wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic initiation factor 4F subunit p130 (eIF-4F p130) (eIF4F p130) (Translation initiation factor 4(4)-F(6) subunit gamma(3) protein 2) (eIF4G2) (mRNA cap-binding protein complex subunit p130) (P39936)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4632 is probably essential when TIF4631 is missing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyadenylate-binding protein, cytoplasmic and nuclear
- ATP-dependent RNA helicase eIF4A
- Eukaryotic translation initiation factor 4E
- Protein NAM8
- U1 small nuclear ribonucleoprotein A
- Eukaryotic initiation factor 4F subunit p150
- Nuclear cap-binding protein complex subunit 1
- Nuclear cap-binding protein subunit 2
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- ATP-dependent RNA helicase DED1
Sequence:
MTDQRGPPPPHPQQANGYKKFPPHDNQYSGANNSQPNNHYNENLYSAREPHNNKQYQSKNGKYGTNKYNNRNNSQGNAQYYNNRFNNGYRLNNNDYNPAMLPGMQWPANYYAPQMYYIPQQMVPVASPPYTHQPLNTNPEPPSTPKTTKIEITTKTGERLNLKKFHEEKKASKGEEKNDGVEQKSKSGTPFEKEATPVLPANEAVKDTLTETSNEKSTSEAENTKRLFLEQVRLRKAAMERKKNGLISETEKKQETSNHDNTDTTKPNSVIESEPIKEAPKPTGEANEVVIDGKSGASVKTPQHVTGSVTKSVTFNEPENESSSQDVDELVKDDDTTEISDTTGGKTVNKSDDETINSVITTEENTVKETEPSTSDIEMPTVSQLLETLGKAQPISDIYEFAYPENVERPDIKYKKPSVKYTYGPTFLLQFKDKLKFRPDPAWVEAVSSKIVIPPHIARNKPKDSGRFGGDFRSPSMRGMDHTSSSRVSSKRRSKRMGDDRRSNRGYTSRKDREKAAEKAEEQAPKEEIAPLVPSANRWIPKSRVKKTEKKLAPDGKTELFDKEEVERKMKSLLNKLTLEMFDSISSEILDIANQSKWEDDGETLKIVIEQIFHKACDEPHWSSMYAQLCGKVVKDLDPNIKDKENEGKNGPKLVLHYLVARCHEEFEKGWADKLPAGEDGNPLEPEMMSDEYYIAAAAKRRGLGLVRFIGYLYCLNLLTGKMMFECFRRLMKDLNNDPSEETLESVIELLNTVGEQFEHDKFVTPQATLEGSVLLDNLFMLLQHIIDGGTISNRIKFKLIDVKELREIKHWNSAKKDAGPKTIQQIHQEEEQLRQKKNSQRSNSRFNNHNQSNSNRYSSNRRNMQNTQRDSFASTKTGSFRNNQRNARKVEEVSQAPRANMFDALMNNDGDSD
Protein: Osteocalcin (OG1) (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein) (P86546)
Organism: Mus musculus (Mouse)
Function: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.
Subcellular location: Secreted {ECO:0000269|PubMed:17693256, ECO:0000269|PubMed:20655470, ECO:0000269|PubMed:20655471, ECO:0000269|PubMed:21333348, ECO:0000269|PubMed:24074871}.
Interaction partners:
- Osteopontin
- Osteocalcin-2
- Runt-related transcription factor 2
- SPARC
- Integrin-binding sialoprotein
- Osteocalcin-related protein
- Tumor necrosis factor ligand superfamily member 11
- Parathyroid hormone
- Transcription factor Sp7
- G-protein coupled receptor family C group 6 member A
Sequence:
MRTIFLLTLLTLAALCLSDLTDAKPSGPESDKAFMSKQEGNKVVNRLRRYLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Protein: Eukaryotic translation initiation factor 4B (F8VP89)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVSKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEESIKEFFRGLNISAVRLPREPSNPERLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDRSFGRDRNRDSDKTDTDWRARPATDSFDDYPPRRGDDSFGDSYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDY
Protein: Bromodomain-containing protein 9 (Q3UQU0)
Organism: Mus musculus (Mouse)
Function: Plays a role in chromatin remodeling and regulation of transcription. Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Orchestrates also the RAD51-RAD54 complex formation and thereby plays a role in homologous recombination (HR).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H8M2}.
Interaction partners:
- BRD4-interacting chromatin-remodeling complex-associated protein
- BRD4-interacting chromatin-remodeling complex-associated protein-like
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- AT-rich interactive domain-containing protein 2
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Actin-like protein 6A
Sequence:
MGKKHKKHKAEWRSSYEDYTDTPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHREKKKKKKKKSEKEKHLDEEERRKRKEEKKRKREKEHCDSEGEADAFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQRLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKAALLGSEDPAAEEPVPEVVPVQVETTKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKKLGDGSLLYSVVNAPEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSASTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKMVDDLLDQITGGDHSRMIFQLKQRRSIPMRPADEMKVGDPLGESGGPVLDFMSMKQYPDVSLDVSMLSSLGKVKKELDHEDSHLNLDETARLLQDLHEAQAERGGSRPSSNLSSLSTASEREHPPPGSPSRLSVGEQPDVAHDPYEFLQSPEPAAPAKN
Protein: Palmitoyltransferase ZDHHC12 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 12) (DHHC-12) (Zinc finger DHHC domain-containing protein 12) (Q8VC90)
Organism: Mus musculus (Mouse)
Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Has a palmitoyltransferase activity toward gephyrin/GPHN, regulating its clustering at synapses and its function in gamma-aminobutyric acid receptor clustering. Thereby, indirectly regulates GABAergic synaptic transmission.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25025157}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96GR4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALWPPLNSGMLVRTGHTVLTWGITLVLFLHDTELRQWEEQGELLLPLTFLLLVLSSLLLYLAVSLMDPGYVTTQPQPQGEPKEEQAAMVPQAVPLRRCRHCLVLQPLRARHCRDCRRCVRRYDHHCPWMENCVGERNHPLFVAYLALQLVVLLWGLCLAWSGLQFFQPWGLWLRSTGLLFTTFLLLSFFALVVALLLASHLYLVARNTTTWEFISSHRIAYLRQRTSNPFDRGPTRNLAHFFCGWPSGPWETLSAEEEEEGSSQVV
Protein: Estradiol 17 beta-dehydrogenase 5 (EC 1.1.1.-) (17-beta-HSD 5) (P70694)
Organism: Mus musculus (Mouse)
Function: Active toward androgens, estrogens, and xenobiotic substrates. Also exhibits low 20 alpha-HSD activity. Shows a-stereospecificity in hydrogen transfer between cofactors and substrates (A-specific). Preferentially catalyzes the reduction of 4-androstenedione, 5-alpha-androstane-3,17-dione, androsterone and dehydroepiandrosterone to testosterone, dihydrotestosterone, 5-alpha-androstane-3-alpha,17-beta-diol and 5-androstene-3-beta,17-beta-diol, respectively.
Interaction partners:
- UDP-glucuronosyltransferase
- Carboxylesterase 3B
- Histidine-rich glycoprotein
- Carboxylesterase 1C
- Alanine--glyoxylate aminotransferase
- Cytochrome P450 2C50
- Apolipoprotein A-V
- Cytochrome P450 2A12
- Cytochrome P450 2C37
- Cytochrome P450 2C54
Sequence:
MDSKQQTVRLSDGHFIPILGFGTYAPQEVPKSKATEATKIAIDAGFRHIDSASMYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFHRPELVRVCLEQSLKQLQLDYVDLYLIHFPMAMKPGENYLPKDENGKLIYDAVDICDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILKKPGLKYKPVCNQVECHPYLNQGKLLDFCRSKDIVLVAYSALGSHREKQWVDQSSPVLLDNPVLGSMAKKYNRTPALIALRYQLQRGVVVLAKSFSEKRIKENMQVFEFQLTSEDMKVLDDLNKNIRYISGSSFKDHPDFPFWDEY
Protein: Uncharacterized protein (Q581V3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MRRFMSLGRCVTMVERVGTGDHRGAAAIRRCKIPPTHVSNGQLEELHKSGMEFFEKGDFRKAISAWEAVLTANDGGGGGNSTTLMNCLNNLACAYGETGDHARKLKLLERSRDMVAHVYGDDHPQYGMVLYNMASAQEEMGQYQEMEDLLQRSLALHERKFNADHPKVGRVLLLLAEAHGYLGKHEAQLQVAERADKIIRRHCGANHIQTTVAMLTLARAHGANGNSFQRLQLAQQAYDIQETRLGGMNPQLAVTLVELASACGANGDHFRRKELLEKAIDVQKRAFGSQHTFLVKTYTALGDTYGDLGEKENQAASYCEALEIARQRYEGNHITLGTAAAKCALGCARVGNMKKARALVKEARAIIEATASETHPAAAQLRHIQKEVEETSRAKDGW
Protein: Uncharacterized protein (Q585C5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- T. brucei spp.-specific protein
- Uncharacterized protein
- Uncharacterized protein
- EF-hand domain-containing protein
Sequence:
MECASQEFALLQHLKVSIPNDPVPPQPKAQAVRNTHRVMSPCRRPPVSQKVARIATAVNTKKELQAPRAPMAEFSGEVMTVVGKNNRPNVEYLIYDAKIPSRNAINMQLAEVKKQRAMGEKVRHRCHRHEVDAWGERDDAKCKQRLLKSLQEVNMEQAHRTRAEREAQQRRRMETEANGIESYTVACNALDPEKTIEGKKALRDQLQQAAFESLDNHKKGEPVEGAAWDLHYEPFPWNNDTRRKRIQRDRCVALMDANRELAEKKRDERQRQRAMEAAWNYGGGKGVSFGGKRYAHDVGRNPSLQAARGSDDGAVEEGAAALSFGQPTECFFRFEGDNPSVRWNECRKLAEVNKQLAEQAERIRKGERLERIEGEKKFNQYIERIEREEKQSRRAEKLKRQKAMSMVTRDASKKKEGLKKVSSANECHDKFLLYSAHEREEKNRLKREQEFYDNLEKHIASSREAQRAAKDRALEEEKRLLQETISETKRYTEEENRKAKQKREAYKAALEKQIREKSNEASHSSPMPHRGPEVRVLYRCPVTKDLLPPEEFVPAASLRRTSTLW
Protein: Reaction center protein L chain (Photosynthetic reaction center L subunit) (D2Z0P3)
Organism: Thermochromatium tepidum (Chromatium tepidum)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MAMLSFEKKYRVRGGTLIGGDLFDFWVGPFYVGFFGVVGFCFTLLGVLLIVWGATIGPTGPTSDLQTYNLWRISIAPPDLSYGLRMAPLTEGGLWQIITICAAGAFISWALREVEICRKLGIGFHVPFAFSFAIGAYLVLVFVRPLLMGAWGHGFPYGILSHLDWVSNVGYQFLHFHYNPAHMLAISFFFTNCLALSMHGSLILSVTNPQKGEPVKTSEHENTFFRDIVGYSIGALAIHRLGLFLALSAAFWSAVCILISGPFWTRGWPEWWNWWLELPLW
Protein: ADAM metallopeptidase with thrombospondin type 1 motif 4 (Q5VTW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQVRPQSAPQAMHCTILRSATT
Protein: Low-affinity iron/zinc ion transport protein fet4 (Q9HFE1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for Fe(2+) ion low affinity uptake (By similarity). Has a role in zinc uptake under conditions of zinc limitation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Cell membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Localizes to the cell tip and barrier septum.
Interaction partners:
- Zinc-regulated transporter 1
- Probable zinc transporter zrg17
- Manganese transporter pdt1
- Adenosine 5'-monophosphoramidase hnt1
- Zinc finger protein C25B8.19c
- Metallothionein zym1
- Copper-transporting ATPase ccc2
Sequence:
MTASITEIDSISEESNVESVSHLQHSPSFEKKGADFSISLNEKKDFASPITEEIPSPDGIATPEPETKKKLSFGARVWDLICSPGRQHDVCVAAPTQLVRSCDDYANSASTLVTNDDGTKTKVDSDEKKHKHKNVRDYIRFKHVDIGGRIFDLITRLAGTSFTFILMLIILIVWAIVGGIYRAPDNWQIVMQDGSSIQCYVSDTLLMRQQQNQHIQVLTMISQLRSRLLTTSRLLGPVLNDKTKISSVNVALMKDDVGDAEKLPTENWFDFICNYVSFMVGSIIFLVVYWIGIFIWIGFGRMLGWSDEWQLYINTAVAVELTFTSVFLQNVRHRHMKYIDRCVTSIFRIDSVIEEELRRMMGDKEPNEEITIKMDKINLGERSIDYYADLIGSGVGVVVSTCVFVAWIAIGNVMHWDSNWWLIIGTYTGLVGFLDGFVLRNVYFRESSKEATEIQTLIDEDYALYQKLDLPLPHEHITNYKSTFGGSLSQWIGWLCALPISVLFSVFVILGLIIAAGSLRFNETAQLFCNTPTMIIEGALLIVLIEAHNIANLKRRIQFRQIHLRRLTILKMLAGDNYSTTSTV
Protein: Putrescine transporter PotE (Putrescine-proton symporter / putrescine-ornithine antiporter) (P0AAF1)
Organism: Escherichia coli (strain K12)
Function: Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9045651, ECO:0000305|PubMed:1939141}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02073}.
Interaction partners:
- Inducible ornithine decarboxylase
- Constitutive ornithine decarboxylase
- Putrescine importer PuuP
Sequence:
MSQAKSNKMGVVQLTILTMVNMMGSGIIMLPTKLAEVGTISIISWLVTAVGSMALAWAFAKCGMFSRKSGGMGGYAEYAFGKSGNFMANYTYGVSLLIANVAIAISAVGYGTELLGASLSPVQIGLATIGVLWICTVANFGGARITGQISSITVWGVIIPVVGLCIIGWFWFSPTLYVDSWNPHHAPFFSAVGSSIAMTLWAFLGLESACANTDVVENPERNVPIAVLGGTLGAAVIYIVSTNVIAGIVPNMELANSTAPFGLAFAQMFTPEVGKVIMALMVMSCCGSLLGWQFTIAQVFKSSSDEGYFPKIFSRVTKVDAPVQGMLTIVIIQSGLALMTISPSLNSQFNVLVNLAVVTNIIPYILSMAALVIIQKVANVPPSKAKVANFVAFVGAMYSFYALYSSGEEAMLYGSIVTFLGWTLYGLVSPRFELKNKHG
Protein: Transketolase-1, chloroplastic (TK) (EC 2.2.1.1) (Q8RWV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively (By similarity). Could act as a stress sensor involved in adaptation process.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Aldolase-type TIM barrel family protein
- transaldolase
- Ribulose-5-phosphate-3-epimerase, chloroplastic
- Sedoheptulose-1,7-bisphosphatase, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Ribulose-phosphate 3-epimerase
- Ribulose-phosphate 3-epimerase
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Fructose-1,6-bisphosphatase, cytosolic
- Glucose-6-phosphate isomerase, cytosolic
Sequence:
MASTSSLALSQALLARAISHHGSDQRGSLPAFSGLKSTGSRASASSRRRIAQSMTKNRSLRPLVRAAAVETVEPTTDSSIVDKSVNSIRFLAIDAVEKAKSGHPGLPMGCAPMAHILYDEVMRYNPKNPYWFNRDRFVLSAGHGCMLLYALLHLAGYDSVQEEDLKQFRQWGSKTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDAEVVDHYTYAILGDGCQMEGISNEACSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTENVDQRFEALGWHVIWVKNGNTGYDEIRAAIKEAKTVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVEATRNNLGWPYEPFQVPDDVKSHWSRHTPEGATLESDWSAKFAAYEKKYPEEASELKSIITGELPAGWEKALPTYTPESPGDATRNLSQQCLNALAKVVPGFLGGSADLASSNMTLLKAFGDFQKATPEERNLRFGVREHGMGAICNGIALHSPGLIPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHIASFRAMPNTLMFRPADGNETAGAYKIAVTKRKTPSILALSRQKLPHLPGTSIEGVEKGGYTISDDSSGNKPDVILIGTGSELEIAAQAAEVLRKDGKTVRVVSFVCWELFDEQSDEYKESVLPSDVSARVSIEAASTFGWGKIVGGKGKSIGINSFGASAPAPLLYKEFGITVEAVVDAAKSFF
Protein: Homeobox protein Hox-B1b (Homeobox protein Hox-A1) (Q90423)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sequence-specific transcription factor. Part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P09022}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
- Pbxy homeodomain protein
- Homeobox protein Meis3
- Early growth response protein 2b
- E3 SUMO-protein ligase EGR2a isoform 1
- Protein phosphatase 1, regulatory
Sequence:
MNSYLDYTIYNRGSNTYSSKVGCFPVEQEYLPSACASTNSYIPEGRPVGGNTFTSAPHETHGTSYAQIQSQPFHLNVDMGKTGHSNFCKQTRPPHSDYGHQHVLTQADDHMRLQSPGFSVVNMGANIGTYSESNCRPGSVSASHYQSYAYGEPEPHGYGSFSKYQVSPDSDSDSKTNIKQAPTFDWMKVKRNPPKTVKVAEYGIHGQQNIIRTNFTTKQLTELEKEFHFNKYLTRARRVEVAATLELNETQVKIWFQNRRMKQKKREKEGTAPVIKRVTLCSSGQNADHSTSSSPGASPTSDSSTAI
Protein: L-ascorbate peroxidase 2, cytosolic (EC 1.11.1.11) (L-ascorbate peroxidase 1b) (APX1b) (AtAPx02) (Q1PER6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in hydrogen peroxide removal.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9144965}.
Interaction partners:
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Heat stress transcription factor A-2
- Monodehydroascorbate reductase 3
- Glutathione S-transferase DHAR2
- Heat shock protein 21, chloroplastic
- 18.1 kDa class I heat shock protein
- Heat stress transcription factor A-3
- 22.0 kDa heat shock protein
- Heat stress transcription factor A-1b
- Galactinol synthase 1
Sequence:
MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELGFADKE
Protein: Nucleolar protein 16 (P40007)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome biogenesis protein YTM1
- Ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- 27S pre-rRNA
- Ribosome production factor 1
- Ribosomal RNA-processing protein 1
- Ribosome biogenesis protein ERB1
- Ribosome biogenesis protein NSA1
- Ribosome biogenesis protein BRX1
- Ribosome biogenesis protein RLP7
Sequence:
MTSVRKRKMNRSSVGKATRRNKDKQRKINIQSNPIIAANWDYSLTMAQNYKKLGLRAKLQTPAGGKEADLSKVVKRIPLTKPVLDEDEDEDEGEDEQNDYNAATVELDENEIPEGGARIQRDKNGDVVRVVYGKKKNFDADEDVNEIKARDTTEETEVVKKLEELASRPVIRKERSQSEREEEWLEKLYKKHGDDYKKMFFDKKLNIYQQSEGDLKRRLLRWKKRNGIASK
Protein: Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) (Q93099)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of homogentisate to maleylacetoacetate.
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Maleylacetoacetate isomerase
- 4-hydroxyphenylpyruvate dioxygenase-like protein
- Fumarylacetoacetase
- Phenylalanine-4-hydroxylase
- Coagulation factor XIII B chain
- Tyrosine aminotransferase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Oxaloacetate tautomerase FAHD2A, mitochondrial
- Oxaloacetate tautomerase FAHD1, mitochondrial
Sequence:
MAELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFTCPRSTNKRSWLYRILPSVSHKPFESIDEGQVTHNWDEVDPDPNQLRWKPFEIPKASQKKVDFVSGLHTLCGAGDIKSNNGLAIHIFLCNTSMENRCFYNSDGDFLIVPQKGNLLIYTEFGKMLVQPNEICVIQRGMRFSIDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQGKLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTVLTAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGHYEAKQGGFLPGGGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMFESSLSLAVTKWGLKASRCLDENYHKCWEPLKSHFTPNSRNPAEPN
Protein: Maternal embryonic leucine zipper kinase (EC 2.7.11.1) (Protein kinase PK38) (mPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2) (Q61846)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Chromosome-associated kinesin KIF4
- Lymphokine-activated killer T-cell-originated protein kinase
- G2/mitotic-specific cyclin-B2
- Baculoviral IAP repeat-containing protein 5
- Disks large-associated protein 5
- Cyclin-A2
- Forkhead box protein M1
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Kinetochore protein NDC80 homolog
Sequence:
MKDYDELLKYYELYETIGTGGFAKVKLACHVLTGEMVAIKIMDKNALGSDLPRVKTEIDALKSLRHQHICQLYHVLETKNKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQILSAVAYVHSQGYAHRDLKPENLLFDENHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYEVPKWLSPSSILLLQQMLQVDPKKRISMRNLLNHPWVMQDYSCPVEWQSKTPLTHLDEDCVTELSVHHRSSRQTMEDLISSWQYDHLTATYLLLLAKKARGKPARLQLLSFSCGTASTTPKSKNLSLEDMSTSDDNCVAGLIDYELCEDKLLAPKTPQVTKHLAESNHAASKSPAPGVRRAVANKLMDKENVCTPKSSVKNEEQFVFSEPKIPVSKNQYKREIPASPTRFPTPAKARAQCLREAPVRTPGNSAGADTLTTGVISPERRCRSMDVDLNQAHMEDTPKKKGTNVFGSLERGLDKVLTALTRNKKKGSARDGPRKRKLHYNVTTTRLVNPDQLLSEIMAILPKKNVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQRPDVVGIRRQRLKGDAWVYKRLVEDILSGCKM
Protein: Disintegrin and metalloproteinase domain-containing protein 7 (ADAM 7) (O35227)
Organism: Mus musculus (Mouse)
Function: May play an important role in male reproduction including sperm maturation and gonadotrope function. This is a non catalytic metalloprotease-like protein.
Subcellular location: Membrane {ECO:0000305|PubMed:20945367}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Epididymal-specific lipocalin-9
- Epididymal-specific lipocalin-8
- Epididymal secretory glutathione peroxidase
Sequence:
MLTTGIFWMTVLISHIQERGIVGVEGQELVHPKKLPLLHKRDLERIHDSDIPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGEHLVYKYNVKAPYATNHSCVGLNFTKKSALIDVENIEEHNAEDHHKEKFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGFPCTCPLGKCVMGDGSIPAIKFSKCSQTQYQQFLQDQKPACILNNPFPEEFNDYPFCGNKKVDEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKDEFQANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCYRMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGRPSSRLGEDKAYNLKNVKQNVTIKCRTMFLHHNSRDMGLVNSGTKCGDGMVCSNGECIEMEKAYNSTICSSPCDENDVDDNEPECQCEEGSIITEWGEALNLTSVSIMVIVLVMVIIGVGLVILLIRYQKCIKMKQVQSSPREIRGVENKGYFPEEHQTRSEPILTDIHPLHTTAESLERVPSSFSSPHYITLKSVSKDSRGIADPKQTDNVNLNLDTQSGCERLG
Protein: Linalool synthase Tps-5073L4, chloroplastic (PfTps-5073L) (EC 4.2.3.-) (C0KWV5)
Organism: Perilla frutescens (Beefsteak mint) (Perilla ocymoides)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSMRIYVAIMKKPSVKHVDYVDKKASKPSWRVSSSATAGLRASSSLQLDVKKPADEILTARRSGNYQPSLWDFNYLQSLNTTHYKEERHLKREAELIEQVKMLLDEEMGAVQKLDLVDDLKNLGLSYFFEDQIKQILTFIYNEHECFRSNVEAKERDLYFTALGFRLLRQHGFQVSQEVFDCFKNEEGSDFKASLGDDTKGLVQLYEASFLLREGEDTLELARQYATKFLQKKVDHELIDDDSNLLSWIRHSLEIPLHWRIQRLEARWFLDAYATRHDVNPIILELAKLDFNIIQATQQEELKDLSRWWNSTCLVEKLPFVRDRLVESYFWAIALFEPHQYGYHRKIAAKIITLITSLDDVYDIYGTLDELQLFTDAIQRWDTESISRLAYYMQLFYMVLYNFVSELAYDGLKEKGFITIPYLQRSWADLVEAYLKEAKWFYNGYTPSMEEYLNNAYISIGATPVISQVFFTLATSIDKPVIESLYEYHRILRLSGMLVRLPDDLGTSPFEMKRGDVPKTIELYMKERNATEIEAQEHVRFLIREAWREMNTATAAADCPFTDDLVAAAANLGRAAQFMYLDGDGNHSQLHQRIASLLFEPYA