wanglab/gogpt-training-data huggingface dataset:
Protein: Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb) (A5PF48)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9WTI7}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9WTI7}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q92002}.
Interaction partners:
- Actin alpha 1, skeletal muscle b.
Sequence:
MESALSARDRVGVQDFLLLENHNSEAAFIENLRRRYREGLIYTYIGSVLVSVNPYKELEIYSKQNMERHRGVNFYEISPHIFALADNSYRALRTERRDQCILISGESGAGKTEASKKILQYYTHICPTRNNTHTIRERLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDIQFDYKGAPIGGHILNYLLEKSRVAHQNHGERNFHIFYQLLEGGEDLLLKRLGLDKTNPQHYHYLIKGNCPRVSSISDKNGWKVVRNALTIIGFEDEEIQALMEIVASVLHLGNTQFGEDEEGETHITTEAQLQFLSQLLGVDGSVLKAALTHKKIVAKGEEMISPLSLEQALSARDSFAKAIYGRAFTWLVQKLNRSLAFKDEIYYSSKCSSVIGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGWERVEYFNNKIICDLVEEKHKGIIAILDEECLRRGDASDITFLEKLEDTLGGHAHFITHKMANGKIRKAIGREEFRLVHYAGEVNYNVNGFLDKNNDLLYRHLKEVLCQSTNHIVSQCFHADELMDQRRPETAATQFKLSLAKLMDILMSKEPSYVRCIKPNDGKQPGRFDEVLVRHQVKYLGLMENLRVRRAGFAYRRSYEAFLERYKSLCPDTWPNWHGNLPEGVATLVKHLNYKPEEFKLGRSKIFIRFPRTLFITEDALEAQKQTIAVTLQKSWRGYRERANYHRIRHAVIVIQSWWRGVKGRRKAKHRRQAADTIRNFIKGFILRNEPRCPDNEYFLDHVRFSFLMKVKRNLPKSVLDKSWPKPPPSLTEASEHIHRICIRNLVNDYCRRIQPEWRKQLEQKVVASGIFKGQKDGYSRSVPKLFVATRLEAEEINLKVLQTLGSDNKVKYGIAVTKYDRHGFRPRVRQLLLTTSSAVLVQEAKIKQRIDYGALLGISVSSLSDGFFVLHIPTADSKQKGDLVLQCDHVIEAVTKLAIMADKIHNVNISQDSIRFAIARGKEGVIDFTSGSDLRVVKSKNGHLSVTTPRIS
Protein: Secretion system chaparone (H9L491)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- Secretion system effector
- Secretion system chaparone
- SPI-2 type 3 secretion system translocon protein SctE
- SPI-2 type 3 secretion system translocon protein SctB
- Secretion system effector
- Secretion system effector
- SPI-2 type 3 secretion system ATPase
- Secreted effector protein SseB
- Secretion system apparatus lipoprotein SsaJ
- Secretion system apparatus protein
Sequence:
MMMKEDQKNKIPEDILKQLLSVDPETVYASGYASWQEGDYSRAVIDFSWLVMAQPWSWRAHIALAGTWMMLKEYTTAINFYGHALMLDASHPEPVYQTGVCLKMMGEPGLAREAFQTAIKMSYADASWSEIRQNAQIMVDTLIA
Protein: Deoxymugineic acid synthase 1 (HvDMAS1) (EC 1.1.1.285) (Q0PCF4)
Organism: Hordeum vulgare (Barley)
Function: Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron.
Interaction partners:
Sequence:
MGAGDRTVAGMPRIGMGTAVQGPKPDPIRRAVLRAIEIGYRHFDTAAHYETEAPIGEAAAEAVRSGAVASRDDLFITSKLWCSDAHGDRVVPALRHTLRNLQMEYVDLYLVHWPVSMKPGRFKAPFTAEDFVPFDMRAVWEAMEECHRLGLAKAIGVANFSCKKLDTLLSFATIPPTVNQVEVNPVWQQRKLREFCRGKGIQLCAYSPLGAKGTHWGSDAVMDAGVLQDIAASRGKSVAQVCLRWVYEQGDCLIVKSFDEARMRENLDVDGWELTEEERRRIAEIPQRKINLGKRYVSDHGPYKSLEELWDGEI
Protein: Ribosome-binding protein 1 (180 kDa ribosome receptor) (RRp) (Q28298)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7790375}; Single-pass type III membrane protein {ECO:0000269|PubMed:7790375}.
Interaction partners:
- PDZ domain-containing protein.
- LEM domain containing 2.
- Immunoglobulin binding protein 1.
- SRP receptor subunit beta.
Sequence:
MDIYDTQTLGVMVFGGFMVVSAIGIFLVSTFSMKETSYEEALANQRKEMAKTHHQKVEKKKKEKTVEKKGKTKKKEEKPNGKIPDHEPAPNVTILLKDPVRAPAVPVAPTPVQPPVVIAPVATVPAMPQEKLAPSPKDKKKKEKKVAKVEPAVSSVVNSVQVLASKAAILETAPKEVPMVVVPPVGAKAGTPATSTAQGKKAEGAQNQSRKAEGAPNQGKKAEGALNQGKKAEGAQNQGKKVEVAPNQGKKAEGGQNQGKKVEGAQNQGKKAEGTPNQGKKAEGAPNQGKKTDGAPNQGKKSEGAPNQGKKAEGAQNQGKKVEVAPNQGKKAEGGQNQGKKVEGAQNQGKKAEGTPNQGKKAEGAPNQGKKTDGAPNQGKKSEGAPNQGKKVEGAQNQGKKVEGVQNQGKKAEGAQNQGKKAEGTSSQGRKEEGTPNLGKKAEGSPNQGKKVEVVQNQSKKVEGAPNQGKKAEGSQNQGKKTEGASNQGKKVDGAQNQGKKAEGAPNQGKKVEGAQNQGKKAEGTPNQGKKAEGAQNQGKKAEGAPNQGKKAEGAPNQGKKAEGAPNQGKKAEGAPNQGKKAEAAPNQGKKAEGAPNQGKKAEGAPNQGKKAEAAPNQGKKAEGAPNQGKKAEGAPNQGKKAEGAPNQGKKAEGAQNQGKKAEGAPNQGKKADLVANQGTKAEGVAGQGKKAEGAPNQGKKGEGTPNQGKKSEGSPNQGKKVDASANQSKRAESAPIQGKNADMVQSQEAPKQEAPAKKKSGSKKKGEPGPPDSDSPLYLPYKTLVSTVGSMVFNEGEAQRLIEILSEKAGVIQDTWHKATQKGDPVAILKRQLEEKEKLLATEQEDAAVAKSKLREVNKELAAEKAKAAAGEAKVKKQLVAREQEITAVQARIEASYREHVKEVQQLQGKIRTLQEQLENGPNTQLARLQQENSILRDALNQATSQVESKQNTELAKLRQELSKVSKELVEKSEAARQEEQQRKALETKTAALEKQVLQLQASHKESEEALQKRLDEVSRELCRSQTSHASLRADAEKAQEQQQQMAELHSKLQSSEAEVKSKSEELSGLHGQLKEARAENSQLMERIRSIEALLEAGQARDTQDAQASRAEHQARLKELESQVWCLEKEATELKEAVEQQKVKNNDLREKNWKAMEALASAERACEEKLRSLTQAKEESEKQLSLTEAQTKEALLALLPALSSSAPQSYTEWLQELREKGPELLKQRPADTDPSSDLASKLREAEETQNNLQAECDQYRTILAETEGMLKDLQKSVEEEEQVWKAKVSATEEELQKSRVTVKHLEDIVEKLKGELESSEQVREHTSHLEAELEKHMAAASAECQSYAKEVAGLRQLLLESQSQLDAAKSEAQKQSNELALVRQQLSEMKSHVEDGDVAGSPAAPPAEQDPVELKAQLERTEATLEDEQALRRKLTAEFQEAQSSACRLQAELEKLRSTGPLESSAAEEATQLKERLEKEKKLTSDLGHAATKLQELLKTTQEQLAKERDTVKKLQEQLDKTDDSSSKEGTSV
Protein: Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (Heparin-binding growth factor receptor) (CD antigen CD333) (Q61851)
Organism: Mus musculus (Mouse)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of STAT1, STAT5A and STAT5B. Plays a role in postnatal lung development.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated receptor (By similarity). {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor 1
- Fibroblast growth factor 2
- Fibroblast growth factor 8
- Fibroblast growth factor 18
- Fibroblast growth factor 9
- Fibroblast growth factor 23
- Klotho
- Fibroblast growth factor 3
- Fibroblast growth factor 17
- Fibroblast growth factor 10
Sequence:
MVVPACVLVFCVAVVAGATSEPPGPEQRVVRRAAEVPGPEPSQQEQVAFGSGDTVELSCHPPGGAPTGPTVWAKDGTGLVASHRILVGPQRLQVLNASHEDAGVYSCQHRLTRRVLCHFSVRVTDAPSSGDDEDGEDVAEDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGKEFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAILGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELMETDEAGSVYAGVLSYGVVFFLFILVVAAVILCRLRSPPKKGLGSPTVHKVSRFPLKRQVSLESNSSMNSNTPLVRIARLSSGEGPVLANVSELELPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDRTAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGMDYSFDACRLPEEQLTCKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTPGGPSPYPGIPVEELFKLLKEGHRMDKPASCTHDLYMIMRECWHAVPSQRPTFKQLVEDLDRILTVTSTDEYLDLSVPFEQYSPGGQDTPSSSSSGDDSVFTHDLLPPGPPSNGGPRT
Protein: Mannose-binding protein A (MBP-A) (Mannan-binding protein) (P19999)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent lectin. Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:3584121}. Note=According to PubMed:10903744, long retention times in the endoplasmic reticulum and the Golgi apparatus that have been observed in former studies may reflect the abnormal physiology of the hepatoma cells used.
Interaction partners:
- Mannan-binding lectin serine protease 2
- Mannan-binding lectin serine protease 1
- Plasma protease C1 inhibitor
- Complement C4
- Ficolin-2
- Complement C2
- Mannose-binding protein C
- Complement C4A
- Pentraxin-related protein PTX3
- Calreticulin
Sequence:
MLLLPLLVLLCVVSVSSSGSQTCEETLKTCSVIACGRDGRDGPKGEKGEPGQGLRGLQGPPGKLGPPGSVGAPGSQGPKGQKGDRGDSRAIEVKLANMEAEINTLKSKLELTNKLHAFSMGKKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (P35731)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in biosynthesis of fatty acids in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Very-long-chain 3-oxoacyl-CoA reductase
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
Sequence:
MHYLPVAIVTGATRGIGKAICQKLFQKGLSCIILGSTKESIERTAIDRGQLQSGLSYQRQCAIAIDFKKWPHWLDYESYDGIEYFKDRPPLKQKYSTLFDPCNKWSNNERRYYVNLLINCAGLTQESLSVRTTASQIQDIMNVNFMSPVTMTNICIKYMMKSQRRWPELSGQSARPTIVNISSILHSGKMKVPGTSVYSASKAALSRFTEVLAAEMEPRNIRCFTISPGLVKGTDMIQNLPVEAKEMLERTIGASGTSAPAEIAEEVWSLYSRTALET
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (A0JMN4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
- Proto-oncogene tyrosine-protein kinase Src
- Protein tyrosine phosphatase non-receptor type 22.
- Paxillin
- Epidermal growth factor receptor precursor.
- Tyrosine-protein kinase
- Paxillin
- SHC-transforming protein 1
- IRS-type PTB domain-containing protein.
Sequence:
MSTFEATWPAGTECVARYNFPGTADQDLPMCKGDVLTIVGVTKDPNWYRAKNSAGREGTIPANYVQKREGVKSASKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCDGKVEHYRIIYHNGKLSIDEEEYFENLMQLMEHYTKDADGLCTRLIKPKIMEGTVAAQDEFSRSGWALNRKELKLIQTIGKGEFGDVMVGDYRGKKVAVKCIKHDATAQAFVAEASVMTQLRHNNLVQLLGVIVEEKGSLYIVTEYMAKGSLVDYLRSRGRTVIGGDRLINFSMDVCKAMEYLEANNFVHRDLAARNVLVSEDNIAKVSDFGLTKEASSTQDTAKLPVKWTSPEALREKKFSTKSDVWSYGILLWEIYSFGRVPYPRIPLKEVVPRVEKGYKMDSPDGCPPVVYDIMKQCWTLDAVVRPSFRDLREKLQDIITNELYR
Protein: Trichome differentiation protein GL1 (Myb-related protein 0) (AtMYB0) (Protein GLABRA 1) (Protein GLABROUS 1) (R2R3-MYB transcription factor GL1) (P27900)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator, when associated with BHLH2/EGL3/MYC146 or BHLH12/MYC1. Involved in epidermal cell fate specification in leaves. Together with TTG1 and GL3, promotes trichome formation and endoreplication. Regulates the production of a signal that induces hair (trichome) precursor cells on leaf primordia to differentiate. Binds to the WER-binding sites (WBS) promoter regions and activates the transcription of target genes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14561633}. Note=Detected in trichome nucleus.
Interaction partners:
- Transcription factor GLABRA 3
- Transcription factor EGL1
- Protein TRANSPARENT TESTA GLABRA 1
- Transcription factor MYC1
- Homeobox-leucine zipper protein GLABRA 2
- At4g12990
- Uncharacterized protein At2g22460/F14M13.14
- Protein TORMOZ EMBRYO DEFECTIVE
- Zinc finger protein GIS
Sequence:
MRIRRRDEKENQEYKKGLWTVEEDNILMDYVLNHGTGQWNRIVRKTGLKRCGKSCRLRWMNYLSPNVNKGNFTEQEEDLIIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNTHLSKKLVGDYSSAVKTTGEDDDSPPSLFITAATPSSCHHQQENIYENIAKSFNGVVSASYEDKPKQELAQKDVLMATTNDPSHYYGNNALWVHDDDFELSSLVMMNFASGDVEYCL
Protein: Ribose-5-phosphate isomerase B (EC 5.3.1.6) (Phosphoriboisomerase B) (P37351)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate.
Interaction partners:
- Ribose-5-phosphate isomerase A
- D-allulose-6-phosphate 3-epimerase
- Transketolase 1
- Transketolase 2
- D-allose kinase
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- HTH-type transcriptional regulator RpiR
- Ribose-phosphate pyrophosphokinase
- Ribokinase
Sequence:
MKKIAFGCDHVGFILKHEIVAHLVERGVEVIDKGTWSSERTDYPHYASQVALAVAGGEVDGGILICGTGVGISIAANKFAGIRAVVCSEPYSAQLSRQHNDTNVLAFGSRVVGLELAKMIVDAWLGAQYEGGRHQQRVEAITAIEQRRN
Protein: Soluble calcium-activated nucleotidase 1 (SCAN-1) (EC 3.6.1.6) (Apyrase homolog) (Putative MAPK-activating protein PM09) (Putative NF-kappa-B-activating protein 107) (Q8WVQ1)
Organism: Homo sapiens (Human)
Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12234496}; Single-pass type II membrane protein {ECO:0000269|PubMed:12234496}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12234496}; Single-pass type II membrane protein {ECO:0000269|PubMed:12234496}. Cell membrane {ECO:0000269|PubMed:16835225}. Note=Processed form: Secreted.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 6
- Bifunctional purine biosynthesis protein ATIC
- Ectonucleoside triphosphate diphosphohydrolase 3
- Ectonucleoside triphosphate diphosphohydrolase 8
- Nucleoside diphosphate phosphatase ENTPD5
- Adenylosuccinate synthetase isozyme 2
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase subunit M2
- Inosine triphosphate pyrophosphatase
Sequence:
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Protein: Phosphoglucomutase (P74643)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Glucose-6-phosphate isomerase
- Glycogen phosphorylase
- Alpha-1,4 glucan phosphorylase
- Glucose-1-phosphate adenylyltransferase
- 1,4-alpha-glucan branching enzyme GlgB
- Ribose-5-phosphate isomerase A
- Transketolase
- Glucose-6-phosphate 1-dehydrogenase
- 4-alpha-glucanotransferase
- Glucokinase
Sequence:
MSKPLIAALHFLQFLYMTSRINPLAGQHPPADSLLDVAKLLDDYYRQQPDPENPAQLVSFGTSGHRGSALNGTFNEAHILAVTQAVVDYRQAQGITGPLYMGMDSHALSEPAQKTALEVLAANQVETFLTTATDLTRFTPTPAVSYAILTHNQGRKEGLADGIIITPSHNPPTDGGFKYNPPSGGPAEPEATQWIQNRANELLKNGNKTVKRLDYEQALKATTTHAHDFVTPYVAGLADIIDLDVIRSAGLRLGVDPLGGANVGYWEPIAAKYNLNISLVNPGVDPTFKFMTLDWDGKIRMDCSSPYAMASLVKIKDHYDIAFGNDTDGDRHGIVTPSVGLMNPNHFLSVAIWYLFSQRQQWSGLSAIGKTLVSSSMIDRVGAMINRQVYEVPVGFKWFVSGLLDGSFGFGGEESAGASFLKKNGTVWTTDKDGTIMDLLAAEITAKTGKDPGLHYQDLTAKLGNPIYQRIDAPATPAQKDRLKKLSPDDVTATSLAGDAITAKLTKAPGNQAAIGGLKVTTAEGWFAARPSGTENVYKIYAESFKDEAHLQAIFTEAEAIVTSALG
Protein: Spermine oxidase (Q5TE25)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
NEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRIRNDPDDPEATKRLKLAMIQQYLKVESCESSSHSMDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDTGEGGQGGEEPRGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLPTEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKTAHGSSTKQQPGHLFSSKCPEQPLDANRGAVKPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGT
Protein: Falcipain-2a (EC 3.4.22.-) (Cysteine proteinase falcipain-2a) (Falcipain-2) (Q8I6U4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Vacuole {ECO:0000269|PubMed:10887194, ECO:0000269|PubMed:17565983, ECO:0000269|PubMed:23471987, ECO:0000269|PubMed:37523385}. Membrane {ECO:0000303|PubMed:17565983}; Single-pass type II membrane protein {ECO:0000269|PubMed:37523385}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:10887194, PubMed:17565983). Localizes to the cell membrane prior to its trafficking to the food vacuole (PubMed:37523385). {ECO:0000269|PubMed:10887194, ECO:0000269|PubMed:17565983, ECO:0000269|PubMed:37523385}.
Interaction partners:
- Uncharacterized protein
Sequence:
MDYNMDYAPHEVISQQGERFVDKYVDRKILKNKKSLLVIISLSVLSVVGFVLFYFTPNSRKSDLFKNSSVENNNDDYIINSLLKSPNGKKFIVSKIDEALSFYDSKKNDINKYNEGNNNNNADFKGLSLFKENTPSNNFIHNKDYFINFFDNKFLMNNAEHINQFYMFIKTNNKQYNSPNEMKERFQVFLQNAHKVNMHNNNKNSLYKKELNRFADLTYHEFKNKYLSLRSSKPLKNSKYLLDQMNYEEVIKKYKGNENFDHAAYDWRLHSGVTPVKDQKNCGSCWAFSSIGSVESQYAIRKNKLITLSEQELVDCSFKNYGCNGGLINNAFEDMIELGGICTDDDYPYVSDAPNLCNIDRCTEKYGIKNYLSVPDNKLKEALRFLGPISISVAVSDDFAFYKEGIFDGECGDQLNHAVMLVGFGMKEIVNPLTKKGEKHYYYIIKNSWGQQWGERGFINIETDESGLMRKCGLGTDAFIPLIE
Protein: cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A) (Q9Z0X4)
Organism: Mus musculus (Mouse)
Function: Cyclic nucleotide phosphodiesterase with specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has also activity toward cUMP (By similarity). Independently of its catalytic activity it is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:11420239}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14432}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Adenosine kinase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- GTP:AMP phosphotransferase AK3, mitochondrial
- Hypoxanthine-guanine phosphoribosyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Inosine triphosphate pyrophosphatase
- Deoxycytidine kinase
Sequence:
MAVRGEAAQDLAKPGLGGASPARVARGNHRHRGESSPSPRGSGCCWRALALQPLRRSPQLSSALCAGSLSVLLALLVRLVGGEVGGELEKSQEAAAEEEEEEGARGGVFPGPRGGAPGGGAQLSPWLQPAALLFSLLCAFFWMGLCLLRAGVRLPLAVALLAACCAGEALVQLSLGVGDGRLLSLPAAGVLLSCLGGATWLVLRLRLGVLMVAWTSVLRTVALVSLERFKVAWRPYLAYLAAVLGLLLARYAEQILPQCSGPAPPRERFGSQLSARTKEEIPGWKRRRRSSSVVAGEMSGCSGKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSGTSITVDIAVMGEAHGLITDLLADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPTVTFSENYTCSDSEEGLEKDKQAISKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSASIKPHEAPSPSAVNPDSWNAPGLTTLTKSRSFTSSYAVSAANHVKAKKQNRPGGLAKISPVPSPSSSPPQGSPASSPVSNSASQQFPESPEVTIKRGPGSHRALTYTQSAPDLSPQIPPPSVICSSCGRPYSQGNPADGPSERSGPAMLKPNRTDDTSQVTSDYETNNNSDSSDILQNEEEAECQREPQRKASACGTYTSQTMIFLDKPILAPEPLVMDNLDSIMDQLNTWNFPIFDLMENIGRKCGRILSQVSYRLFEDMGLFEAFKIPVREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLPSVIGDHGSASDSDSDSGFTHGHMGYVFSKMYHVPDDKYGCLSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLVNLDHVEFKHFRFLVIEAILATDLKKHFDFVAKFNAKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKELHLRWTEGIASEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCHSYDSAGLMPGKWVDDSDDSGDTDDPEEEEEEAETPHEDEACESSIAPRKKSFKRRRIYCQITQHLLQNHMMWKKVIEEEQCLSGTENQSLDQVPLQHPSEQIQAIKEEEEEKGKPRAEETLAPQPDL
Protein: Actin-related protein 2/3 complex subunit 1 (Arp2/3 complex 41 kDa subunit) (p41-ARC) (P38328)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Proline-rich protein LAS17
- Actin
- Protein LDB17
- Myosin-5
Sequence:
MSFSNSKDKSVVAVYKLVKAPIYSHCFSQDKSILAVTCETDCLVYRVSNNTPPVLFATLKDHDKTITAVDISIHGRIVTCSQDRNAYVWEPLSDGTYKPTLVLLRINRAATSVTWAPNGYKFAVGSSARIIAVCYYEHENNWWVSKHIKKPIKSTINCLSWHANGVLLAAGGTDGFMRVFSGFIKGLDSKESVAGSPWGQKFPFGCLIREWYQGSYIHDVEWRSQMERIAYVAHDGTLNVVDYQSPVQSVNAPEGLPYRSLVWINDHEIVCGGYSCHPVLFSEASEGWKFAKNLDKSDNNKSSALTASGNTDELSGNNDESSTFGISALRKFKELDLKGKVSTDVQESAHENAIVELRPFAESNGQITQVSSCGLDGKIVIYTI
Protein: Superoxide dismutase [Cu-Zn], chloroplastic (EC 1.15.1.1) (P07505)
Organism: Spinacia oleracea (Spinach)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MAAHTILASAPSHTTFSLISPFSSTPTNALSSSLQSSSFNGLSFKLSPTTQSLSLSTSAASKPLTIVAATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV
Protein: Photosystem II reaction center protein H (PSII-H) (Photosystem II 10 kDa phosphoprotein) (Q6ENE5)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00752}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00752}.
Interaction partners:
- Cytochrome b559 subunit alpha
- Cytochrome b559 subunit beta
- Photosystem II D2 protein
- Photosystem II CP43 reaction center protein
- photosystem II
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Photosystem II protein D1
- Photosystem II reaction center protein K
- Photosystem II reaction center protein L
Sequence:
MATQTVEDSSRPGPRQTRVGNLLKPLNSEYGKVAPGWGTTPFMGVAMALFAVFLSIILEIYNSSVLLDGILMN