wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich repeat-containing protein 4 (Brain tumor-associated protein BAG) (Nasopharyngeal carcinoma-associated gene 14 protein) (Netrin-G2 ligand) (NGL-2) (Q9HBW1)
Organism: Homo sapiens (Human)
Function: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein. Postsynaptic cell membrane {ECO:0000250}. Note=LRRC4 and DLG4 are interdependent for synaptic localization. {ECO:0000250}.
Interaction partners:
- Netrin-G2
- Netrin-G1
Sequence:
MKLLWQVTVHHHTWNAILLPFVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQASFQCSAPFIMDAPRDLNISEGRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSHVLLSDTGVYTCMVTNVAGNSNASAYLNVSTAELNTSNYSFFTTVTVETTEISPEDTTRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVAVPATDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAATSAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI
Protein: Thiol:disulfide interchange protein DsbD (EC 1.8.1.8) (C-type cytochrome biogenesis protein CycZ) (Inner membrane copper tolerance protein) (Protein-disulfide reductase) (Disulfide reductase) (P36655)
Organism: Escherichia coli (strain K12)
Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Thiol:disulfide interchange protein DsbE
- Thiol:disulfide interchange protein DsbC
- Divalent-cation tolerance protein CutA
- Disulfide bond formation protein B
- Thiol:disulfide interchange protein DsbG
- Thiol:disulfide interchange protein DsbA
- Thioredoxin 1
- Thioredoxin reductase
- Cytochrome c-type biogenesis protein CcmE
- Cytochrome c-type biogenesis protein CcmH
Sequence:
MAQRIFTLILLLCSTSVFAGLFDAPGRSQFVPADQAFAFDFQQNQHDLNLTWQIKDGYYLYRKQIRITPEHAKIADVQLPQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQGCADAGFCYPPETKTVPLSEVVANNAAPQPVSVPQQEQPTAQLPFSALWALLIGIGIAFTPCVLPMYPLISGIVLGGKQRLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQHPYVLIGLAIVFTLLAMSMFGLFTLQLPSSLQTRLTLMSNRQQGGSPGGVFVMGAIAGLICSPCTTAPLSAILLYIAQSGNMWLGGGTLYLYALGMGLPLMLITVFGNRLLPKSGPWMEQVKTAFGFVILALPVFLLERVIGDVWGLRLWSALGVAFFGWAFITSLQAKRGWMRIVQIILLAAALVSVRPLQDWAFGATHTAQTQTHLNFTQIKTVDELNQALVEAKGKPVMLDLYADWCVACKEFEKYTFSDPQVQKALADTVLLQANVTANDAQDVALLKHLNVLGLPTILFFDGQGQEHPQARVTGFMDAETFSAHLRDRQP
Protein: Prestin (Solute carrier family 26 member 5) (P58743)
Organism: Homo sapiens (Human)
Function: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity).
Subcellular location: Lateral cell membrane {ECO:0000305|PubMed:34390643}; Multi-pass membrane protein {ECO:0000269|PubMed:34390643}. Note=Localized at the lateral cell membrane of outer hair cells (By similarity). Alters profoundly the shape of its surrounding lipid bilayer (PubMed:34390643). {ECO:0000250, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643}.
Interaction partners:
- Carboxypeptidase D
- Oncomodulin-2
- Oncomodulin-1
- Hepatic sodium/bile acid cotransporter
- Membrane-associated phosphatidylinositol transfer protein 1
- Transmembrane channel-like protein 1
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MDHAEENEILAATQRYYVERPIFSHPVLQERLHTKDKVPDSIADKLKQAFTCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPIFGLYSSFYPVIMYCFLGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLKESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGLCNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVDGEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALAEQEASAPPSQEDLEPNATPATPEA
Protein: PH-sensitive chloride channel 1, isoform H (M9NEB0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCVFEAAKEQPHKPRSRQLRRNQCRGKAEKAAAGTRGKVAVRGNNDKPAEDIKIKDNYQQNHKTQTETQTEVAAVVAIATDAGAETETETEAEAQKEPATGPEHLKAAAQVLLTIRQARQENNKHSSSQVAETHKDEGEDALARQGSIVDTAAGRIGIDIAATTIQVAERHEDGQHWQQHNVRRRRRQPDPAAHPASITKLSAISLHFHALAALAKTLQKHEDLSPVQDRQPLAYRAWQEHPYAETQMPATMSAAIIANVGATAAATSAAAFQYLGQHYKHYSQSISFYAASSVLLMLCYLTTASTAAATQSETGALDKHPIHGIDWSKFDESSSDKEILDLLLEKKRYDKRLLPPVNDEDFCCGLQSPDMATNQNARRPHNRGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLQVELTFTRDRAYYFTTVFIPGIILVTSSFITFWLEWNAVPARVMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Hair alpha protein) (Keratin-1) (K1) (Type-II keratin Kb1) (P04264)
Organism: Homo sapiens (Human)
Function: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17956333}. Cytoplasm {ECO:0000269|PubMed:32179842}.
Interaction partners:
- Keratin, type I cytoskeletal 10
- Keratin, type II cytoskeletal 2 epidermal
- Filaggrin-2
- Loricrin
- Filaggrin
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Kininogen-1
- Keratin, type II cytoskeletal 5
- Desmoglein-1
- Keratin, type II cytoskeletal 1b
Sequence:
MSRQFSSRSGYRSGGGFSSGSAGIINYQRRTTSSSTRRSGGGGGRFSSCGGGGGSFGAGGGFGSRSLVNLGGSKSISISVARGGGRGSGFGGGYGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGGYGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRMSGECAPNVSVSVSTSHTTISGGGSRGGGGGGYGSGGSSYGSGGGSYGSGGGGGGGRGSYGSGGSSYGSGGGSYGSGGGGGGHGSYGSGSSSGGYRGGSGGGGGGSSGGRGSGGGSSGGSIGGRGSSSGGVKSSGGSSSVKFVSTTYSGVTR
Protein: NF-kappa-B inhibitor-interacting Ras-like protein (Kappa B-Ras) (KappaB-Ras) (Q9V4L4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Atypical Ras-like protein that may act as a regulator of NF-kappa-B activity, possibly by preventing the degradation of NF-kappa-B inhibitor cactus.
Interaction partners:
- Probable Rho GTPase-activating protein CG5521
Sequence:
MLNAKIGKVGKVLVCGMKGVGKTALIEQLVYGHVNPETELHPTIEDIYVASVDTGRGGARETLRIYDTAGLQGEQQQLPRHYLQFPDAFVLVYDPMDPRSLDMLADIKADIEKHKEKKEIPVVVLANVRARAAPNPVEKVMDRANIWCQRERIKHYTVNAMERPSLYEPFTTLCARLHPMQTKSTFPQLRQVMQNRQKSEA
Protein: Glycosyltransferase-like protein gnt15 (Q555X4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May have a role in modulating cell adhesion and glycosylation. Essential for development.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSNFYNNNPRRNTFRLTERIKKKPYQTLIVFILIFLFLYVFGPFGEKKSNNNNNNHPVSKTSSFTESLYTKFQTETFAYRANGDLKKYDISIITQFTVDRFDRIAMMADKWRAPISAAVYITSFKDIDEVFKLVRNSFAVTEFVDLHFLFANKTRYPVNNLRNLALRNARTEWCLLLDVDFISPLGMYDYLHSTLEKLDTSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNENNDNDNGNNNNNNDNEKNFKKKQEDLKIDPNDFEGDLKAIEKLKRNGEKLYVKNLKKVLDGSENNLGKNINFNNNNNDNNNKDDGGGGGYYLNSDNSNINNNNKIAFVIPSFSSSISRFDFPDNKKDLLDFIKQDLIKEINSGVCPKCHGPTNYSRWYLSSEPYLVQYKWIYEPFLLYNRSQIHDYDERLKGYGFDKNSHTFGMAAAGFDFVVLPDAWIIHMNHVSKPWEGADTFNEQMFDCLSIVCESILPDAKSKNGYDPNAKLFNEPLKNNDNCLTREHW
Protein: Prolyl 3-hydroxylase 1 (EC 1.14.11.7) (Leucine- and proline-enriched proteoglycan 1 homolog) (Leprecan-1 homolog) (Q6JHU8)
Organism: Gallus gallus (Chicken)
Function: Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V. May be involved in the secretoty pathway of cells. Has growth suppressive activity in fibroblasts.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase B
- Cartilage-associated protein
- Peptidylprolyl isomerase.
- Protein disulfide-isomerase
- Serpin H1
- Membrane-bound transcription factor site-2 protease
- Transmembrane protein 38B.
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2.
- SEC24 homolog D, COPII coat complex component.
- SERPIN domain-containing protein
Sequence:
MALLLPLLPLLVWAAGPPGPLGPPEHSEPPLPAEPPDALFAAGAEAYARGDWPAVVLQMERALRARAAIRARSVRCRLRCANATAVVPTDGLEPTLHDLLFFRGLLRRAACLRGCGPTQPSRYRLGEELEREFRKRSPYNYLQVAYFKINKVAKAVAAAHTFFVANPEHVEMKQNLEYYQMMAGVRESDFADLEARPHMTEFRLGVRFYSEEQPAAAVLHLEKALQEYFVADTECRALCEGPYDYEGYNYLEYNADLFQAMTDHYMQVLSCKQGCVTELASQPGREKPLEDFLPSHFNYLQFAYYNNGNYEKAIECAKTYLLFFPNDEVMNQNLAYYTAVLGEDLARPIEPRKEIQAYRQRSLMEKELLFFSYDVFGIPFVDPDTWTPEEVIPKRLREKQKVERETAARISEEIGNLMKEIETLVEEKAKESAEMSKFIREGGPLVYEGASVTMNSKSLNGSQRVVVDGVLSAEECRELQRLTNAAASAGDGYRGKTSPHTPSETFYGVTVLKALKLGQEGKVPLQSAHLYYNVTEKVRHMMESYFRLEVPLHFSYSHLVCRTAIDEKQEGRSDNSHEVHVDNCILNAEALVCVKEPPAYTFRDYSAILYLNGDFEGGAFYFTELDAKTQTAEVQPQCGRAVGFSSGSENPHGVKAVTKGQRCAIALWFTLDPRHSERERVQADDLVKMLFRTEEVDLLQETSAEQEPTAATSTAGLHAAGKDEL
Protein: Fat1 protein (Q497H5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
ESLDYKSSHEYYLTVEATDGGTPSLSDVATVNINVTDINDNSPVFSQDTYTTVVSEDAALEQPVITIMADDADGPSNSHIHYSIIEGNQGSPFTIDPVRGEVKVTKPLDRETISGYTLTVQAADNGNPPRVNTTTVNIDVSDVNDNAPLFSRDNYSVIIQENKPVGFSVLKLVVTDKDSSHNGPPFFFTIVSGNDENAFEVNQHGVLLTAATIKRKVKDHYLLHVKVADSGKPQLSSMTHIDIRVIEESIHPPAILPLEIFITAFGEEYSGGVIGKIHATDQDVYDTLMYSLDPHMDGLFSVSSTGGKLIAHRKLDIGQYLLNVSVTDGKFTTVADITVHIQQVTQEMLNHTVAIRFANLTPEEFVGDYWRNFQRALRNILGVRKNDIQIVSLQPSEPHSHLDVLLFVERSGGTHVSTKQLLHKINSSVTDVEEIIGVRILEVFQKLCAGLDCPWKFCDEKVSVDENVMSTHSTARLSFVTPRHHRTAVCLCKDGTCPPVHHGCEDNPCPAGSECVADPREEKYSCVCPGGGFGKCPGSSSITFTGNSFVKYRLLENENRLEMKLSMRLRTYSSHAVVMYARGTDYSILEIHTGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVSLEVEGNYAKLVLDEVHTASGTAPGALKTLNLDNYVFFGGHLRQQGTKHGRGAQVASGFRGCMDSIYLNGQELPLNNKPRAYAHIEEWVDLSHGCLLTATEDCSSSPCQNGGVCNPSPTGGYYCKCSALYVGTFCEVSVNPCSSNPCLYGGTCMVDNGGFVCQCRGLYTGQRCQLSPYCKDDPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECAGNPCRNGALCENTHGSYHCNCSQEYRGKHCEDASPNHYVSTPWNIGLAEGIGIIVFIAGIVLLVMVFVLCRKMISRKKKRQAEPEDKRLGPTTAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESMHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNESLAAPDLSKPRGYHWDTSDWMPSVPLPDIQEFPNYEAIDEHTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAPDELPPLPPEFSDQFESIHPPRDMPAAGSLGSSSRSRQRFNLNQYLPNFYPADMSEPQKQGAGENSPCREPYTPYPPGYQNFEAPTIENMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV
Protein: Histone-lysine N-methyltransferase NSD2 (EC 2.1.1.354) (Nuclear receptor-binding SET domain protein 2) (B8JIA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitochondrial proton/calcium exchanger protein/H
- NK2 homeobox 5.
- N-lysine methyltransferase SMYD2-A
- Ash1
- Negative elongation factor A
- Mediator of DNA damage checkpoint 1.
- Lysine-specific demethylase 4B demethylase 4B)
- Histone H3.2
- Histone H3
- Histone H2B 3
Sequence:
MTDSKGGSLPAMPEPKSPTSMKQLSDSPGGRNGLVDGITDPTMLMNKAATQLAATPQESVPQMIGSHGHNHTHEHLKDLTSRLLNGDTEKIPKLCAAPAGQPLLKGVEPVSQHASPPRKTSVSPELTVKITKCVVNLGGKPNRYEVDYTEEKAEETDAPLRLPEGVLTSPTARRDRQKKKGMVRKRIPPYPILTHAASSDQSPLLHPTINSNDITIEPCGLPVESIEHTHGDMPTCVTAFPDEQPLSDCEETVDAQGVDETDDAQGENDVKESYTETQSNVHFSVGDVIWTKVSGYPWWPCMITTDPEFNMHFRSKVNSRTGLLYHVQYFGDTPERGYVFEKCIVTFSGKHQYQSLSRSNQLPINISGRKRAVPRKFRQKWEIGVSQAKEALGLLTEERLAKFSFVYEDGKAQLNPHMLQVLEEQRNQGLQEEPVQREPQELVSLTPPDSTHSSPTNSSTTSTIPSLFSNPIDSSTSSGKTALPRKARKPSVKTNRRKQRSSTIEWIVTEASSAKQMPLTESTVQCEVNTEHKKKGKTNAGKRPYRKKDLLCIDLDLQPKASQKKPRHIRQKFPAAPNSVKKRKIKAGVSICDTLNTVSTSAGLSEVKASAPSTKLWEKEDASSKGMKKVCKRSRESKQDVTLQPKKKSKLEKDFKKWKCPKAASSAPAAVPAPRGRRRKTDRDENRKRSKKASKEEPPPKAKRGRKRKEESGRQSFPASKKCRPSSYAEPERPDSPSDSTDESHPSKKAERTPGAKKESVCLVCEQTGEDIVTCAGQCYGTYHLHCIGVERSAEKILCTACSTGVHVCFTCKKSEGEVRRCCALHCGRFYHEACVRLSALTVFENRGFRCPLHTCLSCHYSGRAACKATKGKMMRCLRCPVAYHVGDLCVAAGSEMISSSAIVCTNHFRAKKGYSHHSHVNVSWCFICSKGGRLLCCESCPAAFHPDCLNIAMPDGSWFCNDCRSGKKPKYRDVIWVKLGNYRWWPAEIRHPKNIPTNIQHLRHEIGEFPVFFFGSKDYFWTHQGRVFPYMEGDRGSKYQQTGIGKVFKNALLDAETRFKEIEMEREAKEAHENNKKPPPFKYIKVNKPCGRVQVYTADISEIPKCNCKPSTERPCSFESECLNRMLLYECHPQVCPAGERCQNQDFTKRLYPETKIIRTAGKGWGLISLRDIKKGEFVNEYVGELIDEEECRSRIRHAQENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGAPNCSGFLGDRPKNGHTSEPKAKLQKKKPKRKRARNEGKKSEDECFRCGDGGQLVLCDKKGCTKAYHLSCLDRTKRPFGRWDCPWHHCDVCGKNSAAFCQLCPNSFCKAHQEGALRSHPLTGQLCCQEHEDSDIRPQTETAQLPPPTKPRKYRRRAEAKTTSKAPLKKRPRKNAEV
Protein: NAD kinase 1 (EC 2.7.1.23) (ATP-dependent NAD kinase) (Q8Y8D7)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
Interaction partners:
- Probable nicotinate-nucleotide adenylyltransferase
- NAD kinase 2
- NH
- NAD-dependent protein deacetylase
- GTP diphosphokinase
- Pseudouridine synthase
Sequence:
MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRPAEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGTTAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSAKKIHFARFRSFPFWRRVHDSFIED
Protein: Zinc finger and BTB domain containing 14 (J3QL74)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEFFISMSETIKYNDDDHKTLFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFEEVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVSSPDENNGQSKSKYCLKINRPIGDAADTQDDDVEE
Protein: MOB-like protein phocein (Class II mMOB1) (Mob1 homolog 3) (Mob3) (Mps one binder kinase activator-like 3) (Phocein) (Preimplantation protein 3) (Q9QYW3)
Organism: Rattus norvegicus (Rat)
Function: May play a role in membrane trafficking, specifically in membrane budding reactions.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Note=Detected in cell bodies and dendrites of neurons, but not in axons.
Interaction partners:
- Striatin
- non-specific serine/threonine protein kinase
- Striatin-interacting protein 1
- Striatin interacting protein 2
- CTTNBP2 N-terminal like
- Serine/threonine-protein kinase 24
- Serine/threonine-protein kinase 25
- Programmed cell death protein 10
- Striatin-3
- Sarcolemmal membrane-associated protein
Sequence:
MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
Protein: ATP-dependent RNA helicase drs1 (EC 3.6.4.13) (Q09903)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized RNA-binding protein C4F6.14
- Ribosome biogenesis protein ytm1
- Ribosome biogenesis protein erb1
- Pescadillo homolog
- Brix domain-containing protein C1B9.03c
- 25S rRNA
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome production factor 2 homolog
- AdoMet-dependent rRNA methyltransferase spb1
- Probable U3 small nucleolar RNA-associated protein 18
Sequence:
MLWNTQYFRIEGMISLGWPRLAKTSILKFVPIAQNHRIRKMKVQDDFILTIDDSEDDIHYDDYDADAVDEEMPSNVELKKKSKKATPAKDSDFNGEFLFEADVNKDLSSATDMNWDFDMGSKTESNRASNTVDLDAIISRNRKPDDDEFPSSFPSEEELQEPEQENIDSDDEDLAIDGFGAGAIAENEDESSQDESESEEEDDITEPVPSFANISTQDFNSDSAAGSSDSEEDEEEIAKKNAFFAEGDKEKSMMTTTHSSFQSMNLSRPILKGLSNLGFEVPTQIQDKTIPLALLGKDIVGAAVTGSGKTAAFIVPILERLLYRPKKVPTTRVLILCPTRELAMQCHSVATKIASFTDIMVCLCIGGLSLKLQEQELRKRPDIVIATPGRFIDHMRNSQGFTVENIEIMVMDEADRMLEDGFADELNEIIQACPKSRQTMLFSATMTDKVDDLIRLSLNRPVRVFVDNKKTTAKLLTQEFVRVRPQRELLRPAMLIYLCKELFHRRTIIFFRSKAFAHKMRVIFGLLSLNATEIHGSLSQEQRVRALEDFRDGKCNYLLATDVASRGIDIKGIEVVINYEAPATHEVYLHRVGRTARAGRSGRAITLAGEGDRKVLKGVFKNSSAQNTKLVNRNLDFNKVEKFGKEIEELEPVVQKVLDEEKQERELKIAERDLKKGENIMKYGDEIRSRPARTWFQSEKDKQASKASEAKDKKSLAKRKKQMEKEEVPRAYKKTKNDRLSNKKSTKKSKSKRK
Protein: Possible transposase (O50413)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible transposase
- Probable transposase
- Probable transposase
Sequence:
MFRTVGDQASLWESVLPEELRRLPEELARVDALLDDSAFFCPFVPFFDPRMGRPSIPMETYLRLMFLKFRYRLGYESLCREVTDSITWRRFCRIPLEGSVPHPTTLMKLTTRCGEDAVAGLNEALLAKAASEKLLRTNKVRADTTVVEGDVGYPTDTGLLAKAVGSMARTVARIKAADAGSAPLGGSSGPRDRLQAAVTRRAATRSGAGLRAPDHRGASRDRRAGADRGCRGGT
Protein: Histidine-binding periplasmic protein (HBP) (P0AEU0)
Organism: Escherichia coli (strain K12)
Function: Part of the histidine permease ABC transporter. Binds histidine. Interacts with HisQMP and stimulates ATPase activity of HisP, which results in histidine translocation (By similarity).
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P02910}.
Interaction partners:
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP
- Glutamine transport system permease protein GlnP
- Glutamate/aspartate import permease protein GltK
- L-cystine transport system permease protein TcyL
- Arginine ABC transporter permease protein ArtM
- Arginine ABC transporter permease protein ArtQ
- Glutamate/aspartate import permease protein GltJ
- Inner membrane amino-acid ABC transporter permease protein YhdY
Sequence:
MKKLVLSLSLVLAFSSATAAFAAIPQNIRIGTDPTYAPFESKNSQGELVGFDIDLAKELCKRINTQCTFVENPLDALIPSLKAKKIDAIMSSLSITEKRQQEIAFTDKLYAADSRLVVAKNSDIQPTVESLKGKRVGVLQGTTQETFGNEHWAPKGIEIVSYQGQDNIYSDLTAGRIDAAFQDEVAASEGFLKQPVGKDYKFGGPSVKDEKLFGVGTGMGLRKEDNELREALNKAFAEMRADGTYEKLAKKYFDFDVYGG
Protein: Zinc-finger domain-containing protein (Q586Z4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Retrotransposon hot spot
- Zinc-finger protein ZPR1, putative
Sequence:
MKRSFLFLTFSNNTGHYGPPVYMPLEYASRVTNQKQLVFTHPKDPKYGWNTHVHELASLHPGILGPGRRTPQLNWYNRGGIVCEIPPVPVYRHHIWCQGHSHYILQHPKIFIKCPRGEVVCCKWCRLKFINMSTDEDNDDDWREEEQKIATTPEAADDLMQPIRDVGGVLRDRPFQDGREPDPHVYRAVFNPERHRWKHPHHKYEVHPAYAGSSTSSSSADHSCGREGGNSSAAVH
Protein: Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase) (P34112)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II.
Interaction partners:
- G2/mitotic-specific cyclin-B
- Uncharacterized protein
- F-box domain-containing protein
- Ankyrin repeat-containing protein
- Cyclin N-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- M-phase inducer phosphatase
- Probable protein kinase DDB_G0277539
- Anaphase-promoting complex subunit cdc20
Sequence:
MESDGGLSRYQKLEKLGEGTYGKVYKAKEKATGRMVALKKIRLEDDGVPSTALREISLLKEVPHPNVVSLFDVLHCQNRLYLVFEYLDQDLKKYMDSVPALCPQLIKSYLYQLLKGLAYSHGHRILHRDLKPQNLLIDRQGALKLADFGLARAVSIPVRVYTHEIVTLWYRAPEVLLGSKSYSVPVDMWSVGCIFGEMLNKKPLFSGDCEIDQIFRIFRVLGTPDDSIWPGVTKLPEYVSTFPNWPGQPYNKIFPRCEPLALDLIAKMLQYEPSKRISAKEALLHPYFGDLDTSFF
Protein: Transmembrane protein 231 (Q4GZA4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004272}.
Interaction partners:
- B9 domain-containing protein 2
Sequence:
MATIYHEGFKVRYVTRGIGSWVLYFLSLAALFILPFVIATSMGGIWLTNSHFTQHPRLKFSGRCLLRYTTVRGKEKLWTCSDAFNEKLLYGHAELDTLPFFTIYEEDRDSDGSVDCVTIVLGLPVNSLGSRVENSFPPPDEMDAIERVEFIPEFIYEIIHPSIHLNMTAAPLIVFQRPGGGHASASGTGGAHTGGPVCASTSGDILFHTTEPLYSWSNVHYAHTYADSPLDAVESIDDVLNVPRFAQKYASRNQSLLFRRYAESAGGASLLPDITYDRVLGEDMDTVGDFTWKLTLRVQDANVPYVSSIPELIKWAWIQYFTIAYVIQWVLWKLRGMLLKSGMIGSTAIFHRGYAPR
Protein: TOM1-like protein 2 (Target of Myb-like protein 2) (Q6ZVM7)
Organism: Homo sapiens (Human)
Function: Acts as a MYO6/Myosin VI adapter protein that targets myosin VI to endocytic structures. May also play a role in recruiting clathrin to endosomes. May regulate growth factor-induced mitogenic signaling.
Interaction partners:
- Toll-interacting protein
- Zinc finger FYVE domain-containing protein 16
- Unconventional myosin-VI
- Early endosome antigen 1
Sequence:
MEFLLGNPFSTPVGQCLEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLNGNRNYREVMLALTVLETCVKNCGHRFHILVANRDFIDSVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRKGVEFPMADLDALSPIHTPQRSVPEVDPAATMPRSQSQQRTSAGSYSSPPPAPYSAPQAPALSVTGPITANSEQIARLRSELDVVRGNTKVMSEMLTEMVPGQEDSSDLELLQELNRTCRAMQQRIVELISRVSNEEVTEELLHVNDDLNNVFLRYERFERYRSGRSVQNASNGVLNEVTEDNLIDLGPGSPAVVSPMVGNTAPPSSLSSQLAGLDLGTESVSGTLSSLQQCNPRDGFDMFAQTRGNSLAEQRKTVTYEDPQAVGGLASALDNRKQSSEGIPVAQPSVMDDIEVWLRTDLKGDDLEEGVTSEEFDKFLEERAKAAEMVPDLPSPPMEAPAPASNPSGRKKPERSEDALFAL
Protein: CP60 (Q24147)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAIQLDKILQDIAKEKVLHPNNGGASKQEQEEAWARIGRLNKLSVHESRSIFIVLQKKYEQEKLKGNSAWKLFSLMHQIHQDPKISIKEENDQVPMEEVEEYEMLEVQEPEDEDDAHQYGQHTNSTGSASSDGESPTKSHSTGSPEKDERLAYAKPNVDTPRPAIEEKKLLNTLANNTPRSSSLSAAAAVLQKKGITVKKTPSSAAAPKPAIGQQAPASGQRSSSSRTTIQLPDSLKRKLSEEYTSSSAQKKQTKTTSPKQAASSAGATSVHTSVPDQLPAGNNVVHTTTAQLMQVKKEREDNQTPPPGINIITIPSEQQINGGGGGTNSSTAATIASTSVASTNGFSPHIEELDFKNDIIFGPKINAASSNTPEIINLGNFDNSVPPTFFKNLCNSSRHESLGLYVANVMNRLSSRASAKLELSILRAILDVQSDELEQ