCTGEEKLEDLKNTYLDTSQLRITKQCKQAVYAIAHGLDHLSRCQEGQGPFGSNQQCAYIPTFDFWQLMYYMKEIKFKSHEDKWVILDDNGDLKNGHYDVLNWHLDDEGEISFVTVGRFNFRSTNFELVIPTNSTIFWNTESSRRPDSFCTQVCPPGTRKGIRQGQPICCFDCIPCADGYVSEKSGQRECDPCGEDDWSNAGKSKCVPKLVEFLAYGEALGFTLVILSIFGALVVLAVTVVYVIHRHTPLVKANDRELSFLIQMSLVITVLSSLLFIGKPCNWSCMARQITLALGFCLCLSSILGKTISLFFAYRISVSKTRLISMHPIFRKLIVLVCVVGEIGVCAAYLVLEPPRMFKNIEIQNVKIIFECNEGSVEFLCSIFGFDVLRALLCFLTTFVARQLPDNYYEGKCITFGMLVFFIVWISFVPAYLSTKGKFKVAVEIFAILASSYGLLGCLFLPKCFIILLRPKRNTDETVGGRVPTVDRSIQLTSASVSSELNSTTVSTVLDE
Protein: Protein Turandot F (Q9VIR2)
Organism: Drosophila melanogaster (Fruit fly)
Function: A humoral factor that may play a role in stress tolerance.
Subcellular location: Secreted {ECO:0000269|PubMed:11409894, ECO:0000305}.
Interaction partners:
Sequence:
MKTVILFGFLLALLGYLEAEHAQSDPEFTAKARQMLAVFGNSEVDRYTKSRNLPALIEFYEKYSSRLPLTVQDRTYANNVIRRYRAHNNQQVDGVPAQGGVGVVFALLLPFAVSIVEGIAKAIRE
Protein: AT09290p (Radial spoke binding protein 15) (Q9VGC1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
- Calmodulin-related protein 97A
- Cortactin, isoform A
- Yuri gagarin, isoform B
- Proteasome inhibitor PI31 subunit
- Dynamin
- Tropomyosin-1, isoforms 9A/A/B
- LIM and SH3 domain protein Lasp
- Eukaryotic translation initiation factor 3 subunit M
- PFTAIRE-interacting factor 1A, isoform H
- Myosin heavy chain 95F
Sequence:
MNYLIQRGKMRQQAINVPEGLPELLSDVTREVLRCQPKKECLCQFIIDYLHSVIVTREKAMVAKTILDRSLRQVDSIISDLCVCDLSKEKSELMGQVLEDCFRNFLEKRRCEMRRGKQAIKFEDVDILEELLQKCKFTDEELVMSRPAIESAYKRFVDAYMSAERGADGTELLYQYFRDRELKRINEAMRNQAAITIQAAWRGYWVRLQFPQEVCVCVCAAEKEDDGEEKRREQAASVLQRFFRKVMLRVVTKPIVDPCAEPTEPTEVDASSSPDTAKDGYDDVNLSTVPTTAAITAGPTPLPTAPGTVPPSAPGTAPATARTSATAIAEPEAHEEAAEAQPAEEAPAAEAPADEAAPAPAEEAAPPPAEEAAPEAAEEPAPPPPPEEAAAPPPPAEEPAPTEGAAPPAEEAPAEEAPAAE
Protein: GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Glycosylphosphatidylinositol-anchor biosynthesis protein 10) (Q4WPG0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI ethanolamine phosphate transferase 1
- GPI mannosyltransferase 2
- GPI mannosyltransferase 1
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI ethanolamine phosphate transferase 3
- GPI mannosyltransferase 2
- Dolichol-phosphate mannosyltransferase subunit 1
- GPI mannosyltransferase 4
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dol-P-Man:Man
Sequence:
MSSSRRRKSFTSSSSSSSPSFHSPPPTSRLRPRSPPSSNTKTSPTSTTPLATNILLSLIAFRLVNAFTVRTFFQPDEFFQSLEPAWQIAFGENQGAWITWEWRHQLRSSIHPLLFAAVYSAADVVAQLLRLSLASRADLLVAAPKTAQAVIAGLGDFYTWKLARYVYGARSYEAWATLALTVVSPWQWFCSTRTLSNCLETTITIVALYLWPWSWSFETPVRKKATRAASRERAQRGPEGSDSLQRLRQCLSLAAVACILRPTNILIWMGLASVAWFRTSWDRRAILVREVLLCGCAVLGLSCVVDRLFYGSWTFPPLRFLYFNIAQSLAVFYGRNDWHYYVSQGFPLLLTTALPFALVGLYRALAQVRTFGLGHLQSLVQAQLALICVIMPFVLSLVSHKEVRFIYPLLPSLHILSAPPLVDYFLPAVIRSSRSYTPRRLTLIFLLLVNIVIALYTTIYHASGPSNILSYLRQQHELHAPAAQTPSNLRPSVKDPSPHGITAGFLMPCHSTPWRSHLIYPTIHAWALTCEPPVDQTAAQKATYIDEADQFYANPARFLREHMAGGLRHISRKPSYLSAQPRPQHPSTTSTNDASHEWPDYLIFFAQLEPTLQSLLRASSYAECYRTFNTAWHDDWRRKGDIVAWCLDPAEQQAWRSATRQRDLENRERQFDRIIESFRKEASGKRDGKLSPFRRWFSSSSSVAPSSSLSLSWPTSWRWPWGQRKRTAWLGVQIPQWTRTRPSWTAWGGDWFGGWRQKKKTKKLLERDLWS
Protein: Import inner membrane translocase subunit (Q9SHB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitochondrial import receptor subunit TOM9-2
- Mitochondrial import receptor subunit TOM5 homolog
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
- Outer envelope pore protein 16-3, chloroplastic/mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial
- Gamma carbonic anhydrase-like 1, mitochondrial
Sequence:
MVKPSDFKAIQGFIRLHYTRVNPVTIGRSNPSALSSPAIPSNGVSQLQPKFSFHSLSSKPTSKNVGLYQILSSPKLNPKLQQALGLPRVNVSFASAFRLVSTKSSGFRKVDGSFARKVVDKPVKAVSSTFARYREAIGLHIDAFWKKNSLVVFGAAGVFVCIFLWRIMFGIASTFVGLSEGMAKYGFLALSSAIVAFSGLYLRSRFTINPDKVYRMTMRKINTAAEILEVMGAPLSGSDLRAYVMSGGGITFKKFKPTIRSKRCFLLFPVQGSEQKGLVSVEVKKKKGQYDMKLLAVDIPMASGPDQRLFLIGDEEEYRIGGGLISVLRDPVVKAMAATKEFDNLDRIEEEEDAERELQEAERKHREEIEKLEKEGS
Protein: Centrosomal protein of 19 kDa (Q389Q9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase MOCS3 homolog
- Molybdenum cofactor biosynthesis protein, putative
Sequence:
MQFVSDLGLELSVFVCHLYAKYSEEPLKAFHELVLRTRSSCCGSDDSSNYLSLATLSGTQWYQDMTKRYASLRQRLRGERDNDVQEAREVTLSLYPQGCRVSEYADAIVTSAAMLTSNIPSTVLERFASCRVKDLNEKGCVSISADELASDLIERPVLDSFTPSRWWESDKTAPSSSLKDGLVAVKSIGLRVQPVEILIFYTYNGRPRRRFIPLDGLLHENSPIAPLLRRLVRSHGMLVSESQLRSYLQRLQELMRKSVESHASTVKPEGPLQPQFDWKQQIGYSDNAPAAHNTGEEEQHMTSAKTGEPEVNKADVGLLYRDPEAALKNVDLNDADDITLQEFKAKMNEGFMQNALRPGDPGYVYDKRLDVNPTERSEWDDSD
Protein: Translation initiation factor eIF2 assembly protein (Cell division cycle protein 123) (Q9P7N5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates the cell cycle in a nutrient dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit gamma
- Probable eukaryotic translation initiation factor 2 subunit beta
- SWR1 complex subunit swc3
Sequence:
MTLILTKNQVLHCQFSSWYSLFRKLTPKAKVIKPIPATVLKYLHEDSIYVEQPMNTVEEVDSEEDEESAPAYYPEREAIQLIEKAIKELGGAVVPKLNWSTPKDALWITTTGSLKCTTAEEVLLLLKSSDFVAHDLNHAFDDCKDFDNADGSVPKDFSFELVLKEWFPMHASTEFRCFVKSKRLIAFCQRDDNYYEFLKENIDCYEKLISDLLKKLDTFPDPDFVFDVYIHKDRAWLIDINPFYPRTDGLLFSWSELESMNSENMKPEIRLIPKGSMPSTGSAKYYTNRVPFDMIAASEGENLLEFAQKWQDLTNKSNE
Protein: Mg2+ transport protein (O07221)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MQTLTVADFALRLAVGVGCGAIIGLERQWRARMAGLRTNALVATGATLFVLYAVATEDSSPTRVASYVVSGIGFLGGGVILREGFNVRGLNTAATLWCSAAVGVLAASGHLVFTLIGTGTIVAVHLLGRPLGRLVDRDNAVEDEGLQPYQVRVICRPKAETYVRAHIVQRTSSNDITLRGIRTGPAGDDNITLTAHLLMVGHTPAKLERLVAELSLQPGVYAVHWYAGEHAQAE