wanglab/gogpt-training-data huggingface dataset:
Protein: nucleoside diphosphate phosphatase (EC 3.6.1.6) (Guanosine-diphosphatase ENTPD5) (Uridine-diphosphatase ENTPD5) (E7F8A7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- Inosine triphosphate pyrophosphatase
- nucleoside-triphosphate phosphatase
- UMP-CMP kinase
- Ectonucleoside triphosphate diphosphohydrolase 3
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ectonucleoside triphosphate diphosphohydrolase 8
- GMP synthase
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase subunit M2 B
Sequence:
MSQQMLHLTLVSMWLFAGYFLAEATYYNHHMYNRYRAINHNANMDNQLPPEEPVVMEPVAPRQVNFSRVFYGIMFDAGSSGTRIHIYKFIQKDPVELPVLDNEMYHAVKPGLSAYADMPEKGGESIVQLLKVAKKTIPKEQWIQTPVVLKATAGLRLLPEEKAKALLNEVKEVFDDSPFFVPNNSVTIMNGINEGVLAWVTVNFLTGHLYSKTKRTVGILDLGGGSTQITFLPRLKKTVQSAPSDYIAKINMFNSTYELYTHSYLGNGVFASRLATLGALGADGLEWKVFRSSCLPKKFSEEWSFGGLTYKVSGTPDGYAGYKLCYQEVLQVVKGIVHQPFEVKGSSIFYAFSYYYDRAVESGLIDGSRGGTVEVRDFKKKAKEVCNKMTKYRPISPYLCMDMTYITCLLKDGFGFKDSTVLQLAKKVNNVETSWALGAIFDHFHNFSIQ
Protein: Molybdenum cofactor cytidylyltransferase (MoCo cytidylyltransferase) (EC 2.7.7.76) (CTP:molybdopterin cytidylyltransferase) (Mo-MPT cytidylyltransferase) (Molybdopterin cytidylyltransferase) (Molybdopterin-cytosine dinucleotide synthase) (MCD synthase) (Q46810)
Organism: Escherichia coli (strain K12)
Function: Transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor. Is specific for CTP; other nucleotides such as ATP and GTP cannot be utilized. Is also able to convert MPT to MCD in the absence of molybdate, however, with only one catalytic turnover.
Interaction partners:
- Molybdenum cofactor guanylyltransferase
- Probable hypoxanthine oxidase XdhD
- Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC
- Uncharacterized protein YqeC
- Uncharacterized protein YqeB
- Molybdopterin molybdenumtransferase
- Uncharacterized protein YgfM
- Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- Aldehyde oxidoreductase molybdenum-binding subunit PaoC
- Aldehyde oxidoreductase FAD-binding subunit PaoB
Sequence:
MSAIDCIITAAGLSSRMGQWKMMLPWEQGTILDTSIKNALQFCSRIILVTGYRGNELHERYANQSNITIIHNPDYAQGLLTSVKAAVPAVQTEHCFLTHGDMPTLTIDIFRKIWSLRNDGAILPLHNGIPGHPILVSKPCLMQAIQRPNVTNMRQALLMGDHYSVEIENAEIILDIDTPDDFITAKERYTEI
Protein: Cyclin-A3-2 (G2/mitotic-specific cyclin-A3-2) (CycA3;2) (Q9C6A9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase A-1
- Cell division control protein 6 homolog
- Wee1-like protein kinase
- Cyclin-dependent kinases regulatory subunit 1
- Transcription factor E2FC
- Transcription factor E2FA
Sequence:
MTEQEICVRVTRAAAKRKASTAMGIDGDRVNKKRVVLGELLNVSNVNLLANLNQKKETQKPKRNLKPPPAKQIKSAPVAIIDLESKSDIDSRSDDPQMCGPYVADIYEYLRQLEVKPKQRPLPDYIEKVQKDVTPSMRGVLVDWLVEVAEEYKLGSETLYLTVSHIDRFLSLKTVNKQKLQLVGVSAMLIASKYEEISPPKVDDFCYITDNTFSKQDVVKMEADILLALQFELGRPTINTFMRRFTRVAQDDFKVPHLQLEPLCCYLSELSILDYKTVKFVPSLLAASAVFLARFIIRPKQHPWNQMLEEYTKYKAADLQVCVGIIHDLYLSRRGGALQAVREKYKHHKFQCVATMPVSPELPVTFWEDVTI
Protein: arginine kinase (EC 2.7.3.3) (Q9VF23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Arginase
- arginine kinase
- Arginine kinase 1
- Nitric oxide synthase
- 10 kDa heat shock protein, mitochondrial
- FI13205p
- Cytosol aminopeptidase
- Salto, isoform A
- AT13777p
- Transcriptional cofactor Bfc
Sequence:
MTSIESKRVQYRKYLERAGVIDALSKALIKLYEEQNKPEDAIRFVRKFMCESCPDDAQYDVMKNDLEEAKTHISKLEQELERLRGQIKKSPEEYQELTTEGYKSLMDDEENVSSLLRKYLTPELLEEYMLVTTPAPVDAYLYDCAVSGFEHHDAPVGIFAADADSYDVFNKLFDPIIKDYHGQMDNENDVLQKDPDFGNVDEIENLDPERKYILSARIRLARNIEGLPFFPKLTEKQFIEVEEKVRSATETMDGELIGSYLTMADIDAETQAEMVKRHILFQRGDEKLTTAGCYRFWPTGRGVYHNPAETFLIWVNRQDHVHIMSMAQCGDLGDVYNRLVNGLTELEKTLAFARHPRYGNLTACPTNLGTTLRASVHIRLPLLSKDPDRLLALAEEQQLQVRGTDGGELSTVEDGVMDISNKRKLGFTEFELVKTLQDGVVTLINAEEELEISGQEG
Protein: Heat shock factor-binding protein 1 (Q8K3X8)
Organism: Rattus norvegicus (Rat)
Function: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Heat shock transcription factor 1
- E3 ubiquitin-protein ligase RBX1
- WASH complex subunit 3
Sequence:
MAETDPKTMQDITLVVETLLQQMQDKFQIMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELDAENKIPTAQKS
Protein: Capricious, isoform A (Capricious, isoform B) (RE33792p) (Q9VU53)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRRRAITMSLAPHLGQAFSLCLCLCLCLVLATLPVALGLANCPNGCECDDDTLMVNCGEGTLDVLPIALNPAIQRLVIKNNKLKTIDSSMQFYAQLTFLDLSFNDMLTIPERSFAYHAKLQELHLDHNKIGQVSNKTFLGLSTISVLNLRGNLIAELEYRTFSPMVKLAELNLGQNRISHIDPHALDGLDNLRVLYLDDNTLTTVPGELTFQALHSLAELYLGTNSFMTIPGGAFQDLKGLTRLDLRGAGLHNISGDALKGLVSLRFLDLSDNRLPAIPTAAFQRLGRLEQLNIGQNDFEVISSGAFSGLRELRHLELTGAQRLRRVESGAFSGNTNLEHLNLSSNKQLNELSSIALGGLPHLSTVVLKANQLSSLDEGLVPWADLQTLDLSENPFECDCRLLWLRHLLVSRNASGQYAPVICAYPTALRDLPLAHLAEPLLGCAHGAASKQAIIGILVVACAALITTLALVLYTCRHRIREMLKGHSALGRKEREYQKTFSDEEYMSRPPPGGGGVHPAAGGYPYIAGNSRMIPVTEL
Protein: DSC E3 ubiquitin ligase complex subunit 3 ubiquitin-like domain-containing protein (Q38CJ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVRIRFILTGACPPSYSGKQVQLNFPLEDENGAPTTTAHLKQLIRTQWPENMSEMKEVVEKTEMRVLKTGNLLSDDTQIRSVLTATELSECSINPSAEGSGRADEDQKSVLMHLVFQSNQSQGRQRDGSAGGGRRDNASHDSGCCTML
Protein: Adenylate kinase 9 (A0A2R9YJL3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase.
- Thymidylate kinase
- Cytidine monophosphate
- Ribonucleoside-diphosphate reductase large subunit
- GTP:AMP phosphotransferase AK3, mitochondrial
- Nucleoside diphosphate kinase 7
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase
- Guanylate kinase
Sequence:
MSSDLIVSNLPLVDKLIEDEAERAILLSKPACFIIIGKPGVGKSTLAKKIAKTWNCILIDDTDVLNNHINNETDQGKQLFRILAEGKAVPEEMMVNLIVDRLKSPDIKHYGYVLACLPSISEEYMKIQEQIDLIKTLKMSPDFIINIKCADRDLIRRLSEERQHPETGCVFPKEKWDPDKKESLMKQSNMEEEEEEEEEGEEETTEDLEVEEIEEIQLQKDVIAQLVRVTENYPENVTSRIKCYKDNILRPLEDYMAGHNPPYLFELDGNTDPEELFESVMSHLEFMAVRCPAVPVQLMPTEDAELTDQMEPEELFRTLSSCRNVAPGFPWRTSRWAFNCPVALKEGKVIKGKPEFAVGFMDKIYVLSSDDALQKFMANPRCYLLQPKPHVPCRVSVIGPPRSGKSTMCGLLAEKYGALVVDVRELMERNQGLLKQDMLNKVRHDATIAGLEKVRAKMELEATAIEVTEDHPDVQAFVEEAIKEAAESPAPRELYLDALEKHIKEIEAEDADAESKRGWILDIPSSRSHLITIEEIHGALTPEIIFCLKDNDREGRTVLTRMYERNKEEVDQAVMTRLQNQRNLQKTQDHETLKHSEDSKKDSQYSDTLSKLETVHEESESSDKSDDEGKTPSKNEVVLPTVWENGHPDGPEMDVFKVELKQFVTDWESMEQTITCSYAVLEINNKTPQGILQEMTDHMEKPFKHKAIMTSSADLEEEEEAIHMLIQAEKQDDVVNEEEEQESEEFNFKRQLGDTKHFCPVVLKEKGLLQPCLDEYAAKYRDKVYYFSSKEALEKFLQNPELYISNKELLKPPALRVSMLGVRGSGKTTHGKWLAQQLGIFHIQFRERLQELIQRKTQKRVSPADDSEPPEEPPEELQSLLKAQARIQSAESPTDQDNTTSLEETASGSPDAKEEEALTEDEEAIKAYLQNGDPLPSEILEMLLFQWWNQEPYKSTGFILEGFPQNHEEVSFMAEHHLFPDVVAVMSVEVSEVVRRLLPSRLNRWRERRERKQQQIHLVMKLRKEIRERAITKRRAEIMAEQAFRKLSPPTLSPLKEQEEEEEKEEAVDEEQELEEIEAMLLEEFPPEDEEETEDEEQETEESAEERLEVEISERFEKDDDNLTSMTDLLSDNQIPRLVISAGRLPRIVRYQLLKEIKPLMENRDSLFQTCQPISYSLARRLLYCSFKYPSAFGCWDPVKYTEGDLIQPPQDSYHSTFPVILHQFIYFFASKETRNTFILNPIKYLRQPRPNPSLPIKLAIIGPPKSGKTTVAQAFAREYGLTRLSIGDAIRMVLNSQAKTDLACQVQIHLKQGQTVPDELAIQCVEVAVMNLVCTTRGFVLDGFPVTKHQAELLESCIIPMVVVELQLDTVEVLKRGLRDREKNNRSHQVHHDSLQALNIRNSCFRQEAEALRLHLHNQYHNWTPVDAHKSKWWVQERILDEVRISMRHIHSYLERIHKGQAACINRLCITPQELQSRLGEFGHYCPVSLALHRHLVDCSHNTSLELAAEFKGQFYKMASREFLERFLESPEQFVAPGCPYPLPPASLLPHKLSAGQVKSRFPQQVEMKGFCPVTYLDGKQRYEALLRGNMEYAAEYRNKIYIFESEKKQEQFLRSPETYWDQKLPHKLPPLEEPVLLTSLPILGYLEQSVAVPIIKAMTDVGQLKPKFPFLSVKRSAILYLAFHLKAFNSRNSEYIRQKYKKKLQKFEEGCELISYLSTTMKTYKSPLNLPTEFLQKLDRFLALEKSTKTDSGLIQLGGI
Protein: Enoyl-CoA hydratase 2, peroxisomal (EC 4.2.1.119) (Q8VYI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bidirectional monofunctional enoyl-CoA hydratase 2 involved in the degradation of even cis-unsaturated fatty acids. Devoid of 3-hydroxyacyl-CoA dehydrogenase activity.
Subcellular location: Peroxisome {ECO:0000269|PubMed:16982622, ECO:0000269|PubMed:17951448}.
Interaction partners:
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Peroxisome biogenesis protein 5
- Short-chain dehydrogenase/reductase SDRA
- Probable enoyl-CoA hydratase 1, peroxisomal
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Enoyl-CoA delta isomerase 2, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
Sequence:
MATSDSEFNSDLLLAHKLPETRYTYNERDVAIYALGIGACGQDAVDSDELKFVYHRNGQDLIQVLPTFASLFTLGSLTEGLDLPGFKYDPSLLLHGQQYIEIYRPLPSKASLINKVSLAGLQDKGKAAILELETRSYEEGSGELLCMNRTTVFLRGAGGFSNSSQPFSYKNYPSNQGLAVKIPQRQPLTVCEERTQPSQALLYRLSGDYNPLHSDPEFAKLAGFPRPILHGLCTLGFAIKAIIKCVCKGDPTAVKTISGRFLTTVFPGETLITEMWLEGLRVIYQTKVKERNKTVLAGYVDIRGLSSSL
Protein: RNA-binding protein, putative (Q381C7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTSAGTRDLQTYHLARLLHLVPHLHRVYAENCFLVPLFFSSVSPATKQHAKLILLCLSRRFGSPVAGSICSNIFSFLSFPELVVAPPVSSVGILRDLPVNDNINDSGRGSGAPDAASSEETKPISGRKREREENELETRVRTSEDASESGVVKAVDSVGMVDSAGKDMHTQADSRIEPSLTSAATTSGGQAERSEELDRLFLVRPPVVTTPAALTQLYVRMTSEYQLNEETMNTYFGRYGQVSCVLVREQQVGDDRRSGGVSHVQDFIVTVDSMNNALQAVCYAYYRELTFIALHEPEYNVYTRADVDRVLEEVGVEVVEDPSKGADAAEGGDGGFSHHQSFIPDVVVDGLPYWLTVDQLRACFSEYGTVVDVRISIDDRSGSFTGAALLGMSSVEEAIAASEGLNGATLKGHTLVSGVLDARLNIVSLRHGMVVRRADEMLPEDYDLSENGRRWV
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (A0A140VKE5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPELI
Protein: Ubiquitin-conjugating enzyme E2-21 kDa (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme PEX4) (Peroxin-4) (Ubiquitin carrier protein) (Ubiquitin-protein ligase) (P29340)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis (By similarity). Required for UBC4-independent ubiquitination of PEX5.
Subcellular location: Peroxisome.
Interaction partners:
- Peroxisome assembly protein 22
- Peroxisome assembly protein 12
- Peroxisomal ATPase PEX6
- Peroxisomal ATPase PEX1
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 2
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein PEX15
- Proteasome subunit beta type-6
Sequence:
MPNFWILENRRSYTSDTCMSRIVKEYKVILKTLASDDPIANPYRGIIESLNPIDETDLSKWEAIISGPSDTPYENHQFRILIEVPSSYPMNPPKISFMQNNILHCNVKSATGEICLNILKPEEWTPVWDLLHCVHAVWRLLREPVCDSPLDVDIGNIIRCGDMSAYQGIVKYFLAERERINNH
Protein: Uncharacterized protein YaaY (P75620)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Small ribosomal subunit protein bS20
- Insertion element IS1 1 protein InsB
Sequence:
MCRHSLRSDGAGFYQLAGCEYSFSAIKIAAGGQFLPVICAMAMKSHFFLISVLNRRLTLTAVQGILGRFSLF
Protein: Ghrelin (Ghrelin-21) (Q8JFY4)
Organism: Anguilla japonica (Japanese eel)
Function: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRQMKRTAYIILLVCVLALWMDSVQAGSSFLSPSQRPQGKDKKPPRVGRRDSDGILDLFMRPPLQDEDIRHITFNTPFEIGITMTEELFQQYGEVMQKIMQDLLMDTPAKE
Protein: Exocyst complex component SEC3A (AtSec3a) (Q9SX85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23495664, ECO:0000269|PubMed:24307681}. Cell membrane {ECO:0000305|PubMed:23495664}; Peripheral membrane protein {ECO:0000305|PubMed:23495664}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:23495664}. Secreted, extracellular exosome {ECO:0000269|PubMed:24307681}. Note=In interphase, SEC3A localizes to the cytoplasm and plasma membrane, where it forms immobile, punctate structures. Localizes to the early cell plate and completed division wall during cytokinesis (PubMed:23495664). Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). {ECO:0000269|PubMed:23495664, ECO:0000269|PubMed:24307681}.
Interaction partners:
- Exocyst complex component SEC5A
- Exocyst complex component SEC8
- Exocyst complex component SEC5B
- Exocyst complex component SEC6
- Exocyst complex component SEC15B
- Exocyst complex component SEC10a
- Exocyst complex component EXO84B
- Exocyst complex component EXO84C
- Exocyst complex component EXO84A
- Exocyst complex component SEC15A
Sequence:
MAKSSADDEELRRACEAAIEGTKQSIVMSIRVAKSRGVWGKSGKLGRQMAKPRVLALSVKSKGPRKKAFLRVMKYSSGGVLEPAKMYKLKHLSKVEVITNDPSGCTFTLGFDNLRSQSVAPPQWTMRNTDDRNRLLVCILNICKDVLGRLPKVVGIDIVEMALWAKDNTPVVTTQRSTEDGEPVAESVTESDLKVTVEKELVSQAEEEDMEALLGTYVMGIGEAEAFSERLKRELQALEAANVHAILESEPLVDEVLNGLEAATNIVDDMDEWLGIFNIKLRHMREDIESIETRNNKLEMQSVNNKALIEELDKVIERLRVPSEYAASLTGGSFDEADMLQNIEACEWLAKALRGLEVPNLDPIYANMRAVKEKRAELEKLKATFVRRASEFLRNYFASLVDFMVSDKSYFSQRGQLKRPDHADLRYKCRTYARLLQHLKGLDKNCLGPLRKAYCSSLNLLLRREAREFANELRASTKVSRNPTVWLEGSTGSSQNANTDTSAVSDAYAKMLTIFIPLLVDESSFFAHFMCFEVPALAPPGGAGNDKKSQSNNDDGNDDDDLGIMDIDETDKKPGKNSPDLTALNESLQDLLDGIQEDFYAVVDWAYKIDPLRCISMHGITERYLSGQKADAAGFVRLLLGDLESRVSMQFSRFVDEACHQIERNERNVRQMGVLPYIPRFAALATRMEQYIQGQSRDLVDQAYTKFVSIMFVTLEKIAQQDPKYADILLLENYAAFQNSLYDLANVVPTLAKFYHQASEAYEQACTRHISMIIYYQFERLFQFAKKIEDFMYTITPEEIPFQLGLSKVELRKMLKSSLSGVDKSIAAMYKKLQKNLASEELLPSLWDKCKKEFLDKYESFVQLVAKVYPSENVPGVTEMRGLLASM
Protein: Uncharacterized protein (Q57W16)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MSGHRHLGGPSLTQNQGNVLGERPCVRQSRLYREHNGGNTMKELMGQGDLKWDTTCVQGAYAGGKIFDHRKGEQENNEPIRGVCNQKHQHQYQYQHQQQQYCHTEDEDGAELDEEEAADHSFQHYGVNNNTAEHHPSQDVEAQDEYYGVVIEMDDGVEQGGGVDYRAEEKEEEAEKQPTEPIKKQIAPAGVRRGVMEPKAEAPTCQPVAYRSFRPGAGHANRQTYNIFTGE
Protein: Mating-type P-specific polypeptide Pc (P10841)
Organism: Schizosaccharomyces pombe (Fission yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Required for conjugation and efficient meiosis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDPRLRAPIFLPILTPETLQKKKQIKGNKTTIYKNGFMLFRSRLHKILNLSGDWAGASAKCSIIWHTLPQNVRLAWSQLAELSHYQDVRRQIAKLERILYSKRLNGHNNYKLHISRVQ
Protein: Histone-lysine N-methyltransferase PRDM16 (EC 2.1.1.367) (PR domain zinc finger protein 16) (PR domain-containing protein 16) (Transcription factor MEL1) (MDS1/EVI1-like gene 1) (A2A935)
Organism: Mus musculus (Mouse)
Function: Binds DNA and functions as a transcriptional regulator. Displays histone methyltransferase activity and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. Probably catalyzes the monomethylation of free histone H3 in the cytoplasm which is then transported to the nucleus and incorporated into nucleosomes where SUV39H methyltransferases use it as a substrate to catalyze histone H3 'Lys-9' trimethylation. Likely to be one of the primary histone methyltransferases along with MECOM/PRDM3 that direct cytoplasmic H3K9me1 methylation. Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism. Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells. Functions as a repressor of TGF-beta signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:18483224}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAZ2}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
- CCAAT/enhancer-binding protein beta
- Zinc finger protein 516
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Histone-lysine N-methyltransferase EHMT1
- C-terminal-binding protein 1
- Lysine-specific histone demethylase 1A
- C-terminal-binding protein 2
- Lipid transferase CIDEA
- Mitochondrial brown fat uncoupling protein 1
Sequence:
MRSKARARKLAKSDGDVVNNMYEPDPDLLAGQSAEEETEDGILSPIPMGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEMLTDTEVSSQESCIKKQISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAPSLDEDPTFRCDECDELFQCRLDLRRHKKYACSSAGAQLYEGLGEELKPEGLGVGSDGQAHECKDCERMFPNKYSLEQHMIVHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKRFECENCVKVFTDPSNLQRHIRSQHVGARAHACPDCGKTFATSSGLKQHKHIHSTVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHYTPGSIFTPGLPLTPSPMMDKTKPSPTLNHGGLGFSEYFPSRPHPGSLPFSAAPPAFPALTPGFPGIFPPSLYPRPPLLPPTPLLKSPLNHAQDAKLPSPLGNPALPLVSAVSNSSQGATAATGSEEKFDGRLEDAYAEKVKNRSPDMSDGSDFEDINTTTGTDLDTTTGTGSDLDSDLDSDRDKGKDKGKPVESKPEFGGASVPPGAMNSVAEVPAFYSQHSFFPPPEEQLLTASGAAGDSIKAIASIAEKYFGPGFMSMQEKKLGSLPYHSVFPFQFLPNFPHSLYPFTDRALAHNLLVKAEPKSPRDALKVGGPSAECPFDLTTKPKEAKPALLAPKVPLIPSSGEEQPLDLSIGSRARASQNGGGREPRKNHVYGERKPGVSEGLPKVCPAQLPQQPSLHYAKPSPFFMDPIYRVEKRKVADPVGVLKEKYLRPSPLLFHPQMSAIETMTEKLESFAAMKADSGSSLQPLPHHPFNFRSPPPTLSDPILRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCNRCFGQQTNLDRHLKKHEHEGAPVSQHSGVLTNHLGTSASSPTSESDNHALLDEKEDSYFSEIRNFIANSEMNQASTRMDKRPEIQDLDSNPPCPGSASAKPEDVEEEEEEELEEEDDDSLAGKSQEDTVSPTPEPQGVYEDEEDEEPPSLTMGFDHTRRCVEERGGGLLALEPTPTFGKGLDLRRAAEEAFEVKDVLNSTLDSEVLKQTLYRQAKNQAYAMMLSLSEDTPLHAPSQSSLDAWLNITGPSSESGAFNPINHL
Protein: Reticulon-like protein (Q9VMW1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}.
Interaction partners:
Sequence:
MAAGLEQLQGLLQSLGELKDLPLNRESLESLIYWRDVKKSGIVFGAGLITLAAISSFSVISVFAYLSLLTLFGTVAFRIYKSVTQAVQKTNEGHPFKDYLELDLTLSHEKVQNIAGVAVAHINGFISELRRLFLVEDIIDSIKFGVILWVFTYVGAWFNGMTLVILAFVSLFTLPKVYENNKQSIDTHLDLVRSKLTEITDKIRVAIPIGNKKPEAAAESEKDK
Protein: 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Protein dhp1) (P40848)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the processing of nuclear mRNA and rRNA precursors. May promote the termination of transcription by RNA polymerase II (By similarity). Essential for vegetative cell growth and chromosome segregation. Possesses 5'->3' exoribonuclease activity.
Subcellular location: Nucleus.
Interaction partners:
- Decapping nuclease din1
- UPF0400 protein C337.03
- 5'-3' exoribonuclease 1
- Exosome complex exonuclease rrp6
- Polynucleotide 5'-hydroxyl-kinase grc3
- Rpb7-binding protein seb1
- Exosome complex exonuclease dis3
- Exosome complex component rrp45
- Exosome complex component rrp46
- Uncharacterized protein C4G9.04c
Sequence:
MGVPALFRLLSRKFAKVITPVIEAPTEKLPDGTEIEPDLSLPNPNGVECDNLYLDMNGIVHPCSHPEDRPAPETEDEMMVAVFEYTDRILAMVRPRQLLFIAIDGVAPRAKMNQQRSRRFRSSREAALKEEELQAFIEEAKQQGIPIDENATKKKSWDSNCITPGTPFMDTLAKSLRYYIINKLNSDPCWRNVRFILSDASVPGEGEHKIMEFIRSQRVKPEYDPNTHHVVYGLDADLIMLGLATHEPHFRVLREDVFFQQGSTKKTKEERLGIKRLDDVSETNKVPVKKPFIWLNVSILREYLEVELYVPNLPFPFDLERAIDDWVFFIFFVGNDFLPHLPSLDIRDGAVERLTEIWRASLPHMGGYLTLDGSVNLARAEVILSAVGNQEDDIFKRLKQQEDRRNENYRRRQQRESNQESESYVDNVVIQRSVETQSTEVVTSSKSTSVDTKPPKKTQKIDAPAPVDLVNLSEKTSNRSLGATNRELINNRAANRLGLSREAAAVSSVNKLAASALKAQLVSNETLQNVPLEDSIASSSAYEDTDSIESSTPVVHPIDTKVSNVGQKRKAPDSTEENENTDTVRLYEPGYRERYYEQKFHISPDEPEKIREAVKHYVHGLCWVLLYYYQGCPSWTWYYPYHYAPFAADFKDLASIDVKFELNQPFKPYEQLLGVLPAASKNNLPEKLQTLMTDENSEIIDFYPENFTIDLNGKKFEWQGVALLPFIDENRLLNAVSKIYPQLTEEESKRNEDGSTLLFISEHHPMFSELVKQLYSKKRQGKPLKLSGKMAHGLFGKVNTNDSVIPNVSVQCPIDVTSADALQKYGSIDDNQSISLVFEVPKSHFVHKSMLLRGVKMPNRVLTPEDINQVRAERSFSSRRNNGNSYRGGHQSYGVRRSYQSQSYSSRQSYTGVTNGFANGGVQPPWSGNGNFPRSNASYNSRGGHEGYGGRSRGGGYSNGPPAGNHYSSNRGKGYGYQRESYNNNNRNGYY
Protein: Dynein axonemal assembly factor 3 homolog (Dynein assembly blocked protein 1) (Paralyzed flagella protein 22) (F5A894)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22387996}.
Interaction partners:
Sequence:
MDEHNVHHFWGISPAVDLGTLLPTGDGAADLPVDQPVRFLQVAPYDARHTLTTLSRACRHPALMRQLPPGQPACRLYVWEDSPEGLARHVLLAAVLLDGGVPAAQRGQLLLELHGNAVLRRRAAEYLDEKARQLESLFVGLAAGQPPPAGPEAEARGLAALAALLDLSLLKFQEKDLIVEALQRWRLPNPTSSTSTSAASASAAAAPYDMVAAWDGRCRKVYGERYDFRRNMVDWDYHMRLQPAGTPGCDPASGSIIHFHHFRHWRLHGVAHELRDSAYNSANRCRGEGGVGEFKDRTGRDVGRSVSAWGFWADVLNSPYHAFGTACEQPEFYRITNKQFVRTAVDVAEHNIAALLHELRTGRRLELGEGQEAHRAQAARGPTTLEDLTAAAEEAAAAASGAGAEAGAGAGPGGEAAAGASSSSGKEEAAAAAAAGKEQGQGEGQGEDWTAGSGSGAPGAGTGQAVAEGREGPGGPQDSDPAAAASTAAPAAAAAAASSSSTSVPTYSSGGRAQVAKAMAAAAAAAGAGAGAGAEASSSGAASAASAAPTAGASSGAADGKAAEAAAAPLDEAAREQMAAEEAAVRAAEAALDAAARQRAGRFRLVLVTGDLAKTLTGRAKYAGAFSGLSLGHRHTHMLEPQYKLAAAAAPGARLVAENARHVLQLSQEQAALFAAKMDELAAAGGWRPLPAAQRPPGITEAAAVYVRAA
Protein: Keratocan (KTN) (Keratan sulfate proteoglycan keratocan) (O60938)
Organism: Homo sapiens (Human)
Function: May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Mimecan
- Growth-regulated alpha protein
- Carbohydrate sulfotransferase 6
- Carbohydrate sulfotransferase 1
- Protein phosphatase 3 catalytic subunit alpha
- Lumican
- Aggrecan core protein
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Bleomycin hydrolase
- UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7
Sequence:
MAGTICFIMWVLFITDTVWSRSVRQVYEVHDSDDWTIHDFECPMECFCPPSFPTALYCENRGLKEIPAIPSRIWYLYLQNNLIETIPEKPFENATQLRWINLNKNKITNYGIEKGALSQLKKLLFLFLEDNELEEVPSPLPRSLEQLQLARNKVSRIPQGTFSNLENLTLLDLQNNKLVDNAFQRDTFKGLKNLMQLNMAKNALRNMPPRLPANTMQLFLDNNSIEGIPENYFNVIPKVAFLRLNHNKLSDEGLPSRGFDVSSILDLQLSHNQLTKVPRISAHLQHLHLDHNKIKSVNVSVICPSPSMLPAERDSFSYGPHLRYLRLDGNEIKPPIPMALMTCFRLLQAVII