wanglab/gogpt-training-data huggingface dataset:
Protein: Protein CPL1 (J9VQE5)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Virulence factor which promotes fungal virulence by enhancing type 2 inflammation in the mouse host. Likely binds mouse Tlr4 independently of Ly96/Md2 and activates Tlr4 signaling to drive Stat3 phosphorylation in interstitial macrophages, which promotes the initial induction of Arg1/arginase-1 and increases macrophage sensitivity to Il4 signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:35896747}.
Interaction partners:
Sequence:
MFSIPPSVRRLVFLFLIAAPLLSIVLPVAAAPAGVDPPSKLQPRAPQPSRRMGATKRSKKIEPLKKKDYSSFLCPGGSVACPIPGDEVSPSSVEALEKSLNSLADWFKVGFECVELETELNSCGGCLALGSGQDCALIENARTTGCENGSCQVYSCFDGYVVSPDRTSCVKRGSTIPATPVTAVNVEEFVADDQLPFGQ
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1 (PDE1) (EC 3.1.4.17) (B7YZV4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Required for male fertility and male mating behavior.
Interaction partners:
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11
- AMP deaminase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Apyrase
- Adenylate kinase 2
- Adenine phosphoribosyltransferase
- AT10229p
- Inosine triphosphate pyrophosphatase
- Adenosine kinase
- Adenosine kinase
Sequence:
MQPSSPNATNYLADNIQISSANLSQTEMVVGRDSADYTAMHSINVGVGNSFLRGDTDIPQESGHSFETPSNMSFTAGQWDTESLPPVDTPDALNKAAGRIRSLLRRMDHETVAYEDMQRNLHYAARVLEAVFIDESREGCNGNCKNLNCSRHSHGRDDQQQDNNNSNRSCSLQEASPGGAGAGVTPGADNQDSIESRTKGVSQAPQTHSGPTGPPSNTSSETIAQPAPKLQPALETVRESVMEESPSKDPGDKGPPPPASTSTLTSQTTTSSSATAEPSAKAAESQAGSAGSSGSCSNPAAVHRQRRLRTPTWARSMSTNKTRLADEDDELSEVQPDAVPPEVREWLASTFTRQMATSRRKSDEKPKFRSVAHAIRAGIFVDRMYRRVSSSALTAFPPDVVRLLKNLDDWTFDVFALTEAASGQVVKYVAYELFNRYGSIHKFKIAPGILEAFLHRVEEGYCRYRNPYHNNLHAVDVMQTIHYCLCNTGLMNWLTDLEIFASLLAALLHDYEHTGTTNNFHVMSGSETALLYNDRAVLENHHASASFRLLREDEYNILSHLSREEFRELRGLVIEMVLGTDMTNHFQQMKAMRQLLTLQEATIDKQKVLSLVLHCCDISHPAKQWGVHHRWTMLLLEEFFRQGDLEKELGLPFSPLCDRNNTLVAESQICFIDFIVEPSMGVMSDMLELILAPIAPMNKSKPATLVEHETTANSTTNSAIVIPNSGITPSMDKPRDHRTEAKTTAAECLARKSVTGTTASKFNIPKPWLTCLVENKRIWKEQAVKDAEARALATAAEEAAAAAAAEAEESKPETETADGEQSEPAAEPADGAAA
Protein: Mitochondrial inner membrane protease subunit 2 (EC 3.4.21.-) (Q9UST2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Uncharacterized mitochondrial carrier C1442.03
- Eukaryotic translation initiation factor 2 subunit alpha
- Mitochondrial inner membrane protease subunit 1
- Signal peptidase complex subunit 2
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
Sequence:
MANPFVRNQSFKSVFFKNLVGITLWVPVLMFVEQHVVSVGTIEGRSMKPAFNPETNMLQRDRVLLWKWNKDYKRGDVVILRSPENPEELLVKRVLGVEYDIMKTRPPKKLSLVPVPEGHVWVEGDEQFHSIDSNKFGPVSTGLITAKVIAILFPFSRAGRIDHEGFRKNAVFLSGKRSVK
Protein: Thyroid hormone receptor beta (F1NWE9)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MNYCMQEIYEVHPAAGSNCYMQSTDYCTYIEDNQGYSSCDAQVLHSNNIYMEQAWAVNQPYTCSYPGNVFKSEYSDMDMALNQYNQPEYFTEEKPTFSQVQSPSYSQKKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYEGKCVIDKVTRNQCQECRFKKCIFVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKTIGHKPEPTDEEWELIKIVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSQFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLVCVERIEKCQEGFLLAFEHYINYRKHHVAHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Protein: Gamma-aminobutyric acid receptor subunit gamma-3 (GABA(A) receptor subunit gamma-3) (GABAAR subunit gamma-3) (Q99928)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inactive phospholipase C-like protein 1
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit alpha-1
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor subunit theta
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MAPKLLLLLCLFSGLHARSRKVEEDEYEDSSSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDEHSCPLIFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTALGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTTTKKTTSLLHPDSSRWIPERISLQAPSNYSLLDMRPPPTAMITLNNSVYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRKGRIHIDILELDSYSRVFFPTSFLLFNLVYWVGYLYL
Protein: Probable threonine protease PRSS50 (EC 3.4.25.-) (Cancer/testis antigen 20) (Serine protease 50) (Testis-specific protease-like protein 50) (Q9UI38)
Organism: Homo sapiens (Human)
Function: May be involved in proteolysis through its threonine endopeptidase activity.
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:17283160}. Note=May also localize to cytoplasmic membranes.
Interaction partners:
- P antigen family member 5
- Sarcoma antigen 1
Sequence:
MGRWCQTVARGQRPRTSAPSRAGALLLLLLLLRSAGCWGAGEAPGALSTADPADQSVQCVPKATCPSSRPRLLWQTPTTQTLPSTTMETQFPVSEGKVDPYRSCGFSYEQDPTLRDPEAVARRWPWMVSVRANGTHICAGTIIASQWVLTVAHCLIWRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQRFWSWVGQANDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQFRTIQEKEVIILNNKECDNFYHNFTKIPTLVQIIKSQMMCAEDTHREKFCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWIWDCLNGQALALPAPSRTLLLALPLPLSLLAAL
Protein: Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) (O00091)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- Probable 6-phosphogluconolactonase
- Glucose-6-phosphate isomerase
- Hexokinase-1
- Phosphoglucomutase
- Hexokinase-2
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glucose-6-phosphate 1-dehydrogenase gcd1
- Probable glucose-6-phosphate 1-dehydrogenase C7.13c
- Fructose-bisphosphate aldolase
Sequence:
MSSANLSIKENGAMVVFGASGDLSKKKTFPALFSLFSEGRLPKDIRIVGYARSKIEHEDFLDRITQNIKIDEEDSQAKEKLEEFKKRCSYYRGSYDKPEDFEGLNSHLCEREGDRSTHNRIFYLALPPDVFVSVATNLKKKCVPEKGIARLVIEKPFGVDLKSAQELQSQLAPLFDEKEIYRIDHYLGKEMVQNLVHLRFCNPVISHLWDKNSISSVQITFKEPIGTEGRGGYFDSSTIVRDIVQNHLVQILTLLTMETPTTFSADDLRDEKVKVLRRTRLGDLKDIVLGQYVKSKDGKKPGYLDDETVPKGSRCPTYSAIPCFIDTERWRGVPFLLKAGKAMDIGKVEIRVQFKAAANGLFKDAYHNELVIRVQPDEAIYFKMNIKQPGLSEAPLLTDLDLTYSRRFKNMKLHEAYEALFLDAFAGDQSRFARIDELECAWSLVDPLLKYMEEEKPVPEPYEYGSDGPECLYSFLKKFGYIYDSPDYYDYPVMSVPSDH
Protein: THO complex subunit 2 (AtTHO2) (Protein EMBRYO DEFECTIVE 2793) (F4IAT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- THO complex subunit 5B
- THO complex subunit 1
- THO complex subunit 3
- THO complex subunit 6
- THO complex subunit 5A
- THO complex subunit 7B
- THO complex subunit 7A
- THO complex subunit 4B
- Cell division cycle 5-like protein
- Nuclear cap-binding protein subunit 2
Sequence:
MSLPLLECKYVTEEFVREGKNGNYGTKLPSSVPMLRFLYELSWILVRGELPIQSCKAVLEGVEFLDKPSREELASCFADVVTQIAQDLTMSGDQRSRLIKLAKWLVESQTVPQRLFQERCEEEFLWEADMVKIKAQDLKGKEVRLNTRLLYQQTKFNLLREESEGYAKLATLLCRGSASSSHNASAATMGIIKSLIGHFDLDPNRVFDIVLDCFELEQDYDTFLNLIPIFPKSHASQILGFKFQYYQRLEVNSPVPVGLYKLTALLVKEEFINLESIYAHLLPKDEEVFEDYNVSSAKRFEEANKIGKINLAATGKDLMEDEKQGDVTVDLFAALDMESEAVTERLPELENNQTLGLLNGFLSVDDWYHANILFERLAPLNPVAHDQICSGLFRLIEKSITHSYRIARQTRFQSSSSASTVKLTPTANTTANRTYLDLPKEVFQMLVTVGPYLYRNTQLLQKICRVLRAYYLSALDLVRDGSNQEGSAYEVSRGHLKEVRLRVEEALGTCLLPSLQLVPANPAVGHEIWEVMSLLPYEARYRLYGEWEKDDEQNPLLLAARQVAKLDTRRILKRLAKENLKQLGRMVAKLAHANPMTVLRTIVNQIEAYRDMIAPVVDAFKYLTQLEYDILEYVVIERLAQSGRDKLKDDGINLSDWLQSLASFWGHLCKKYPSMELRGLFQYLVNQLKRGQGIELVLLQELVQQMANVQYTENLTEDQLDAMAGSETLRYHATSFGMMRNNKALIKSSNRLRDSLLPNDEPKLAIPLLLLIAQHRSLVVVNADAPYIKMVTEQFDRCHGILLQYVDFLSSAVSPTTAYARLVPSLDELVHTYHLEAEVAFLVFRPVMRLFKCRRNGDVSWPLDSGESMDADSEISESESSMILDVGTSEKAVTWSDVLDTVRTMLPSKAWNSLSPDLYATFWGLTLYDLHVPRNRYESEISKQHTALKTLEEVADNSSSAITKRKKEKERIQESLDRLTGELKKHEEHVASVRRRLSREKDTWLSSCPDTLKINMEFLQRCIFPRCTFSMADSVYCAMFVNMLHSLGTPFFNTVNHIDVLICKTLQPMICCCTEYEVGRLGRFLFETLKIAYHWKSKESVYEHECGNMPGFAVYYRYPNSQRVTFGQFVKVHWKWSGRITRLLIQCLESNEYMEIRNALIMLTKISGVFPVTRKTGINLEKRATKIKNDEREDLKVLATGVGAALSARKPHWVTDEEFSMGFLELKAPPVHTPKHASSQNGLLVGVSQGEPTGERATVNQQPESGGLGKDQMLKTKPLDGRTESIPSKSDQGHLKSKGGNPLDSQPSISKKSMEQKETDETPRISDENPVKPASKYSEAELKASSKRGASVNKSAKQDFGKDDGKSGKAIGRTSTADKDLNYLESRQSGLTKALSSTAANGSIATGSSKVKDDGAEALDAQKQSSRTVHSPRHEIVTSVRSSDRLQKRANAVEDSERISKRRKGDAEHKEHDSEPRSSDRDRSVEARLDLNKTVTDDQSTHRDQDRSKDKGYERQDRDHRERVDRSDKPRGDDVEKARDKSLERHGRERSVEKGLDKGTTRSYDRNKDERNKDDRSKLRHSEASLEKSHPDDHFHSQGLPPPPPLPPNIIPHSMAAKEDLERRAGGARHSQRLSPRHEEREKRRSEENLSVSVDDAKRRRDDDIRDRKRDDRETITVKGEEREREREREREREKSLPLKEDFEASKRRKLKREQQVPSAEPGEYSPMPHHSSLSTSMGPSSYEGRERKSSSMIQHGGYLEEPSIRLLGKEASSKMARRDPDPIAKSKSKNSNFLDIALESMTVNGKTTRGEQSGSGEIGSRE
Protein: O-acetylserine sulfhydrylase (OAS sulfhydrylase) (OASS) (EC 2.5.1.47) (Cysteine synthase A) (CSase A) (O-acetylserine (thiol)-lyase A) (OAS-TL A) (O-acetylserine-specific cysteine synthase) (Sulfide-dependent cysteine synthase) (P9WP55)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide.
Interaction partners:
- Serine acetyltransferase
- Cystathionine gamma-synthase
- O-succinylhomoserine sulfhydrylase
- Sulfite reductase [ferredoxin]
- Sulfur carrier protein CysO
- S-sulfocysteine synthase
- L-cysteine desulfhydrase Cds1
- Phosphoserine aminotransferase
- cysteine-S-conjugate beta-lyase
- Putative cystathionine beta-lyase
Sequence:
MSIAEDITQLIGRTPLVRLRRVTDGAVADIVAKLEFFNPANSVKDRIGVAMLQAAEQAGLIKPDTIILEPTSGNTGIALAMVCAARGYRCVLTMPETMSLERRMLLRAYGAELILTPGADGMSGAIAKAEELAKTDQRYFVPQQFENPANPAIHRVTTAEEVWRDTDGKVDIVVAGVGTGGTITGVAQVIKERKPSARFVAVEPAASPVLSGGQKGPHPIQGIGAGFVPPVLDQDLVDEIITVGNEDALNVARRLAREEGLLVGISSGAATVAALQVARRPENAGKLIVVVLPDFGERYLSTPLFADVAD
Protein: DNA-binding protein RFX5 (Regulatory factor X 5) (P48382)
Organism: Homo sapiens (Human)
Function: Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters.
Subcellular location: Nucleus.
Interaction partners:
- MHC class II transactivator
- DNA-binding protein RFXANK
- Regulatory factor X-associated protein
- Cyclic AMP-responsive element-binding protein 1
- HLA class II histocompatibility antigen, DR alpha chain
- Ankyrin repeat family A protein 2
- Nuclear transcription factor Y subunit beta
- DNA-binding protein RFX7
- Nuclear transcription factor Y subunit alpha
- Nuclear transcription factor Y subunit gamma
Sequence:
MAEDEPDAKSPKTGGRAPPGGAEAGEPTTLLQRLRGTISKAVQNKVEGILQDVQKFSDNDKLYLYLQLPSGPTTGDKSSEPSTLSNEEYMYAYRWIRNHLEEHTDTCLPKQSVYDAYRKYCESLACCRPLSTANFGKIIREIFPDIKARRLGGRGQSKYCYSGIRRKTLVSMPPLPGLDLKGSESPEMGPEVTPAPRDELVEAACALTCDWAERILKRSFSSIVEVARFLLQQHLISARSAHAHVLKAMGLAEEDEHAPRERSSKPKNGLENPEGGAHKKPERLAQPPKDLEARTGAGPLARGERKKSVVESSAPGANNLQVNALVARLPLLLPRAPRSLIPPIPVSPPILAPRLSSGALKVATLPLSSRAGAPPAAVPIINMILPTVPALPGPGPGPGRAPPGGLTQPRGTENREVGIGGDQGPHDKGVKRTAEVPVSEASGQAPPAKAAKQDIEDTASDAKRKRGRPRKKSGGSGERNSTPLKSAAAMESAQSSRLPWETWGSGGEGNSAGGAERPGPMGEAEKGAVLAQGQGDGTVSKGGRGPGSQHTKEAEDKIPLVPSKVSVIKGSRSQKEAFPLAKGEVDTAPQGNKDLKEHVLQSSLSQEHKDPKATPP
Protein: Sodium/potassium-transporting ATPase subunit alpha (P90735)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362084}.
Interaction partners:
- Probable sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta
Sequence:
MGKKDKKQELHDLKQEVKMDEHIVPIEELVARLGTNLETGLTRQKAQEVLAKNGPNALSPPETTPEWIKFCKNLFGGFAMLLWVGAILCYIAYSVDYFTMEYPSKDNLYLGIVLMTVVVITGVFQYYQESKSSKIMDSFKNMVPTFALVHRDGQKQQVKTEELVVGDIVEVKGGDRVPADLRVVSAFGFKVDNSSLTGESEPQSRSPDCTNENPLETRNIAFFSTNAVEGTAKGIVIYTGDNTVMGRIAHLASGLDTGMTPIAREIEHFIHLITGVAVFLGISFFIIAFILGYHWLTAVVFLIGIIVANVPEGLIATVTVCLTLTAKRMASKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWYDETIHECDTTETQTSQEKRTGASFEALVRIASLCNRAEFKAGQQDTPILRRDCTGDASEIALLKFTELTQGNVIAVREKNKKIAEIPFNSTNKYQVSIHDNGDHYLLVMKGAPERILDVCSTIFLNGKESELTDKLREDFNTAYLELGGMGERVLGFCDFVLPADKFPKGFKFDVEEVNFPLKNLRFVGLMSMIDPPRAAVPDAVAKCRSAGIKVVMVTGDHPITAKAIAKSVGIISDGTETVEDIAIRRGIPVEEVNPREAKAAVIHGSDLREMSEDQLAEIIKYHSEIVFARTSPQQKLMIVEGFQKQGQIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVVGVEEGRLIFDNLKKSIAYTLTSNIPEISPFLTYILFGIPLPLGTVTILCIDLGTDMVPAISLAYEEAESDIMKRQPRDPIRDKLVNERLISLAYGQIGMIQASAGFFTYFWIMADNGFMPWDLYQLRAQWDSRAYNNVLDSYGQEWTYANRKILEYTCQTAYFVSIVVVQWADLIISKTRRNSLVQQGMSNWTLNFGLVFETALAWFMCYCPGLDNGLRMYGLRFSWWFCALPFSILIFVYDEIRRFLIRRYPGGWVERETYY
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q8MSL3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MCIKLKDDLRRFMHWGPITLLTLTLIVTWTVIHMNSMWWAPGSSLESVLNYALIWIQTFGTLYNFIRSLMVGPGFVPLKWHPQLAKDKMFLQFCTRCNGYKAPRSHHCRRCDRCVMKMDHHCPWINTCVGWSNQDSFVYFLLFFMSGSIHGGIIIVSAVIQGIKKRWLIRLGLRHMATVHLTQTNLLACVFSLGVIMGTVLASIKLLYMQMKSILKNQTEIENWIVKKAAFRRNAYPRKGIKPFVYPYNLGWKTNIREVFLSTGDGISWPVLPECNEYSLTCEQLQQKKDKRARTRVFRCIRPATGHWVPIFSQGLWVSLQIPCTDDPRIALKPDDIIHVTRIQEYWLYGEIMISEKQKEKIRARNGAIRGWFPSCCAIEICEDSDSENDLAGGEPVKEQDTAAIESVETDQEIIDFMRDFSCNDGKKAKRLHIE
Protein: POU domain protein (Q6TGI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- PROP paired-like homeobox 1.
- Prolactin.
- Thyroid-stimulating hormone subunit beta a.
- Prolactin 2.
- Zinc finger homeobox 3.
- LIM/homeobox protein Lhx3
- T-box transcription factor 19.
- Pituitary homeobox 2
- LIM homeobox 4
Sequence:
MSCQAFSTSDSFSGLGGDTGAALPLLMHHSAAADCHNTNICSTVPSGLPLVQSSKRSHMHLSTSALGNASASLHYPMPPCHYSNQQTTYGMMAAQEMLSASISQTRILQTCSVPHANMVNGANSLQGALAPRLYKFPEHSLAGGSCALSHGFAPLPQTLLTDEPILGDIKQELRRKSRTLDETPDMDSPQIRELEKFANDFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKSILAKWLEEAEQAGALFNEKMGLHERKRKRRTTISLGAKEALERSFVEKSKPSSQEIVRMAEGLHLEKEVVRVWFCNRRQREKRVKTSLHHSSFMTKDCRA
Protein: Protocadherin related 15 (A0A8I5Y0L1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSPQFALWKCMPHGILLASLLIVSWGQYDDDCKLARGGPPATIVAIDEESRNGTILVDNMLIKGTAGGPDPTIELSLKDNVDYWVLLDPVKQMLFLNSTGRVLDRDPPMNIHSIVVQVQCVNKKVGTVIYHEVRIVVRDRNDNSPTFKHESYYATVNELTPVGTTIFTGFAGDNGATDIDDGPNGQIEYVIQYNPEDPTSNDTFEIPLMLTGNVVLRKRLNYEDKTRYYVIIQANDRAQNLNERRTTTTTLTVDVLDGDDLGPMFLPCVLVPNTRDCRPLTYQAAIPELRTPEELNPILVTPPIQAIDQDRNIQPPSDRPGILYSILVGTPEDYPRFLHMHPRTAELTLLEPVNRDFHQKFDLVIKAEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYNVYVYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGSKGDFVINRTTGLVSIAPGVELVVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAVLLNLQATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFTNSTYTVVVEENLPAGTAFLQIEAKDVDLGANVSYRIRSPEVKHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGTPITTVYAEDADPPGLPASRVRYRVDDVQFPYPASIFDVEEDSGRVITRVNLNEEPTTIFKLVVVAFDDGEPVMSSSATVRILVLHPGEIPRFTQEEYRPPPVSELAARGTVVGVISAAAINQSIVYSIVAGNEDDKFGINNVTGVIYVNSPLDYETRTSYVLRVQADSLEVVLANLRVPSKSNTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFTSVLRVKATDRDTGNYSAMAYRLIIPPIKEGKEGFVVETYTGLIKTAMLFHNMRRSYFKFQVIATDDYGKGLSGKADVLVSVVNQLDMQVIVSNVPPTLVEKKIEDLTEILDRYVQEQIPGAKVVVESIGARRHGDAFSLEDYSKCDLTVYAIDPQTNRAIDRNELFKFLDGKLLDINKDFQPYYGEGGRILEIRTPEAVTSIKKRGESLGYTEGALLALAFIIILCCIPAILVVLVSYRQFKVRQAECTKTARIQSAMPAAKPAAPVPAAPPPPPPPPPPGAHLYEELGESAMYEMPQYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSTGEDSAPESQRSRTHKPSGPSNVNGNIYIAQNGSVVRTRRACIADNLKVPSPVLLGRHRKKLDKLAGTHEENVPLNTLFKGPFATEKVKRTPTLVTFAPCPVVAEHSAAKPSGTRLKNTAEQESMVDSRLSREPMEFHGDNTPSEEEQLWMGPWNSLHIPMTKL
Protein: Ribosomal protein L5 (Ribosomal protein L7) (Ribosomal protein large subunit 5) (Q2F957)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MFPLHFHYEDVLRQDLLLKLNHANVMEVPGLFEIRLVPKAASDFKIQFGKLAMEILCGQRFIQTQRGPYFKAGKSFRSNPFLGSEKDTGYVSDFARQSVLRGHGMYHFLVRILTVMSMLDSPVEIWENSIKFFMETEFCEFSPELEDHFEIFEHIRGFNVTIVTSANTKDETLLLWSGFLLKDEGETK
Protein: S-adenosylmethionine synthase isoform type-1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (Methionine adenosyltransferase I/III) (MAT-I/III) (Q00266)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- Methionine adenosyltransferase 2 subunit beta
- S-adenosylmethionine synthase isoform type-2
- Betaine--homocysteine S-methyltransferase 1
- Methionine synthase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Tyrosine aminotransferase
- Methylenetetrahydrofolate reductase
- DNA
- DNA
- DNA
Sequence:
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDSKTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDTVYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
Protein: Hgt7p (A0A1D8PG81)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- Hexokinase-2
- Regulatory protein MIG1
Sequence:
MSQDNVSSTSTAEAVNNEIKVKDEFPQEEQAHTSLEDKPVSAYIGIIIMCFLIAFGGFVFGFDTGTISGFINMSDFLERFGGTKADGTLYFSNVRTGLMIGLFNAGCAIGALFLSKVGDMYGRRVGIMTAMIVYIVGIIVQIASQHAWYQVMIGRIITGLAVGMLSVLCPLFISEVSPKHLRGTLVCCFQLMITLGIFLGYCTTYGTKSYSDSRQWRIPLGLCFAWALCLVAGMVRMPESPRYLVGKDRIEDAKMSLAKTNKVSPEDPALYRELQLIQAGVERERLAGKASWGTLFNGKPRIFERVIVGVMLQALQQLTGDNYFFYYSTTIFKSVGMNDSFETSIIIGVINFASTFVGIYAIERMGRRLCLLTGSVAMSICFLIYSLVGTQHLYIDKPGGASRKPDGDAMIFMTSLYVFFFASTWAGGVYSIISELYPLKVRSKAMGLANASNWTWGFLISFFTSFITDAIHFYYGFVFMGCLVFSIFFVYFMVYETKGLTLEEIDELYSTKVLPWKSAGWVPPSEEEMATSTGYAGDAKPEEEHV
Protein: Menin (O88559)
Organism: Mus musculus (Mouse)
Function: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression (By similarity). May be involved in normal hematopoiesis through the activation of HOXA9 expression. May be involved in DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:9824159}. Note=May be perinuclear in testis. {ECO:0000269|PubMed:9824159}.
Interaction partners:
- Histone-lysine N-methyltransferase 2A
- Transcription factor JunD
- PC4 and SFRS1-interacting protein
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Catenin beta-1
- WD repeat-containing protein 5
- Mothers against decapentaplegic homolog 3
- Histone-lysine N-methyltransferase 2D
- Histone-lysine N-methyltransferase 2B
Sequence:
MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYQDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLETGEERTGEQAQGTQGQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVHIVSREAEAAEAEEPWGDEAREGRRRGPRRESKPEEPPPPKKPALDKGPGSGQSAGSGPPRKTSGTVPGTTRGGQEVGNAAQAPAPAASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL
Protein: Transcription factor bHLH68 (Basic helix-loop-helix protein 68) (AtbHLH68) (bHLH 68) (Transcription factor EN 60) (bHLH transcription factor bHLH068) (Q8S3D1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor bHLH122
- Transcription factor ABA-INDUCIBLE bHLH-TYPE
- WAT1-related protein At3g45870
- WAT1-related protein At3g18200
- WAT1-related protein At4g30420
Sequence:
MNRGVLESSPVQQLMAAGNPNWWNVSGGMRPPPPLMGHQQAPLPPHMTPNNNYLRPRMMPTPFPHFLPSPATSSSSSSSSPSLPNNPNLSSWLESNDLPPESWSLSQLLLGGLMMGEEERLEMMNHHNHHDEQQHHGFQGKIRLENWEEQVLSHQQASMVAVDIKQEGNINNNNGYVISSPNSPPNKSCVTTTTTTSLNSNDDNINNNNNMLDFSSNHNGLHLSEGRHTPPDRSSECNSLEIGGSTNKKPRLQPSPSSQSTLKVRKEKLGGRIAALHQLVSPFGKTDTASVLSEAIGYIRFLQSQIEALSHPYFGTTASGNMRHQQHLQGDRSCIFPEDPGQLVNDQCMKRRGASSSSTDNQNASEEPKKDLRSRGLCLVPISCTLQVGSDNGADYWAPALGSAGFH
Protein: Protein YfgG (P64545)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeF
Sequence:
MSQATSMRKRHRFNSRMTRIVLLISFIFFFGRFIYSSVGAWQHHQSKKEAQQSTLSVESPVQR
Protein: Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI) (O43014)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphomannomutase
- Glucose-6-phosphate isomerase
- Hexokinase-1
- Hexokinase-2
- ATP-dependent 6-phosphofructokinase
- Probable glutamine--fructose-6-phosphate aminotransferase
- Fructose-1,6-bisphosphatase
- Probable 6-phosphofructo-2-kinase C222.13c
- Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase C144.17c
- Probable 6-phosphofructo-2-kinase PB17E12.14c
Sequence:
MYRLKCDVKSYGWGKVGHESLAAKLAEAGYGFEVDPNTPYAELWMGSHPSGPSFVMQTGKPLSELLTPETVGEKVYKKYGKQLPFLFKVLSINKVLSIQAHPDKPLGKQLHKTNPKEYKDDNHKPEMAVALTEFDALCGFRPVKQIEQFLDSIAPLREFVGEEAVRQFKGTVKQDERKALETLFNELMHKDEKRIQEFTPQLVQLAKSDANNFGGTEYGGKAFSDLIIHLNSQFPDDIGLFVTPFLNYVRLHPGEAVFLRALDPHAYVSGNIIECMAASDNVIRLGFTPKFKDIETLVNNLTYQTADAKSQLTQPVPFAKACGSGKTLLYDPPIEEFSILQTKVSPGQKQCIRGINGPSILLVTEGSGILNGDKGDVASISPGFVYFISANFPLTISATSEPVVVYQAFCEI