wanglab/gogpt-training-data huggingface dataset:
Protein: Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Protein adenylyltransferase (AMPylator) (EC 2.7.7.108) (Protein guanylyltransferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor] (Q29ST3)
Organism: Legionella pneumophila
Function: Virulence effector that plays a key role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a GDP-GTP exchange factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C), thereby converting Rab1 to an active GTP-bound state, leading to the incorporation of Rab1 into LCVs. Also shows RabGDI displacement factor (GDF) activity; however, this probably represents a passive activity following the GEF activity. Also acts as an adenylyltransferase by mediating the addition of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby rendering RAB1B constitutively active. Also has adenylyltransferase activity towards Rab6 and Rab35. Also displays guanylyltransferase activity by mediating the addition of guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however such activity remains uncertain in vivo. Specifically binds phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection.
Subcellular location: Secreted {ECO:0000269|PubMed:19095644}. Host cytoplasmic vesicle membrane {ECO:0000269|PubMed:16906144}; Peripheral membrane protein {ECO:0000305|PubMed:16906144}. Note=Translocated into the host cell via the type IV secretion system (T4SS). Membrane association is mediated by PtdIns(4)P-binding. {ECO:0000269|PubMed:19095644}.
Interaction partners:
Sequence:
MSIMGRIKMSVNEEQFGSLYSDERDKPLLSPTAQKKFEEYQNKLANLSKIIRENEGNEVSPWQEWENGLRQIYKEMIYDAFDALGVEMPKDMEVHFAGSLAKAQATEYSDLDAFVIVKNDEDIKKVKPVFDALNNLCQRIFTASNQIYPDPIGINPSRLIGTPDDLFGMLKDGMVADVEATAMSILTSKPVLPRYELGEELRDKIKQEPSFSNMVSAKKFYNKAIKDFTAPKEGAEVVSVKTHIMRPIDFMLMGLREEFNLYSEDGAHLSAPGTIRLLREKNLLPEEQIARIESVYNQAMSKRFELHAEHKKEHDEMPYSDAKAMLDEVAKIRELGVQRVTRIENLENAKKLWDNANSMLEKGNISGYLKAANELHKFMKEKNLKEDDLRPELSDKTISPKGYAILQSLWGAASDYSRAAATLTESTVEPGLVSAVNKMSAFFMDCKLSPNERATPDPDFKVGKSKILVGIMQFIKDVADPTSKIWMHNTKALMNHKIAAIQKLERSNNVNDETLESVLSSKGENLSEYLSYKYATKDEGREHRYTASTENFKNVKEKYQQMRGDALKTEILADFKDKLAEATDEQSLKQIVAELKSKDEYRILAKGQGLTTQLLGLKTSSVSSFEKMVEETRESIKSQERQTIKIK
Protein: NAC transcription factor (F6IAY2)
Organism: Hordeum vulgare subsp. vulgare (Domesticated barley)
Interaction partners:
Sequence:
MSEVSVINQATEVEDAAAGLDLPPGFRFHPTDEEIISHYLTPKALDHRFCSGVIGEVDLNKCEPWHLPGKAKMGEKEWYFFCHKDRKYPTGTRTNRATMSGYWKATGKDKEIFRGRGILVGMKKTLVFYLGRAPRGEKTGWVMHEFRLEGRLPHPLPRSAKDEWAVSKVFNKELTATNGAMATAMAAAPDAGIERVSSFGFISDHFLDAGELPPLMDPPLGGDVDQVIDFNSNSAYATGGRSGSGLEVKMEQHMPPHMMYSSPYFSLPAANSGDLSPAIRRYCKAEQVSGQTSALSPSRDTGLSTDPNAAGCAEISSAPTPSSHNQDFLDHLDEYPALNLADIWKY
Protein: Eukaryotic translation initiation factor 4E type 1B (A6NMX2)
Organism: Homo sapiens (Human)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structure.
Interaction partners:
- Eukaryotic translation initiation factor 4E-binding protein 1
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 4 gamma 3
- Cytoplasmic FMR1-interacting protein 2
- Nuclear cap-binding protein subunit 1
- Cytoplasmic FMR1-interacting protein 1
- Eukaryotic translation initiation factor 4E-binding protein 3
- Eukaryotic translation initiation factor 4E type 2
- MAP kinase-interacting serine/threonine-protein kinase 2
Sequence:
MLAVEVSEAEGGIREWEEEEKEEEAAERTPTGEKSPNSPRTLLSLRGKARTGGPMEVKLELHPLQNRWALWFFKNDRSRAWQDNLHLVTKVDTVEDFWALYSHIQLASKLSSGCDYALFKDGIQPMWEDSRNKRGGRWLVSLAKQQRHIELDRLWLETLLCLIGESFEEHSREVCGAVVNIRTKGDKIAVWTREAENQAGVLHVGRVYKERLGLSPKTIIGYQAHADTATKSNSLAKNKFVV
Protein: Whirlin (Q80VW5)
Organism: Mus musculus (Mouse)
Function: Involved in hearing and vision as member of the USH2 complex. Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear. Involved in the maintenance of the hair bundle ankle region, which connects stereocilia in cochlear hair cells of the inner ear. In retina photoreceptors, required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport.
Subcellular location: Cytoplasm. Cell projection, stereocilium {ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Cell projection, growth cone {ECO:0000269|PubMed:17584769}. Photoreceptor inner segment {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Synapse {ECO:0000250|UniProtKB:Q810W9}. Note=Detected at the level of stereocilia in inner and outer hair cells of the cochlea and vestibule. Localizes to both tip and ankle-link stereocilia regions. Colocalizes with the growing ends of actin filaments (PubMed:15590698, PubMed:15590699, PubMed:15654330, PubMed:24334608). Colocalizes with MPP1 in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies and at the connecting cilium (CC) (PubMed:17584769). In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment that surrounds the connecting cilia called periciliary membrane complex (PubMed:20502675, PubMed:24334608). {ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}.
Interaction partners:
- Adhesion G-protein coupled receptor V1
- Usherin
- Unconventional myosin-XV
- Epidermal growth factor receptor kinase substrate 8
- Peripheral plasma membrane protein CASK
- Taperin
- PDZ domain-containing protein 7
- Vezatin
- Espin
- G-protein-signaling modulator 2
Sequence:
MNAQLDGLSVSSSSTGSLGSAAAAAGGGGGAGLRLLSANVRQLHQALTALLSEPEREQFTHCLNAYHARRNVFDLVRTLRVLLDSPVKRRLLPMLRLVIPRSDQLLFDQYTAEGLYLPATTPYRQPAWAAPDGAGPGEVRLVSLRRAKAHEGLGFSIRGGSEHGVGIYVSLVEPGSLAEKEGLRVGDQILRVNDKSLARVTHAEAVKALKGSKKLVLSVYSAGRIPGGYVTNHIYTWVDPQGRSTSPPSSLPQPHGSTLRQREDDRRSTLHLLQSGDEKKVNLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAESSGLKVGDQILEVNGRSFLNILHDEAVKLLKSSRHLILTVKDVGRLPHARTTVDQTKWIASSRIGESVANSAGFPGDHTEEGTSKPGFYKGPAGSQVTLSSLGNQTRALLDDQARHLLTEQERATMMYYLAQYRGGTISVEAMVMALFELLNTHAKFSLLSEVRSIISPQDLDRFDHLVLRREIESMKARQPPGPGVGDTYSMVSYSDTGSSTGSHGTSTTVSSARERLLWLIDLMENTLDLEGTGETTQGSTNALPDVSVDDVKSPSEDLPGIKPPPPPPPLAQGHDRLLGQPRKPGREDPAPLSSAAHSGIVFSAPRNRSPPPGTAPTPGPSSAQDSPSSPIYASISHANPSSRKPLDTHLALVNQHPIGPFPRVQSPPHLKSPPAETPGAGACLPPPSPSEHPDAVGANQHFVLVEVHRPDSEPDVNEVRALPQTRTASTLSQLSDSGQTLSEDSGVDAGETEASTSGRGRQTASAKNKNGKEQPRTERTAEGANKPPGLLEPTSTLVRVRKSAATLGIAIEGGANTRQPLPRIVTIQRGGSAHNCGQLKVGHVILEVNGQTLRGKEHKEAARIIAEAFKTKERDYIDFLVTEFNVML
Protein: E3 ubiquitin-protein ligase RNF115 (EC 2.3.2.27) (RING finger protein 115) (RING-type E3 ubiquitin transferase RNF115) (Rab7-interacting RING finger protein) (Rabring 7) (Zinc finger protein 364) (Q9Y4L5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021}. Nucleus {ECO:0000269|PubMed:24852021}. Endoplasmic reticulum {ECO:0000269|PubMed:35343654}. Golgi apparatus {ECO:0000269|PubMed:35343654}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes. {ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
Sequence:
MAEASAAGADSGAAVAAHRFFCHFCKGEVSPKLPEYICPRCESGFIEEVTDDSSFLGGGGSRIDNTTTTHFAELWGHLDHTMFFQDFRPFLSSSPLDQDNRANERGHQTHTDFWGARPPRLPLGRRYRSRGSSRPDRSPAIEGILQHIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVDMGLECPVCKEDYTVEEEVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQSQSTEASASNRFSNDSQLHDRWTF
Protein: Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK) (Q9NYL2)
Organism: Homo sapiens (Human)
Function: Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation. Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways. Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6. Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress. May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15684425}. Nucleus {ECO:0000269|PubMed:15684425}. Note=Translocates to the nucleus upon ultraviolet B irradiation. {ECO:0000269|PubMed:15684425}.
Interaction partners:
- Serine/threonine-protein kinase N1
- Dual specificity mitogen-activated protein kinase kinase 7
- Dual specificity mitogen-activated protein kinase kinase 3
- Zinc finger protein 567
- Ubiquitin-conjugating enzyme E2 N
- Zinc finger protein 33A
- Myeloid differentiation primary response protein MyD88
- Dual specificity mitogen-activated protein kinase kinase 4
Sequence:
MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQCWEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERDLSFKEQELKERERRLKMWEQKLTEQSNTPLLPSFEIGAWTEDDVYCWVQQLVRKGDSSAEMSVYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYINLFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQDCKWKMYMEMDGDEIAITYIKDVTFNTNLPDAEILKMTKPPFVMEKWIVGIAKSQTVECTVTYESDVRTPKSTKHVHSIQWSRTKPQDEVKAVQLAIQTLFTNSDGNPGSRSDSSADCQWLDTLRMRQIASNTSLQRSQSNPILGSPFFSHFDGQDSYAAAVRRPQVPIKYQQITPVNQSRSSSPTQYGLTKNFSSLHLNSRDSGFSSGNTDTSSERGRYSDRSRNKYGRGSISLNSSPRGRYSGKSQHSTPSRGRYPGKFYRVSQSALNPHQSPDFKRSPRDLHQPNTIPGMPLHPETDSRASEEDSKVSEGGWTKVEYRKKPHRPSPAKTNKERARGDHRGWRNF
Protein: Glucose-6-phosphate isomerase, cytosolic B (GPI-B) (EC 5.3.1.9) (Phosphoglucose isomerase B) (PGI-B) (Phosphohexose isomerase B) (PHI-B) (P42863)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8722567}.
Interaction partners:
- phosphoglucomutase
- phosphoglucomutase
- Os06g0258900 protein
- Os09g0535000 protein
- Triosephosphate isomerase, cytosolic
- Os01g0841600 protein
- phosphopyruvate hydratase
- phosphopyruvate hydratase
- Enolase
- Os01g0926300 protein
Sequence:
MASSALICDTEQWKGLQAHVGAIQKTHLRDLMDDAERCKAMTAEYEGIFLDYSRQRATGETMEKLFKLAEAAKLKEKIEKMFSGDKINSTENRSVLHVALRAPRDEVIKSDGVNVVPEVWGVKDKIKQFSETFRSGSWVGATGKALTNVVSVGIGGSFLGPLFVHAALQTDPEAAESAKGRQLRFLANVDPVDVARSIKDLDPETTLVVVVSKTFTTAETMLNARTLKEWIVSSLGPDAVAKHMIAVSTNLELVEKFGIDPKNAFAFWDWVGGRYSVCSAVGVLPLSLQYGFPIVQKFLEGAASIDKHFRSSSFEKNIPVLLGLLSVWNVSFLGYPARAILPYSQALEKFAPHIQQLSMESNGKGVSIDGVQLSFETGEIDFGEPGTNGQHSFYQLIHQGRVIPCDFIGVVKSQQPVYLKGEIVSNHDELMSNFFAQPDALAYGKTPEQLHSEKVPEHLISHKTFQGNRPSLSLLLPSLSAYEIGQLLSIYEHRIAVQGFLWGINSFDQWGVELGKSLASQVRKSLHASRMEGKPVQGFNSSTASLLTRYLAVEPSTPYNTTTMPKV
Protein: Mitogen-activated protein kinase kinase kinase kinase (EC 2.7.11.1) (A1ZBH8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAAHSHHNANMLSSDISRRNPQDEYELIQKIGSGTYGDVYKAKRIQSNELAAIKVIKLEPSDDIQIIQQEIIMMRDCRHPNIIAYYGSYLRRDKLWICMEFCGGGSLQDIYQVTGPLTEVQIAYMCRETLKGLEYLHSMGKMHRDIKGANILLTEYGDVKLADFGVSAQITATINKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWACGITAIELAELQPPMFDLHPMRALFLMSKSGFKPPTLNNKDKWSPTFHNFIKTALTKNPKKRPTAERLLQHPFVQCEMSLRVAKELLQKYQSPNPQFYYYLDGDEESVAGVPQRIASKMTSRTNGVPAQNHTLKTGMTTNSTWNERSSSPETLPSDMSLLQYIDEELKLSGDAVVGGNGGGSSNISSSGGASSGTNGLLDKHELDALPQAATKSAGDGFSHSNSPTANSGAGATGSRDNDGPSSSNSSHLYQNLLRSSSGETPAGSSSAGNNCDYRHENNQNGLEDSPRRHSSMDQLIGLLENMGKSPRTRSLSDGGTQDDDEAEKEAQPDLLNNTPPVPPKRSHKRRHTPPRPISNGLPPTPKVHMGACFSKIFNGCPLRVHCTASWIHPETRDQHLLIGAEEGIYNLNMNELHDAAIDQLFPRRTTWLYVIKDVLMSLSGKSCQLYRHDLVALHSKQTVRFSLHMNKIPERLVPRKFALTTKVPDTKCCTQCCVTRNPYNGYKYLCGATPSGIFLMQWYDPLNKFMLLKQCEWPAISIQGGGHGCVQNGHTPVFEMIITPELEYPIVCTGVRKAMNGCLKLELINMNSASWFHSEDLEYDAMATMVPRRDLLKVVRVHQVEKDAILVCYGNLIQVVTLQGNPKQHKKMVSQLNFDFNVDSIVCLPDSVLAFHKHGMQGKSLRNGEVTQEIKDMSRTYRLLGSDKVVALESQLLRTGSLGSEEGHDLYILAGHEASY
Protein: L,D-transpeptidase 5 (LDT 5) (EC 2.3.2.-) (Ldt(Mt5)) (P9WKV3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems.
Interaction partners:
- UDP-N-acetylenolpyruvoylglucosamine reductase
- Uncharacterized protein Rv0481c
Sequence:
MVIRVLFRPVSLIPVNNSSTPQSQGPISRRLALTALGFGVLAPNVLVACAGKVTKLAEKRPPPAPRLTFRPADSAADVVPIAPISVEVGDGWFQRVALTNSAGKVVAGAYSRDRTIYTITEPLGYDTTYTWSGSAVGHDGKAVPVAGKFTTVAPVKTINAGFQLADGQTVGIAAPVIIQFDSPISDKAAVERALTVTTDPPVEGGWAWLPDEAQGARVHWRPREYYPAGTTVDVDAKLYGLPFGDGAYGAQDMSLHFQIGRRQVVKAEVSSHRIQVVTDAGVIMDFPCSYGEADLARNVTRNGIHVVTEKYSDFYMSNPAAGYSHIHERWAVRISNNGEFIHANPMSAGAQGNSNVTNGCINLSTENAEQYYRSAVYGDPVEVTGSSIQLSYADGDIWDWAVDWDTWVSMSALPPPAAKPAATQIPVTAPVTPSDAPTPSGTPTTTNGPGG
Protein: Histone H1t (Testicular H1 histone) (P22492)
Organism: Homo sapiens (Human)
Function: Testis-specific histone H1 that forms less compacted chromatin compared to other H1 histone subtypes. Formation of more relaxed chromatin may be required to promote chromatin architecture required for proper chromosome regulation during meiosis, such as homologous recombination. Histones H1 act as linkers that bind to nucleosomes and compact polynucleosomes into a higher-order chromatin configuration (Probable).
Subcellular location: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
Interaction partners:
- Histone H1.8
- Testis-specific H1 histone
- Histone H1.10
- Nuclear autoantigenic sperm protein
- Histone RNA hairpin-binding protein
- Histone H4
- Histone H2B type 1-A
Sequence:
MSETVPAASASAGVAAMEKLPTKKRGRKPAGLISASRKVPNLSVSKLITEALSVSQERVGMSLVALKKALAAAGYDVEKNNSRIKLSLKSLVNKGILVQTRGTGASGSFKLSKKVIPKSTRSKAKKSVSAKTKKLVLSRDSKSPKTAKTNKRAKKPRATTPKTVRSGRKAKGAKGKQQQKSPVKARASKSKLTQHHEVNVRKATSKK
Protein: Eukaryotic translation initiation factor 2 subunit beta (eIF2-beta) (Protein EMBRYO DEFECTIVE 1401) (Q41969)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit alpha homolog
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit B
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit G
Sequence:
MADEINEIREEQEQLAPFDPSKKKKKKKVVIQEPVEDLAESSQTEKSDSLPVNDGLESSFTGMKKKKKKPTESSLLNNESVDAGEDLDEIANDEQEGEEGIVLQQRYPWEGSERDYIYDELLGRVFNILRENNPELAGDRRRTVMRPPQVLREGTKKTVFVNFMDLCKTMHRQPDHVMQYLLAELGTSGSLDGQQRLVVKGRFAPKNFEGILRRYITDYVICLGCKSPDTILSKENRLFFLRCEKCGSQRSVAPIKTGFVARVSRRKT
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase delta (PfPDEdelta) (EC 3.1.4.35) (Q8IKD3)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Probably by regulating cGMP levels, required for activation of gametogenesis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanylate cyclase beta
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta
- cGMP-specific 3',5'-cyclic phosphodiesterase alpha
- AMP deaminase
- Inosine triphosphate pyrophosphatase
- Adenylate kinase 1
- Hypoxanthine phosphoribosyltransferase
- GTP:AMP phosphotransferase
- Adenylosuccinate lyase
- GMP synthase
Sequence:
MNEYNNDNMEQEKEKKKEEQKYKNIIKKEYFIFPRLYDKNKEIEYNKLRIHNIKEYICIHLTISLFIILIECFVFSFNLNIKDTTYVEICVVIFSILNCLMHIVVLIKMYFFTSESVYTKGVFIGYIVLNQVFQFLSLYFFTKRNEQSKNDIAHLKYYDNSFNLYVHFFVDSVFILCLPALSFFLSVLFMMMFLCLNILLINMIKFNKTNYGSDIYHICLLSVVLLMFLILRYMMEERNRLLFFFIKDMMFDNYKKWYSDYIGAHYDKDKDSTTINGDNNKYEKEKCEDYKFLFSNKCILFHDFTLNACYKDYYSMICFLNKLLKSCNIKEDMSSNTSVNINGDTYQNMNFHDNINSNIPKNYNSFYEELKKNLNESDILTIAYEVEVLKNIKKINCDEIGKNWDYSFIDSEYGKSTLVILEVGYHLISPYIENNENKKKKLQLFLLLINSMYFPNPYHNANHGATVCHLSKCLAHITDYDSYLNNTYMICYLIASIAHDVGHPGKTNSYLSETNHILSIRYNDMSILENYHCSITFSILQLIGFDFLINNEDTKLVEKNNYTNMRKFIIELIISTDMKLHFEYVDIFKKRKKSQNFDISDTDAINLGTINIKLADIGHTCLKWKDHAKWTMLVSEEFFSQKRVEELHKNKNIDPLNFSNFGKEDNIDEGMIFNYENIYINYINNINNINTYDYSYIKLNFIHHHDFVKSIPSTQVYFFEIIVMPLIKELQSMEKSKKEITQKVLHNLNINLQTWRLIEKNINLFYNTEKMTGTDYYKNLEKQKLLRGIRLLDIAEEDVISLTKNFKEEIKHGKL
Protein: Nrm1p (A0A1D8PCB2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Kleisin alpha
- Yox1p
Sequence:
MSLTTNRIALSTIKDSHLNSSPSNTPSKDKKLPTLYNSNKPKSKLFSPSHSRIRQPDLITKSFSIAHSATSLNKKFSPLRAVSFSDYRSTLSNKPSSSSSSSSSPSNLKLQSTDDAFKNDTIGLAATKLKLKLQLALYKVQQNKQTRLKTTKYYNNNNNNNINSYNHKIHKTNGHKSMAIKLNSILGSLESPPTSNRSSPVSAYESPNPTNNNHMVKSSTASLPTPPEQVRTSNYYSHSINVNLNATPRFNKTKLLKNITKPTNSATSTLNKVASSRTKNTKINKPSKLKLFQIKKDSIYYCSNQKKLPLSQNNTTHVTNQSKYTNNLDITATNGTTHSFNNMSTPSSQGTVTGGAGNGQSMSFFTFYPTSQEQESSQNSTTNVGTTRLPSITVDRTTNEVPSNRNTNHAQNSFYSSLDATNTALPSINKILKTPIRRANNASKQFSFQRSFNNAAPLVTNNNNNNNNNNSNTYGNDETTIDEDNDITIIQNTTISNTTIDQNATIDEEKTEYDVEQEEITQEIKNSNEEDDNEDINSPSKQQDILTSSPLSNQQFTTPNKFSVAKSLLQLGGHRM
Protein: Envelope glycoprotein K (L8B1Q7)
Organism: Equid alphaherpesvirus 1 (Equine herpesvirus 1)
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004252}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004252}. Host cell membrane {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004598}. Host endosome membrane {ECO:0000256|ARBA:ARBA00004330}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004330}.
Interaction partners:
Sequence:
MLLGGRTAYLSVLGLITAYAAFTIWYTLTAQLHNPCVYATVSIDSKDGIAAKWEVYNSTIVYAYPENGAKRFSDGLSGFDYVCMENWVNESKLNVLKNMKELHDKVRIVVGTRNCRAYLWSVQLQMITGVWLIYIAFLCLRQERRLLGPFRNQNEFLSPTGYTFNYATYTLATTVLKTHYTKFALLLCEASLRRVALSRTFKRDPIGFLCEHSAALALIGLEVGTHFVARLLVVGTVTLVHTPCSQIYPIYLKLASWGFVVAVTIVEIVAIIYEKPPKTGSSANPPTPATHGVKGLCTSCCSTVLANLCGKLVYLLLVIGAMSILLHYEQRIQIGLLGKSFSS
Protein: Canoe, isoform D (Q8IPP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSHDKKMLDREAVRSVIQQWNANRLDLFALSEPDENLLFHGVMRFYFQDAGQKVATKCIRVASDATVTDVIDTLIEKFRPDMRMLSVPNYALYEVHANGEERRLNADEKPLLVQLNWHIDDREGRFLLKNIDQKTTPIEQTDLNFKRKLSKREKKEQKKKEKMAKLSSDPPTSNGSHLGLGNGVGASSGSAHMNGNAGGTGGDSSDAVAGKLYTELPETSFTRSISNPEAVMRRRRQQKLEKKLQQFRSRDGGPDTGGTLKIYGESLCQDVPYKTLLLSIRDCAQAVVREMLTKYGLEKADPLHYCLVQVNSDGTEYILDDDECPLSILMNHPTSRGSIMFHVRRRPADSQPRRRKKKPLGAANGANHISGDREGPVLVEVTHSGDGGRRIKLGSDPVEVGSANTNCLQLFGPSIQPRHCLISLLEGVCTVTPLHTDALTFVNGHHISQPTILHNGSVVMFGRVASYRFLDSPTDGRYNLALSQSQLDSACLYESRSPTSPGSWNDEDGALSSTHKSDYDHHQQANHSSAYHNNNNNSSDHPLSSTLRDVVDSKAGQDQGANSGNYDGQSLEGNLENETKSISSLKSGGSNSQDRSPKMTGSGILAGGGSGSGDTQGQEPILPAVLEFPETHQELFLRHIISELDVNVPHFKLAPVYSLYLCARYRASTHYRPELQPTERAHKLTMFLHHVANLVYSVVQEQYTDPRILAFWMANSSEFLHFLKSDRHISAFSVQAQEVLAEAVQTAFRNLVNCFRLELSQTLNQFLSENIDHDSAAGLVLTVLGSAMALLRRCRVNAALTIQLFSQLFHYINVICFNTIVANSQMCTGDWGKVMTERLQLLELWAERQGLELAADCHLAKINQCAQFLQAPKSSVEEIQQLACSCFRLNSLQMAALLQQEKLPRNLVDTAIRMAESVADELTRADGREVRLEESPELHLALLLPDDGFSCDVVRGIPTGLVDFLNPLQQQGMCRLAAQPTSIGLWTVYMHQFNARSSSAMSNKLPQPELQLIKLHKNSNGMGLSIVAAKGAGQEKLGIYIKSVVPGGAADADGRLQAGDQLLRVDGQSLIGITQERAADYLVRTGPVVSLEVAKQGAIYHGLATLLQQPSPVIQRASPSNFLQHLNTGQQRRHSSFQQQARYYNNSISDDSLNRSRRESFACMRASSPPVRRLSASCLQEELCALGHQLHIDPRYRDTRPIARSASNLYLGNDQGGYYHPPPMAPCVTHFSPMRPLRKTPPPSIYIEEYHDEPAKDSQESFGNFAAYSDAHQPLNEEGIASMALSDEIPFIDDEEEEKQHQQRPCMSTSSCSSTVKRNPAAGYRKTVSFDLEQGDGEPGAIGIDRKYHTHDAISHFAASASSTESLMADKDERIPLIQKIRRELNSKRATNCSADGFSSGGSGSNSQRSSSESIERMPLLRQNHSPCQRQLNTQRSHKRSGVGTAAPIVSIQVPSVCEIESSSTRSPTVNTSNRYCASTTFQTKTIPSTTMKANSRRASSQVNLNPRFLLPLGQGKVREMAEYFNANKNFPPIINKSRSTSALDDPGSNPCAKLSQAEQSRILKQLKEWSLHGSAGKDFDEAEKVGDKISCECPCCAHCRGKREQHQGKQEQHQVAATFKCYDSCRDVEAEPTKQKPELSRYTSYRQSVMCSNRQAHSVRQLKRNKQQKHVQLRTKPSSHSRHHHHHHCHKQQRPRAPATPPSTDNTKSNSSDTKRSSASMRNPQSCSNCGDAIDDCHSCSCSEVESCSSAGESSSSCCAAHCEVLETCGHSRRGDNDSNAGGGIDGNHGGGGHCVKMSLPVSTETTSTTVFPTHR
Protein: Fatty acid desaturase (Q9NFT2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPRNTKDTTGVLYESDVETVDGGLSTELSNRKTTDGSKLELVWFNIVLFVILHISSLYGVWLLFTSATWTTVVLFWPTVVVTILGVSGGAHRLWAHRTFKANTPLKLIFLFLNTLAFQDAVYYWARDHRVHHKYTETDADPYNSQRGWFFAHIGWLCCRKHPEVVEKGKQIDLSDLEADPLIMFQKKYYLLLMPIICFVLPTVLPMYLWGESLNVSWHVMALLRWCLSLNLIWTVNSSAHMHGMRPYDKNICSVDQGFLIFFRVGEGYHNYHHVFPWDYKSAELGKYSQDVTTKFIEFMAYLGWAYDLKSVSLDLVKQRVQRSGDGSHPVWGWGDKDQLKEDVGVTTITHQRNEK
Protein: ATP synthase subunit a, chloroplastic (ATP synthase F0 sector subunit a) (F-ATPase subunit IV) (P0C2Y6)
Organism: Oryza sativa subsp. indica (Rice)
Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
Interaction partners:
- ATP synthase subunit c, chloroplastic
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit beta, chloroplastic
- ATP synthase subunit gamma, mitochondrial
- ATP synthase CF0 subunit I
- ATP synthase subunit beta
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit beta
- F-ATPase gamma subunit
Sequence:
MNIIPCSIKTLKGLYDISGVEVGQHFYWQIGGFQIHAQVLITSWVVITILLGSVIIAVRNPQTIPTDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH