wanglab/gogpt-training-data huggingface dataset:
Protein: mRNA transport regulator MTR10 (Q99189)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mRNA transport from nucleus to cytoplasm.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/arginine
- Exportin-T
- Importin subunit beta-2
- Protein MSN5
- GTP-binding nuclear protein GSP1/CNR1
- Importin subunit beta-3
- Exportin-1
- Nonsense-mediated mRNA decay protein 5
- Importin subunit beta-1
- Importin beta SMX1
Sequence:
MDNLQVSDIETALQCISSTASQDDKNKALQFLEQFQRSTVAWSICNEILSKEDPTNALLELNIFAAQTLRNKVTYDLSQLENNLPQFKDSLLTLLLSHNQKLIITQLNVALARLAIQFLEWQNPIFEIISLLNSSPSILLNFLRILPEETLDIASTSLTEVEFNSRIHELIDPIAEDVLKFLVSCIDLLQNTDGNSSSSISLEQILRCLNSWSYEFPVEQLLTVQPLINLVFETISNGNESDMEAFDSAIDCLCVILRESRDTTNEQLISALFHQLMLLQEKLLPTLFTDHPLNDEYDDDLLEGMTRLFVEAGEAWSVVISKNPDFFKPMVLVLLMLTCKNEDLDVVSYTFPFWFNFKQSLVLPRYQESRKAYSDIFVKLINGIITHLQYPSGQFSSKEEEDKFKDFRYHMGDVLKDCTAVVGTSEALSQPLIRIKSAIENNNSWQIMEAPLFSLRTMAKEISLTENTILPEIIKIICNLPEQAKIRYASTLVLGRYTEWTAKHPELLEVQLQYIFNGFQLHEGSSDMQSIITASSHALMFFCSDCSKLLVGYIDQLINFFLNVQSSIDIESQFELCQGLSAVINNQPEAKVSVIFQKLVDDNLRQIEALIPQWKANPTLLAPQIADKIDLLYALFEELKPRYNYPQQGSEPLLPRIEFIWKALRTLLVDAGAMTDSIIVERVAKLLRRIFERFHVFCEPILPSVAEFLIQGYLTTGFGSYLWCSGSLIVIFGDDESFPISPSLKDAVWKFALSQCETFILNFNKFDKLQLNDYHEAIIDFFSLISDLIMFYPGAFLNSTELLGPVLNVALECVNKLDNYDAYICILRCLDDIISWGFKTPPISTVSIEIVPDEWRKQVINEVVIAHGNQLILVLFIGLVTTFENTAHSDAISCIVKCLRILTEANNNDATICIDWIYKVVEQLGQVTLNERDNLAKAVVEGLNSKDYRKVREGIRAFVGWYSRKNINSRFE
Protein: cDNA FLJ57161, highly similar to Guanine nucleotide-binding protein subunit beta 4 (B4DLV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLSLSPDMRTFVSGACDASSKLWDIRDGMCRQSFTGHVSDINAVSFFPNGYAFATGSDDATCRLFDLRADQELLLYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTLKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLRIWN
Protein: Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10) (P63072)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases.
Subcellular location: Nucleus {ECO:0000269|PubMed:11445583}. Cytoplasm {ECO:0000269|PubMed:11445583}. Note=Accumulates in aggresomes under proteasome inhibition conditions.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-like protein NEDD8
- NEDD8 ultimate buster 1
- 26S proteasome non-ATPase regulatory subunit 4
- Predicted gene 20431
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 variant 1
- Proteasome subunit beta type-9
- Proteasome subunit beta type-8
- Ubiquitin-like protein ISG15
Sequence:
MASVRTCVVRSDQWRLMTFETTENDKVKKINEHIRSQTKVSVQDQILLLDSKILKPHRKLSSYGIDKETTIHLTLKVVKPSDEELPLFLVESKNEGQRHLLRVRRSSSVAQVKEMIESVTSVIPKKQVVNCNGKKLEDGKIMADYNIKSGSLLFLTTHCTGG
Protein: Ubiquitin carboxyl-terminal hydrolase 31 (EC 3.4.19.12) (Deubiquitinating enzyme 31) (Ubiquitin thioesterase 31) (Ubiquitin-specific-processing protease 31) (Q70CQ4)
Organism: Homo sapiens (Human)
Function: May recognize and hydrolyze the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Interaction partners:
Sequence:
MSKVTAPGSGPPAAASGKEKRSFSKRLFRSGRAGGGGAGGPGASGPAAPSSPSSPSSARSVGSFMSRVLKTLSTLSHLSSEGAAPDRGGLRSCFPPGPAAAPTPPPCPPPPASPAPPACAAEPVPGVAGLRNHGNTCFMNATLQCLSNTELFAEYLALGQYRAGRPEPSPDPEQPAGRGAQGQGEVTEQLAHLVRALWTLEYTPQHSRDFKTIVSKNALQYRGNSQHDAQEFLLWLLDRVHEDLNHSVKQSGQPPLKPPSETDMMPEGPSFPVCSTFVQELFQAQYRSSLTCPHCQKQSNTFDPFLCISLPIPLPHTRPLYVTVVYQGKCSHCMRIGVAVPLSGTVARLREAVSMETKIPTDQIVLTEMYYDGFHRSFCDTDDLETVHESDCIFAFETPEIFRPEGILSQRGIHLNNNLNHLKFGLDYHRLSSPTQTAAKQGKMDSPTSRAGSDKIVLLVCNRACTGQQGKRFGLPFVLHLEKTIAWDLLQKEILEKMKYFLRPTVCIQVCPFSLRVVSVVGITYLLPQEEQPLCHPIVERALKSCGPGGTAHVKLVVEWDKETRDFLFVNTEDEYIPDAESVRLQRERHHQPQTCTLSQCFQLYTKEERLAPDDAWRCPHCKQLQQGSITLSLWTLPDVLIIHLKRFRQEGDRRMKLQNMVKFPLTGLDMTPHVVKRSQSSWSLPSHWSPWRRPYGLGRDPEDYIYDLYAVCNHHGTMQGGHYTAYCKNSVDGLWYCFDDSDVQQLSEDEVCTQTAYILFYQRRTAIPSWSANSSVAGSTSSSLCEHWVSRLPGSKPASVTSAASSRRTSLASLSESVEMTGERSEDDGGFSTRPFVRSVQRQSLSSRSSVTSPLAVNENCMRPSWSLSAKLQMRSNSPSRFSGDSPIHSSASTLEKIGEAADDKVSISCFGSLRNLSSSYQEPSDSHSRREHKAVGRAPLAVMEGVFKDESDTRRLNSSVVDTQSKHSAQGDRLPPLSGPFDNNNQIAYVDQSDSVDSSPVKEVKAPSHPGSLAKKPESTTKRSPSSKGTSEPEKSLRKGRPALASQESSLSSTSPSSPLPVKVSLKPSRSRSKADSSSRGSGRHSSPAPAQPKKESSPKSQDSVSSPSPQKQKSASALTYTASSTSAKKASGPATRSPFPPGKSRTSDHSLSREGSRQSLGSDRASATSTSKPNSPRVSQARAGEGRGAGKHVRSSSMASLRSPSTSIKSGLKRDSKSEDKGLSFFKSALRQKETRRSTDLGKTALLSKKAGGSSVKSVCKNTGDDEAERGHQPPASQQPNANTTGKEQLVTKDPASAKHSLLSARKSKSSQLDSGVPSSPGGRQSAEKSSKKLSSSMQTSARPSQKPQ
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (O88275)
Organism: Rattus norvegicus (Rat)
Function: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Retinoic acid receptor RXR-alpha
- NAD-dependent protein deacetylase sirtuin-1
- PR/SET domain 16.
- Nuclear receptor corepressor 1
- Nuclear receptor coactivator
- Nuclear receptor corepressor 2
- Catenin beta-1
- Mediator of RNA polymerase II transcription subunit 1
- Retinoic acid receptor RXR-beta
Sequence:
MGETLGDPPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY
Protein: Substance-P receptor (SPR) (NK-1 receptor) (NK-1R) (Tachykinin receptor 1) (P14600)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Protachykinin-1
- Tachykinin-3
- Tachykinin-4
- Beta-arrestin-2
- Guanine nucleotide-binding protein G
- Beta-arrestin-1
- Transient receptor potential cation channel subfamily V member 1
- Neurotensin/neuromedin N
- Neprilysin
Sequence:
MDNVLPMDSDLFPNISTNTSESNQFVQPTWQIVLWAAAYTVIVVTSVVGNVVVIWIILAHKRMRTVTNYFLVNLAFAEACMAAFNTVVNFTYAVHNVWYYGLFYCKFHNFFPIAALFASIYSMTAVAFDRYMAIIHPLQPRLSATATKVVIFVIWVLALLLAFPQGYYSTTETMPSRVVCMIEWPEHPNRTYEKAYHICVTVLIYFLPLLVIGYAYTVVGITLWASEIPGDSSDRYHEQVSAKRKVVKMMIVVVCTFAICWLPFHVFFLLPYINPDLYLKKFIQQVYLASMWLAMSSTMYNPIIYCCLNDRFRLGFKHAFRCCPFISAGDYEGLEMKSTRYLQTQSSVYKVSRLETTISTVVGAHEEEPEEGPKATPSSLDLTSNGSSRSNSKTMTESSSFYSNMLA
Protein: Ectonucleoside triphosphate diphosphohydrolase 6 (NTPDase 6) (EC 3.6.1.6) (CD39 antigen-like 2) (Q9ER31)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. Has a strong preference for nucleoside diphosphates, preferentially hydrolyzes GDP, IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP. The membrane bound form might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11042118}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:11042118}. Cell membrane {ECO:0000269|PubMed:11042118}; Single-pass type II membrane protein {ECO:0000255}. Note=Exists as a secreted and membrane-bound forms in the medium of transfected cells, the secreted form is predominant. {ECO:0000269|PubMed:11042118}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ectonucleoside triphosphate diphosphohydrolase 3
- Ectonucleoside triphosphate diphosphohydrolase 8
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- UMP-CMP kinase
- GMP synthase
- 5'-nucleotidase
- Uridine-cytidine kinase
- 5'-nucleotidase, cytosolic IA
Sequence:
MRKIPNHGTLRMTKVAYPLGLCVGLFIYVAYIKWHRASAAQAFFTIAGAASGVRWTQQAFSSPDSATRGHEVFYGIMFDAGSTGTRIHVFQFARPPGETPTLTHETFKALKPGLSAYADDVEKSAQGIQELLNVAKQHIPYDFWKATPLVLKATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITVNFLTGSLKTPGSSSVGMLDLGGGSTQITFLPRVEGTLQASPPGHLTALQMFNRTFKLYSYSYLGLGLMSARLAILGGVEGKPAEDDKELVSPCLSPRFRGKWEHAEVTYRISGQKAVGLYELCASRVSEVLRNKVHRTEEAQHVDFYAFSYYYDLAASFGLIDAEKGGSLVVGDFEIAAKYVCRTLETQPPSSPFACMDLTYISLLLHEFGFPGDKVLKLARKIDNVETSWALGAIFHYIDSLKRQKVPAL
Protein: Alpha-1,2-mannosyltransferase MNN5 (EC 2.4.1.-) (P46982)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for addition of first and second mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:20236934, ECO:0000269|PubMed:9756928}. Note=Golgi localization depends on SVP26.
Interaction partners:
- Mannosyltransferase KTR6
- Alpha-1,2-mannosyltransferase MNN2
- Glutamyl-tRNA
- Alpha-1,3-mannosyltransferase MNN1
- Mannan polymerase I complex VAN1 subunit
- Mannan polymerase complexes subunit MNN9
- Mannosyltransferase regulator 4
- Probable mannosyltransferase KTR3
- Glycolipid 2-alpha-mannosyltransferase
- Initiation-specific alpha-1,6-mannosyltransferase
Sequence:
MLIRLKKRKILQVIVSAVVLILFFCSVHNDVSSSWLYGKKLRLPVLTRSNLKNNFYTTLVQAIVENKPADSSPDLSKLHGAEGCSFANNVAAHDSGHDSDLSYESLSKCYNLNKTVQESLREVHSKFTDTLSGKLNFSIPQREALFSGSEGIVTIGGGKYSVLAYTMIKKLRDTGTTLPIEVIIPPQDEGEDDFCKNWLPKFNGKCIYFSDIVPSKPLSDLKLTHFQLKVFGLIISSFKRIIFLDADNYAVKNLDLAFNTTSFNDTGLILWPDFWRRVTPPAFYNIIGSSINIGKRVRFVSDDISPVSRYDPFVSNSNDYTPKERQEHFLKHVPLHDLDGTMPDLSSESGQMVIDKIRHFNTLLLALYYNVYGPTWYYKMISQGTAGEGDKDTFVAAAHALNMPYYQVRTNFEFDGFFYQKDDYKGLALLQHDFEQDYKQYQKAQQKVKANIEEFSKLDPDYTLDNGFLKTLMVNDDGSDLDIMFIHASFYKADPWTLYHENRFIGPNGEQVRGFRKPHRYGMDFELFLFNDMRGSFCTTPKSQVIKFKYFTDKVNTPEWDAMCEYLTNHVNYLESTHKEAMGEKN
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15 (GPI-GlcNAc transferase complex subunit GPI5) (GPI-GnT subunit GPI5) (EC 2.4.1.198) (PIGH homolog) (P53961)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
- GPI ethanolamine phosphate transferase 3
- GPI mannosyltransferase 1
Sequence:
MISKEYEFGKTSILNRKKYTLVIDEDKNGNFIRFTVLPVSNRKFKKVKQNGRVEINMGIQYHQIVLILLLNILFYVICLRSRFLEHINRTFEVTIARSFQILIIMGLFALGTIILVRGPSVETVTIFKESGLQLSRVKGMVIFPQQWNRKFFEQVEFISNERIIDVVINEGFCRGFRVIFYLAAIVRKSSTLKLLFPSNLPSIDDQRLIYNISRKYLSKQEKPLSRPKD
Protein: Hsp90 co-chaperone Cdc37 (Cell division control protein 37) (Hsp90 chaperone protein kinase-targeting subunit) (O94740)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.
Subcellular location: Nucleus. Cytoplasm. Note=When in the nucleus associated with chromatin.
Interaction partners:
- Heat shock protein 90 homolog
- Heat shock protein sti1 homolog
- Uncharacterized protein C1711.08
- Serine/threonine-protein phosphatase T
- Hsp70/Hsp90 co-chaperone cns1
- TATA-binding protein-associated factor mot1
- Tuberous sclerosis 1 protein homolog
- NAD reductase coq12
- 40 kDa peptidyl-prolyl cis-trans isomerase
- Cell division control protein 42 homolog
Sequence:
MAIDYSKWDKLELSDDSDIEVHPNVDKKSFIRWRQRDIHEKRAVRKQKMEDIKGAMAMNRRLLSRISEMETVLEKESPSDPYVLLGSFLEAKKSEDMDSAIPGGMSYHHMLMSLLKVIKDAEDTTEEKSMDDSDKCLRRLKSHKERLLKLLEDAQKEYDTLEAESKNYITSEDLHLGFDSTYVQKKEPEKPKKTKTKKETIQVIESLNNPTPPTDFPGAKEQASTGNAPKNPVNENESEDEEGLSLSEDGKKFANIDFGDYSSSEEFLKEHLNILADEEESDAILLEAFNAELEGKPSLAKQYVHQALLISYCRQLGPNGLSIFFQKIKDPNHQSQRLFLEDVHNTYVRIHERSAAISKEQAESGEGVEQIQLCAVDPNTKLSITIPEAGSTDPETQKARAAFESFPPNLQKALMTNDLDKINVVLGKMAVENAEEVVEKLSSTGMLSIEEGIIDTTKGETIPQLS
Protein: Protein kinase domain-containing protein (G1NJW4)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MCPVSNLLCIKDLSQPNFMWAVFQLFLNFFQENPAMAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKLQQEERMRMESRRQVTVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQPNHYQVLYFKLCMWLFKCGVYNLVVACGFDSLLLHPQIAYELEKDFLSHLGLTSFFFCCFLSSLTVTA
Protein: ATP-dependent chaperone, putative (Q38A33)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MRRCVAYVQLKVGKITPSLWCVTIHHTRRSVALPDPHSILTSPAGLFALMSGRGSTSYDNTSCPKGVKMSGGRRRRRTEHGNGDGDGDKSSAGKGAFFNRDALSLAVLILLLAVTWEALVSQKHIFINKLKEWVFLTLEVRSSREEYAMIMDWMGQQPQGKRARNISLMPISVMKESSNENENEAMRGCSEDECSSCGFVPGFGSHYMKFEGTRLWITRSIDTTKQYRSSPHMDREDEVLRLVFFTRDRDVARRFMEKVRLSWEERSRDTVRVYLPGGWGNRWEFLSRRLRRPLSTLHLPESTTTIVDDAKFFLSSRDLYMSLGVPWRRGYLFEGAPGTGKTSFILALASELSLPVYLLSLQSKELDDSTLIKLVNSVPPRSLLVVEDLEAAIKSQVVRGEDISSANVVFNTEVGGGRDSGVSLSALLNAIDGIASSEGRILVITTNETMRLPAPQALLRPGRIDRRVCFGPLDATIMQEMQHSFLHLVKPFCADREGSRVTLEDCGVGALGTTPAELQNQFLAAIYRKCRR
Protein: Cytosolic 5'-nucleotidase 1B (cN1B) (EC 3.1.3.5) (Autoimmune infertility-related protein) (Cytosolic 5'-nucleotidase IB) (cN-IB) (Q96P26)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of nucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside, AMP is the major substrate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BXI3}.
Interaction partners:
- 5'
- 5'
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 3A
- Deoxycytidine kinase
- Adenylosuccinate synthetase isozyme 1
- Inosine triphosphate pyrophosphatase
- Adenylosuccinate lyase
- 5'-nucleotidase
Sequence:
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHSSCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQWSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPPASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSPTEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPWPPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQYVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLKAYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHFTKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARSAASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIAAYGFNKKFSS
Protein: Uncharacterized protein (Q4GYR9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRTFSRTARITSSAACVGRFEHQGVSRDAVLARWSLQVVKPNAMKTGGLIGKGMKFASPLGPSGWATRNSGTGSTVLDVNWDLRERMDYYVHYSVPSTWTVVEHVSDNSVAIQSKPPVCDSPGAEGPTVHGFSLNCFAYKQKVKEPDCEKLLSLFLHRFDASVSNSLAVLSKASGRGNGVICGTAKPEQDISEVLANRLECAVAEITFTPAVGEPLAHGLCRAFYNSNRRFHYVVVVAVPEDEFTLSKDLLTHALLAVVESRVEAAPKGT
Protein: 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase (DCD dehydrogenase) (EC 1.3.1.53) (Terephthalate dihydrodiol dehydrogenase) (Q3C1E1)
Organism: Comamonas sp
Function: Involved in the degradation of terephthalate (TPA) via the protocatechuate (PCA) 4,5-cleavage pathway. Catalyzes the dehydrogenation of 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate (DCD) to yield protocatechuate (PCA).
Interaction partners:
Sequence:
MTIVHRRLALAIGDPHGIGPEIALKALRQLSANERSLIKVYGPWSALEQAAQICQMESLLQDLIHEEAGSLAQPAQWGEITPQAGLSTVQSATAAIRACENGEVDAVIACPHHETAIHRAGIAFSGYPSLLANVLGMNEDQVFLMLVGAGLRIVHVTLHESVRSALERLSPQLVVNAVQAAVQTCTLLGVPKPQVAVFGINPHASEGQLFGLEDSQITAPAVETLRKCGLAVDGPMGADMVLAQRKHDLYVAMLHDQGHIPIKLLAPNGASALSIGGRVVLSSVGHGSAMDIAGRGVADSTALLRTIALLGAQPG
Protein: LidA (Q5ZWZ3)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Interaction partners:
Sequence:
MAKDNKSHQVKTSEGSLESVKTKEKEPVLEKMRVEDSKKEDKLSMPTTKKESQPNEPVKPFKTSFEKWIESSLLDPQAKEDRGSTINLGREGLKNASQVKKFLLSPAGKDVIAELGAQMALQRNINLQNQQDRMEHELFKRRLMAALFLWYLSKKSHAAEKVKEIIREYNEKAIKNAEKASKPSQQSTSSTSQADKEIQKMLDEYEQAIKRAQENIKKGEELEKKLDKLERQGKDLEDKYKTYEENLEGFEKLLTDSEELSLSEINEKMEAFSKDSEKLTQLMEKHKGDEKTVQSLQREHHDIKAKLANLQVLHDAHTGKKSYVNEKGNPVSSLKDAHLAINKDQEVVEHEGQFYLLQKGQWDAIKNNPAALEKAQKDYSQSKHDLATIKMEALIHKLSLEMEKQLETINNLIMSTDPKENEEATKLLHKHNGLNLKLANLQDMLAVHRKEKSFFNEKGEEVTSLNDAHYVIGKDQQLFNLGGKFYPIHKEQKILEKDGKFYLLKQGEDWESIKDSPEKQKKAEHDFHKLQYETPMTVKKLVHHNKGLETTIHKERVEETKQQLEDNGKEKIEIANNISKLQSTVGVALNQLNQPTLDTESPVLTPSGGSTTSSPKPTPSLASVTTFFKTKIDEMKKNENVKVTFDDLLALSIKIADPKARTYFTGELLKEVPRSGAIPFQTMQRMLQTLEQYGVDTTKPSVTSIRSKTDEVLEQRFNPTPSLSPFKTS
Protein: DNA replication regulator sld2 (DNA replication and checkpoint protein 1) (O14216)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm10
- S-M checkpoint control protein rad4
- DNA replication licensing factor mcm4
- DNA replication regulator sld3
- DNA replication complex GINS protein sld5
- 26S proteasome regulatory subunit rpn8
- Cyclin-dependent kinase 1
- DNA replication complex GINS protein psf3
- DNA polymerase epsilon subunit B
Sequence:
MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS
Protein: Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (Phosphoinositide lipid phosphatase) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16, EC 3.1.3.48) (Q8WUK0)
Organism: Homo sapiens (Human)
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (By similarity). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (By similarity). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P0C089}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C089}; Matrix side {ECO:0000250|UniProtKB:P0C089}.
Interaction partners:
- Phosphatidate cytidylyltransferase, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MAATALLEAGLARVLFYPTLLYTLFRGKVPGRAHRDWYHRIDPTVLLGALPLRSLTRQLVQDENVRGVITMNEEYETRFLCNSSQEWKRLGVEQLRLSTVDMTGIPTLDNLQKGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHKWSPEEAVRAIAKIRSYIHIRPGQLDVLKEFHKQITARATKDGTFVISKT
Protein: Ventral anterior homeobox 2a (Xvax2) (Q9PU20)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated tcf7l2 isoform that cannot bind ctnnb1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle. May be a regulator of axial polarization in the retina.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MFDQATSMGDGVSEERSPLCGKSATSCSERVRDKGTRADLECSLRGHSLKDIPVTSTSSPGSSKEEVQDSQSTGEADYCRRILVRDAKGTIREIVLPKGLDLDRPKRTRTSFTAEQLYRLELEFQRCQYVVGRERTELARQLNLSETQVKVWFQNRRTKQKKDQSRDSEKRSSSTSESFATCNILRLLEQGRLLSVPAPPNLISSSQNNMGTSSGNGTNLGTSGSTSPIISTTPPGAGAFSLQVPSLAASSSPRLPTSLCFPGPLLGGLHEIPSGYGLGSSAFEPYTRLDRKDTASSKKSTS
Protein: Rifin (Q8I219)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHKSTNLHTQNNRSLCECELYAPATYDDDPQMKEVMVKFSKQTQQRFHEYDERMVEKRMQCKDKCDKEIQKIILKDKMEKELMDKFATLQTDIQSDAIPTCVCEKSLADKVEKGCLRCGYGLGTVAPTVGLIGSVAVHVWKPKALEAAIAKAIAEGTADIAAAAEAAGKARGMEFVIKALKHFGVENFFPGICDTISSTGNYTKVTEFVNTIYSKYNGTCNLMRSSINPTACYTIETELSIKTGGAGTGDHPPLYAIRQMIKGLAEEATEAAKAAEAAKNAKLTAAIKEKQTALIEAGFNSSITSINASIIAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLKE