wanglab/gogpt-training-data huggingface dataset:
Protein: Caspar, isoform A (Caspar, isoform B) (LD03368p) (Q7JUP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin fusion degradation protein 1 homolog
- GM09977p
- Nuclear protein localization protein 4 homolog
- GH28815p
- Nuclear factor NF-kappa-B p110 subunit
- BTB/POZ domain-containing protein 9
- Phospholipase A2 activator protein, isoform A
- Uncharacterized protein, isoform A
- UBX domain-containing protein 6
- Transitional endoplasmic reticulum ATPase TER94
Sequence:
MSENKDEALTSFQSITGIDDVGEAFSHLEAADWNLVEALSRVIPHEDAPLTSPHPILVPEPPARNAVESTNGFRPPGFDEMPGTSNASGFFAAALQNQNQNLNLNQPHIQQRFPTSQLLAQLTSSINLDPASSQNNNQNVITFNIHFNQQLYQLRLPSEATVEQLKRKIFAETSVPVCRQAIRGWPPSKASDAQQLGTRLCNLDLSPENELILVDLTEDGFMDTEQDEVTQRVDKDFTIFIQFESDPPLTLSLPGRMTVQEVKMNVFDIKSIPVRHQEWTGWPNGCDNDTTLAQSGIGLSHRFAVRSTERSAPTNSNQHNAFDVVTVDSESSTDEFEDATDFNNAEYIFTDSPPAQPPNRHLIPNDTDDEISGSTQFVENYKARYGEPCPEFFVGSLENAKQLACLRSAKERKLLAIYLHHGKSILSNVFCDQLMKHESIIQTFKEKFVLYGWDMTYESNKDMFLSSLTACISSNASLTARNIKLDKLPAIMLVGKSRQLGSNCEVLSVIHGNIGLDDLLTRLIETCEMFEEQLQVEIRQEDERAARDQVKAEQDMAYQETLQADMAKDAAKRQKEAAQLAERKRMESERAEEDARRESIRLVAQQSLPQEPSEQETGTSKIRVRKPTGDFLERRFFINNNLQDLLNFVTANGFLIEEYKLISSWPRRDLTAIESSQTLESLKLYPQETVILEER
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (A3RJH1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
Protein: Hemoglobin alpha, adult chain 2 (A0A8I6GMB4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVLSADDKTNIKNCWGKIGGHGGEYGEEALQRTFLAFPSTKTYFPHLDLKPGSSQVKAHAQKVADALTLAAHHLDDLPGSLSALSDLHAHELRVDPANFQFFSHCLLVTLARHYPGDFSPEMHASLDKFLGHVTSALVSKDR
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FV91)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 26S proteasome regulatory subunit RPN11
- 26S proteasome regulatory subunit 6A
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- 26S proteasome regulatory subunit RPN2
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- 26S proteasome regulatory subunit 8 homolog
Sequence:
MEKEKDLVEKVDLRFALADTAEKFQAVLDTFLAPLLLKLASPHEPVRQQVFESIKNILQRLGSLPTVRIPVLRLVEQAKKADGHNNVALYSLLFASKGVDRLNDSQEIQAMIPTVMGGISQLPEMCAARMFNLLCRLLLLWKPPMVSSLEEDQVSKLLALEDPRDLEFLMLKFTKFFMMVPNSNTNSGIIPRGYSSPGLSAAEIEFFTYKAGVAFNKDQLLRYKTAIFHFVTRGLIVFSMEEQLRDPENDPTNDDLKAVSLVTFLCVVSTDNSDLGELAITRLKRVHIPYENESFVNFMISLFTGDKSNGIPPTSSNIQETIFSILNRSIYATTSPENVKLICAISLNSTNHKLASLCLSFIRHVAKNNYDSLTLISSASSESDHYGINLPSMIRNNIQTNGWPRLQLGQGQQFNLSIKQRELQYETLGDLLKNDFDLIKDISYIEFLFTSLKNDIPQCTASIQHALNSVLHHLPQLHSDNKKKLKKLLHSILADDYYKIELKENGKLGTVEGKEREDALMSARYMAIKFTNSAFSFDDEEARMLNIFGTSTENRLDITEEAKKGLHPYWFRINYFKSFKTSANAVVESLDQQLGSQITKTKLPTLKTMSSLLLEEVHLLKEDRNSQRVIDKCLNNAVSFLRNCLVEEAIQGKNTIIVQDQDWLVRIEEAIVSDSNVMELVSEYISGIHEKYFVDLLRLLLDEFTERDHSGTQVSIAAAKNHIYQDFLLLLLKACHSDVLKYIYDKVDNLSYLAINITTYPNTEVITSSRALGIIGSSSEEVSNLLIEKFKLSNDLTASKLSHEHLKSILPNILILSHLLPRLSMRGYKDANMTAQLHATLDMLENFFSESITFERKLVLSATAEILKYGLLCILDASDTQSKIKKLLFLLGKKYLNDEDCTRVLSYLSLYTSSVPEMENIADLLWKTTNSKEIDYLFSVGECISIIAGGWHSKILLDDLDIYDPKLVTQLKQDFNDRYAEEVLKKVMTLCTSPNPTLKKAGTMWLLSLVQFTSSSPVIIEKCAEIHRCFVSALIHKDEIVQESAARGLALVYELGSTDVKEDMIKGLFKSFTSNVDGLKISSGSISESTELFDKDTLKTTDGSISTYKDILSLASEVGDPSIVYQFMSLAKNSMLWSSRKGIAFSLGSIMSKASLEKYLIQNKDLANKLIPKLYRYKFDPYTVVAQSMNDIWNTLIVDSKSTIDQYFDSILLELLEGMGNKEWRVREASTTALMDFVRSQPEEKFSGKILDIWTMAFRSMDDIKESVREAGTRFTTVLSKMLVRSIDTSNNVSPEHSEEILSNILPFLMGTKGINSDAEDVKNFSLKLLLDLVKNSPKPLSKFAPEIIYQFITLFSSLEPQVVNYLSLNAKNYNIDMKEIDNQRKNGIAVSPLFEALTKLIGTTNENQVSEVVDAVIRGIKKSIGLPSKVAAAQVVILIVKHYSLAIKQYSGKLLKRCVDMFEDKNEAVSIAYAQSFGYIYKVISAEKSLKYAKQLKVLFFSNSIDHIKIVVAAAILSLFRNAPSEFAELARVLTPVILLGKNDIDQATANVFSDLWTDTASSGAGTTKLYLDEIIDTIRDNIQSNDFSTRRSCAKTIAGISLSIDENTPRKTLSKIFDVTIQSLSGRSWDGKEDIVSALVSISEKCTTYLNGNKELATKIETTLCTEISRNNIRYVRSISKDYLRFVRIVPSDKLYCSFNKELLTKLFAENDENAATEIKTNPEVQLQSNKRMKTSITQHLSKDNIQAVDFMIQVLHEMAKDCIPYMENKYPLEFLNMILEYAQHLTLSHTMSKTWRVRESVCLIITELCKNFPLTIINQEIEDKFKSIWSSIFNENKTHETTENVKIETIRLGGEMIKKFSKLSDQIQRDLSIFTEEELSTARLAVELKNVGI
Protein: ECF RNA polymerase sigma factor SigC (ECF sigma factor SigC) (Alternative RNA polymerase sigma factor SigC) (RNA polymerase sigma-C factor) (Sigma-C factor) (P9WGH1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are usually held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis; this sigma factor does not seem to have a cognate anti-sigma factor however. It has been suggested that the sigma domains 2 and 4 may interact via polar residues in this protein to autoregulate. Positively regulates expression of a small regulon of genes.
Interaction partners:
- ECF RNA polymerase sigma factor SigL
- ECF RNA polymerase sigma factor SigH
- ECF RNA polymerase sigma factor SigM
- Uncharacterized protein Rv0093c
- RNA polymerase sigma factor SigF
- ECF RNA polymerase sigma factor SigD
- ECF RNA polymerase sigma factor SigK
- RNA polymerase sigma factor SigB
Sequence:
MTATASDDEAVTALALSAAKGNGRALEAFIKATQQDVWRFVAYLSDVGSADDLTQETFLRAIGAIPRFSARSSARTWLLAIARHVVADHIRHVRSRPRTTRGARPEHLIDGDRHARGFEDLVEVTTMIADLTTDQREALLLTQLLGLSYADAAAVCGCPVGTIRSRVARARDALLADAEPDDLTG
Protein: E3 ubiquitin-protein ligase RNF38 (EC 2.3.2.27) (RING finger protein 38) (RING-type E3 ubiquitin transferase RNF38) (Q9H0F5)
Organism: Homo sapiens (Human)
Function: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.
Subcellular location: Nucleus {ECO:0000269|PubMed:23973461}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- Polyubiquitin-B
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-conjugating enzyme E2 K
Sequence:
MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQEDAHFKAFFQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPSQHHFSGERCNTPARNRRSPPVRRQRGRRDRLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLPVGGFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPIPPPPYHPSLLPYVLSMLPVPPAVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKANRTCPICRADASEVHRDSE
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 3) (Glucuronosyltransferase I) (GlcAT-I) (UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase) (GlcUAT-I) (P58158)
Organism: Mus musculus (Mouse)
Function: Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O94766}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O94766}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:O94766}.
Interaction partners:
- Beta-1,3-galactosyltransferase 6
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Chondroitin sulfate N-acetylgalactosaminyltransferase 1
- Beta-1,4-galactosyltransferase 7
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Exostosin-like 3
- UDP-glucuronic acid decarboxylase 1
- Xylosyltransferase 2
- 2-phosphoxylose phosphatase 1
- Xylosyltransferase 1
Sequence:
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQADLRRPPPVPAQPPEPEALPTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKAQRLREGEPGWVRPRGVEQRNKALDWLRGKGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPNRPFPLDMAGFAVALPLLLAKPNAQFDATAPRGHLESSLLSHLVDPKDLEPRAANCTQVLVWHTRTEKPKMKQEEQLQRQGQGSDPAIEV
Protein: Ubiquitin-conjugating enzyme E2 13 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 13) (Ubiquitin carrier protein 13) (Ubiquitin-protein ligase 13) (P52490)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a role in the DNA error-free postreplication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
Interaction partners:
- DNA repair protein RAD5
- Ubiquitin-conjugating enzyme variant MMS2
- Polyubiquitin
- Ubiquitin-activating enzyme E1 1
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- DNA polymerase zeta catalytic subunit
- Ubiquitin-ribosomal protein eS31 fusion protein
- Protein SIP5
- Ubiquitin-ribosomal protein eL40A fusion protein
- Proliferating cell nuclear antigen
Sequence:
MASLPKRIIKETEKLVSDPVPGITAEPHDDNLRYFQVTIEGPEQSPYEDGIFELELYLPDDYPMEAPKVRFLTKIYHPNIDRLGRICLDVLKTNWSPALQIRTVLLSIQALLASPNPNDPLANDVAEDWIKNEQGAKAKAREWTKLYAKKKPE
Protein: Myb family transcription factor PHL6 (Protein PHR1-LIKE 6) (Q949U2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Transcription factor bHLH123
- Phospholipase A2-gamma
- Vesicle-associated protein 1-3
- Transcription factor bHLH106
Sequence:
MYIKAIMNRHRLLSAATDECNKKLGQACSSSLSPVHNFLNVQPEHRKTPFIRSQSPDSPGQLWPKNSSQSTFSRSSTFCTNLYLSSSSTSETQKHLGNSLPFLPDPSSYTHSASGVESARSPSIFTEDLGNQCDGGNSGSLLKDFLNLSGDACSDGDFHDFGCSNDSYCLSDQMELQFLSDELELAITDRAETPRLDEIYETPLASNPVTRLSPSQSCVPGAMSVDVVSSHPSPGSAANQKSRMRWTPELHESFVKAVIKLEGPEKATPKAVKKLMNVEGLTIYHVKSHLQKYRLAKYMPEKKEEKRTDNSEEKKLALSKSEADEKKKGAIQLTEALRMQMEVQKQLHEQLEVQRVLQLRIEEHAKYLEKMLEEQRKTGRWISSSSQTVLSPSDDSIPDSQNMSKTKASSPQPPLPAENKASETEDDKCESPQKRRRLENIAESEDPKR
Protein: Probable glutathione-independent glyoxalase HSP32 (EC 4.2.1.130) (Glyoxalase 3 homolog 2) (Heat shock protein 32) (Q08992)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:24706893}. Note=Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock. {ECO:0000269|PubMed:24706893}.
Interaction partners:
- Glyoxalase I
- NADPH-dependent methylglyoxal reductase GRE2
- Hydroxyacylglutathione hydrolase, mitochondrial
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- Catabolic L-serine/threonine dehydratase
- D-serine dehydratase
- Threonine dehydratase, mitochondrial
Sequence:
MTPKRALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKALARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITGFPLEGEIALGVDDILRSRKLTTVERVANKNGAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINALYS
Protein: Probable GTP diphosphokinase RSH2, chloroplastic (EC 2.7.6.5) (RelA/SpoT homolog 2) (AtRSH2) (ppGpp synthetase RSH2) (Q9LVJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses ppGpp (guanosine 3'-diphosphate 5'-diphosphate) synthetase activity in vitro and is able to functionally complement E.coli relA mutants. May be involved in a rapid plant ppGpp-mediated response to pathogens and other stresses.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial
- Inosine triphosphate pyrophosphatase
- Alkaline-phosphatase-like family protein
- Large ribosomal subunit protein bL31c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL28c
- 50S ribosomal protein L33
Sequence:
MVVATTIALYASPPSSVCSTPHQISCDLDLTSRSSSTSSSMASSPQKPIVGGLSSLFSSASVKSSSSSSCSYSTGVDEFSSLRYDRSDDLKDLSFSSSFGYSPAKFVNSFRRDHQSPISVLHGPVSCSCSPPMRMSRDRNLDGSFRLGASGLFNGFVRKALGSCVDYEFGSDSVLVDELTFPMEVDTIKPYARDLLRRAQLRHKIFNDESVIKAFYEAEKAHRGQMRASRDPYLQHCVETAMLLANIGANSTVVVAGLLHDTIDDSFMSYDYILRNFGAGVADLVEGVSKLSQLSKLARENNTACKTVEADRLHTMFLAMADARAVLIKLADRLHNMKTLYALSPVKQQRFAKETLEIFAPLANRLGISTWKVQLENLCFKHLYPNQHNEMSTMLEDSFDEAMITSAIEKLEQALKKAGISYHVLCGRHKSLYSIYSKMLKKKLTVDEIHDIHGLRLIVDNEGDCYKALGVVHSLWSEVPGKLKDYITHPKFNGYQSLHTVVMDNGTVPLEVQIRTQEMHLQAEFGFAAHWRYKEGGCKYSSFVLQMVEWARWVVTWHCEAMSKDRSSISSSDSIKPPCKFPSHSEDCPASYKPNSSQDGPVYVIVIENDKMSVQEFPASSTVSDLLSRAGPGSSRWSMYGIPAKEELRPRLNQIPVSDLKWKLKMGDVVELTPTIPDESLTEYREEIQRMYDRGLAFSRPGTMVGWGS
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (Q5V913)
Organism: Influenza B virus (B/Memphis/13/2003)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}.
Interaction partners:
Sequence:
MSNMDIDGINTGTIDKAPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPERATTISEADVGRKTQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILLAATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRVTFLKEEVKTMYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTLPRRSGATGVAIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRNPGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATPVSILRVGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGAALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADVKGNLLKMMNDSMAKKTNGNAFIGKKMFQISDKNKTNPVEIPIKQTIPNFFFGRDTAEDYDDLDY
Protein: Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (Q7KWJ4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Adenylosuccinate synthetase
- Adenylate kinase isoenzyme 6 homolog
- Adenylate kinase 1
- GTP:AMP phosphotransferase
- Adenylate kinase 2
- Inosine-5'-monophosphate dehydrogenase
- AMP deaminase
- Hypoxanthine phosphoribosyltransferase
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta
- cGMP-specific 3',5'-cyclic phosphodiesterase alpha
Sequence:
MDVHVNQLKNISPIDGRYKRSCQEVSEYFSEYALIKYRIIVEIKWLLFLNDKEYFFPKVSEKSLSNITSIMELINDNDILRVKKIEEETNHDVKAVEYFIREKLESLKNEEITKVIPYVHYLCTSEDINNIAYGLCLYNCIHNIIIPNIQNIIDKLKEFSFNYSDVSLLSKTHGQPASPTTFGKEMSNYYYRLYKHINKLKNIEIYVKFNGAVGNFNAHKVCDPNIDWIDNIKYFIETYFNLHFSLYCTQIQDHDYICEISDTLARLNYTLIDLSVDMWLYISSNVLKLKVIQKEIGSSTMPHKVNPIDFENAEGNLHLANSLFKLFSSKLPISRLQRDLSDSTVLRNLGSSFAYSLISYKSLLRGLNKIDVDQNVMNEQLNQNWCTLAEPIQIIMKKYNIADSYEQLKNFTRGKSIDKQCMYQFIQQNCSHLPKNAIDELMNLTPHNYLGYASYLSKNVEHFSQEYIKKN
Protein: Mitochondrial import inner membrane translocase subunit Tim10 B (Mitochondrial import inner membrane translocase subunit Tim9 B) (TIMM10B) (Tim10b) (Q9WV96)
Organism: Mus musculus (Mouse)
Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y5J6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y5J6}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim9
- Acylglycerol kinase, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim29
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Putative mitochondrial import inner membrane translocase subunit Tim8 A-B
- Mitochondrial import inner membrane translocase subunit Tim8 B
- tRNA methyltransferase 10 homolog B
Sequence:
MEQQQQQLRNLRDFLLVYNRMTELCFQRCVPSLHHRALDAEEEACLHSCAGKLIHSNHRLMAAYVHLMPALVQRRIADYEAASAAPGIPAEQTRDSPSGS
Protein: LOC495502 protein (Q3B8L5)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
SMDEKSTKIIMWLKKMFGDKPLPPYEVNTRTMEILYQLAEWNEARDKDLSLVTEDLKLKSAEVKAEAKYLQDLLTEGLGPSYTNLSRMGNNYLNQIVDSCLALELKNSSLSSYIPAVNDLSSELVAIELNNQEMEAELTSLRKKLTEALVLEKSLEQDLKKAEEQCNFEKAKVEIRSQNMKKLKDKSEEYKYKIHAAKDQLSSAGMEEPLTHRSLVSLSETLTELKAQSMAAKEKLNSYLDLAPNPSLVKVKIEEAKRELKATEVELTTKVNMMEFVVPEPSKRRLK
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q583D1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
- Phosphodiesterase
- Phosphodiesterase
Sequence:
MVTFMRELYVRDGAVTYVVFSLLLQVLTASSLANDKIQVKVYNMLYSNKISAKIYDPIIAGFNASITNGNPPSGANVEVVYVPPMDDSKYADFLNNETSFGENNKISIILGPVGDQNTLGLLKYFKEKNVTSFSPFTGSSKVRSWNPNLYFLTASPAAEMLALLRYAITQLRLHRLGFMYLKDVSYGDDEYKLAVELTTRMDRKLCGVFALKSQIEKESDDSSFSAEWNKFANTRPQGVIVFGSPIPDTKKFLIKSLEDERTKGGYLLIPSTLQYVIKNKWSEELGRDRFVPGKIIITGTNPLAKDDGYDAIKRFRGELANFLKVNGNNFSKDNWNVTLNANENNFTEQDTEGELMVSGWIAGEVLKQALSCREWLTSRDAFITSLYNQRRYVIDDIVVGDFGGECRGMAGERGASCLCNQGGNVVYMKKMEEDHRLYPMKEGVLALTSSRCYRDLSQLYAPLSGIMFKLTDDPKALRTAEAIYDGAFYVVGKGQLGHSDRFFLHWLSSKSHDTSTALYDEVEKRVVTAVFGVVDDSLLSTKGMAFIDPITLTPQLSNPRRNVIHLSPTLEQQLFVIVEHIIQNGAGKMHAIVRSGDTKDIGEMLNKTLDFFESSLSSFVASGEGSTLRDKLPTAGEVLVAGLISDDIPIILSHLGKHHNVRIFVPFFDVALLYDELVSAFRDKPFADRLLFATNLPHWGDKNTESDLVREFHRVVQNESKWKPLSLLGYVTARAMINVLQRMGHVTPEDLVDAIFSQSVITVDDMRYGPFDDKCTNGASFEEKHCAVNYGATHISVWSMSRVLNPSVSPVVTHVTPLMMDGYAKWFRLKRGHIAAIAVSCVVVLALFVTVLLLVIRSSRRNARDNNNAPKEPTDPVTLIFTDIESSTAQWAAHPEQMPDLVATHHRLIRSLITRYECYEVKTVGDSFMIACKSPFAAAQLACDLQRDFLNHDWKTTELDESYREFERKRAEDDSDYTPPTASLDPEVYRQLWNGLRVRVGIHTGLCDIRHDEVTKGYDYYGRTSNMAARTESVGNGGQVLMTRSTYLSLSGKEREQINVTPLGDVPLRGVPKPVEMYQLNAVPGRTFAALRLDRDVEDEENEESEGIFTDVSDICSSTHELCGSSLHVAQSLETVLGTLPATQRQRMLTSICERWRVPPPKSVKNRWDKATFRLAVHHIAVRAGPIMNVVIRNSTGTALSTERSSFALSHSICDVSQLGRQHPLPSVRFHTPMEVKEYLCMSPTDKFDFSIYSCSTIDINMFNGTLEKFDSREPLFGTSLGDNGKNS
Protein: N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) (Q8I8A4)
Organism: Leishmania major
Interaction partners:
- phosphatidylinositol N-acetylglucosaminyltransferase
- Putative phosphatidylinositolN-acetylglucosaminyltransferase subunit c
- PIG-P domain-containing protein
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Mannosyltransferase
- Putative GPI transamidase
- GPI mannosyltransferase 1
Sequence:
MHSITVVCISVVLALLLLLWMKISNLAGTSVRSDVLFVFAHPDDEAMFFTPLLHSLRTQRVTVHFLCLSNGNYAGMGKEREKELYASGAFFGVQRRNIRVVDHADLQDGMCNIWSPLLIRREIESYMQKAGNISTIVTFDKYGVSGHPNHIAVHNGVRELKENMPPGILHLQLRTRSLLWKYVGLLAVLPYALWSSTCVSRASFVAVIPPASVWESMAAMRKHAGQLVWFRYLFVIFSSYTYVNEIEEL
Protein: Amyloid beta precursor like protein 1 (S4R3U6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
XQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP
Protein: Probable G-protein coupled receptor 132 (G2 accumulation protein) (Q9Z282)
Organism: Mus musculus (Mouse)
Function: May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton-sensing activity (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:15728718}; Multi-pass membrane protein {ECO:0000305|PubMed:15728718}. Note=Internalized and accumulated in endosomal compartments. LPC triggers the relocalization from the endosomal compartment to the cell surface.
Interaction partners:
Sequence:
MRSEPTNAAGNTTLGVTSVLQSTSVPSSETCHVSYEESRVVLVVVYSAVCLLGLPANCLTAWLTLLQVLQRNVLAVYLFCLSLCELLYISTVPLWIIYIQNQHKWNLGPQACKVTAYIFFCNIYISILLLCCISCDRYMAVVYALESRGHRHQRTAVTISACVILLVGLVNYPVFDMKVEKSFCFEPLRMNSKIAGYHYLRFTFGFAIPLGILAFTNHQIFRSIKLSDSLSAAQKNKVKRSAIAVVTIFLVCFAPYHVVLLVKAASFSFYQGDMDAVCAFESRLYTVSMVFLCLSTVNSVADPIIYVLGTDHSRQEVSRIHTGWKKWSTKTYVTCSKDSEETHLPTELSNTYTFPNPAHPPGSQPAKLGLLCSPERLPEELC
Protein: Serine protease persephone (EC 3.4.21.-) (Q9VWU1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases. Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz. Nec regulates the cascade by inhibiting psh.
Subcellular location: Secreted {ECO:0000269|PubMed:12098703}.
Interaction partners:
- GH10112p
- Spaetzle-processing enzyme
- Gram-negative bacteria-binding protein 3
- Gram-negative bacteria-binding protein 1
- Protein spaetzle
- Peptidoglycan-recognition protein SA
Sequence:
MPLKWSLLLGTFVLISCSSVEAAVTVGRACKVTDTMPGICRTSSDCEPLIDGYIKSGVLTLNDVPSCGLGAWGEIFCCPTKPCCDNSTITSVSTSSTTSTKAPMTSGRVDVPTFGSGDRPAVAACKKIRERKQQRSGNQLVIHIVGGYPVDPGVYPHMAAIGYITFGTDFRCGGSLIASRFVLTAAHCVNTDANTPAFVRLGAVNIENPDHSYQDIVIRSVKIHPQYVGNKYNDIAILELERDVVETDNIRPACLHTDATDPPSNSKFFVAGWGVLNVTTRARSKILLRAGLELVPLDQCNISYAEQPGSIRLLKQGVIDSLLCAIDQKLIADACKGDSGGPLIHELNVEDGMYTIMGVISSGFGCATVTPGLYTRVSSYLDFIEGIVWPDNRV