wanglab/gogpt-training-data huggingface dataset:
Protein: Myristoylated alanine-rich C-kinase substrate (MARCKS) (P26645)
Organism: Mus musculus (Mouse)
Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30185885}; Lipid-anchor {ECO:0000269|PubMed:30185885}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P29966}. Cytoplasm {ECO:0000269|PubMed:30185885, ECO:0000269|PubMed:30655546}. Note=PKC-dependent phosphorylation displaces MARCKS from the cell membrane and subsequent dephosphorylation is accompanied by its reassociation with the membrane. {ECO:0000250|UniProtKB:P29966}.
Interaction partners:
- Calmodulin-1
- Calmodulin-4
- Calmodulin 5
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Protein kinase C delta type
- MARCKS-related protein
- Protein kinase C epsilon type
- Protein kinase C alpha type
- Brain acid soluble protein 1
Sequence:
MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE
Protein: Tenascin-N (TN-N) (Tenascin-W) (TN-W) (Q9UQP3)
Organism: Homo sapiens (Human)
Function: Extracellular matrix protein that seems to be a ligand for ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity). Involved in neurite outgrowth and cell migration in hippocampal explants (By similarity). During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (By similarity). In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19884327}.
Interaction partners:
- Integrin alpha-9
- Syndecan-4
- Integrin alpha-8
- Integrin beta-6
- Integrin alpha-V
- Integrin beta-3
- Integrin beta-1
- Syndecan-1
Sequence:
MSLQEMFRFPMGLLLGSVLLVASAPATLEPPGCSNKEQQVTVSHTYKIDVPKSALVQVDADPQPLSDDGASLLALGEAREEQNIIFRHNIRLQTPQKDCELAGSVQDLLARVKKLEEEMVEMKEQCSAQRCCQGVTDLSRHCSGHGTFSLETCSCHCEEGREGPACERLACPGACSGHGRCVDGRCLCHEPYVGADCGYPACPENCSGHGECVRGVCQCHEDFMSEDCSEKRCPGDCSGHGFCDTGECYCEEGFTGLDCAQVVTPQGLQLLKNTEDSLLVSWEPSSQVDHYLLSYYPLGKELSGKQIQVPKEQHSYEILGLLPGTKYIVTLRNVKNEVSSSPQHLLATTDLAVLGTAWVTDETENSLDVEWENPSTEVDYYKLRYGPMTGQEVAEVTVPKSSDPKSRYDITGLHPGTEYKITVVPMRGELEGKPILLNGRTEIDSPTNVVTDRVTEDTATVSWDPVQAVIDKYVVRYTSADGDTKEMAVHKDESSTVLTGLKPGEAYKVYVWAERGNQGSKKADTNALTEIDSPANLVTDRVTENTATISWDPVQATIDKYVVRYTSADDQETREVLVGKEQSSTVLTGLRPGVEYTVHVWAQKGDRESKKADTNAPTDIDSPKNLVTDRVTENMATVSWDPVQAAIDKYVVRYTSAGGETREVPVGKEQSSTVLTGLRPGMEYMVHVWAQKGDQESKKADTKAQTDIDSPQNLVTDRVTENMATVSWDPVRATIDRYVVRYTSAKDGETREVPVGKEQSSTVLTGLRPGVEYTVHVWAQKGAQESKKADTKAQTDIDSPQNLVTDWVTENTATVSWDPVQATIDRYVVHYTSANGETREVPVGKEQSSTVLTGLRPGMEYTVHVWAQKGNQESKKADTKAQTEIDGPKNLVTDWVTENMATVSWDPVQATIDKYMVRYTSADGETREVPVGKEHSSTVLTGLRPGMEYMVHVWAQKGAQESKKADTKAQTELDPPRNLRPSAVTQSGGILTWTPPSAQIHGYILTYQFPDGTVKEMQLGREDQRFALQGLEQGATYPVSLVAFKGGRRSRNVSTTLSTVGARFPHPSDCSQVQQNSNAASGLYTIYLHGDASRPLQVYCDMETDGGGWIVFQRRNTGQLDFFKRWRSYVEGFGDPMKEFWLGLDKLHNLTTGTPARYEVRVDLQTANESAYAIYDFFQVASSKERYKLTVGKYRGTAGDALTYHNGWKFTTFDRDNDIALSNCALTHHGGWWYKNCHLANPNGRYGETKHSEGVNWEPWKGHEFSIPYVELKIRPHGYSREPVLGRKKRTLRGRLRTF
Protein: Dihydropyrimidinase (DHP) (DHPase) (EC 3.5.2.2) (Dihydropyrimidine amidohydrolase) (Hydantoinase) (Q9EQF5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate (By similarity).
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Beta-ureidopropionase
- Uridine 5'-monophosphate synthase
- Dihydroorotate dehydrogenase
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MAPQGRLLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEDASRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLARDKGVNSFKMFMAYKGLYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWSEEWSHAAHHVMGPPLRPDPLTPGFLMDLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHGKFIPRQPFAEYIYKRIKQRDQTCTPVPVKRAPYKGEVTTLKARETKEDDTAGTRMQGHS
Protein: LD19356p (Q7K107)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PSLRLHSACTQIGLVVQSKSNAIQCSSAIVECLNKPIGAQHTVTMGNKSSLFLRNEEIAQIQEETGFTPNQIERLYSRFTSLDRNDCGTLSREDLMRIPELAINPLCERIVHSFFAESNDDRVNFRQFMNVLAHFRPLRDNKQSKLNSREEKLKFAFKMYDLDDDGVISRDELLSILHMMVGANISQDQLVSIAERTILEADLCCQGKISFEDFCKALDRTDVDQKMSIRFLN
Protein: RNA helicase (EC 3.6.4.13) (Q38B75)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PRP8 protein homologue
- Pre-mRNA-splicing factor SYF1
- Spliceosome-associated protein, putative
- Cell division control protein, putative
- Pre-mRNA splicing factor, putative
- Splicing factor 3B subunit 1, putative
- Uncharacterized protein
- PHD finger-like domain-containing protein 5A
- U5 small nuclear ribonucleoprotein component, putative
- MI domain-containing protein
Sequence:
MDREAMRRAQQTSRDAYLRKRAAMREKAASVVLQEKITEIEAGVLPSSFTEIELLSKRAQEVKAAERLQVAANMRQEIITLDGGPALGEKRHRDVVVPPLIQEEMIVQEDTQRHAEASHGFVAMDKAIIDDRIEKHDYTEEVTEEEIKRERTAALQNQNRRLQEQRRSLPIYQSRGALLELIRNNPVVIIVGETGSGKTTQLLQYLYEENLHEPAPPTSANAEGVTSEPVGEVTQGKRLICTQPRRLAAISVAERVAQEMNTRCGSIVGYKVRFDDRTGPLTRVLFVTDGMMLKEVVGDPSLNTVAAIMVDEAHERSLNTDILLGLLKDIIRGNKQLRVIVASATINADKFSDFFNRAPIFTVKGRSFPVDTSYITEPVADYVKASVDCILMLHATKPLPGDILVFLPGQEEIESCAAAVREALVETAGQLRPLLVLPVYSSLPPREQKRIYEVPPPNTRKVVIATNIAETSITIDGIVYVVDCGLCKQNYYNHRAMIEELRVLPISQASATQRAGRAGRTREGDCYRLYTTYTFHNEFPSETVPEILRSSMSSVVLQLKALGINNLLQFEFIDAPSTASLERALDHLYLLGAMKQDGRLTLTGRRMAEFPLDPSLSKSVIRASAMGCLRHMAIAVAMLSLDSIFINTRDPKERIAMTSARDKMFSSGNGDVVGYVRLMEEWLRSGSLKQEFCDTNYVNSKSLLRARDILDQILKTCERLGFDLPNGQEADALSVEALTKALLSGFFMNVSVLGLDKRTYSIVRPIDPTVSRLGAASQVGSGNRFGDAESAVELHPSSYLFRTGTSTHGERSKGLPPTPSMVAMEERPRLVVFTQLRCTKKRYMMHVTAVPSADWVLAVAPVNYFTKEELEVETHKRKHV
Protein: Lysophospholipase (EC 3.1.1.5) (A0A1D8PEB1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- PNPLA domain-containing protein
- Lysophospholipid acyltransferase
- Glycerophosphocholine phosphodiesterase GDE1
Sequence:
MKVNLKLIIGSILISQAQAIWPFDSSGSSSSSDSSPSETGSSGGTFPFDLFGSGSSLTQSSSAQASSTKSTSDSASSTDSSLFSSSNSGSSWYQTFLDGDSGDQKTDYAPFNLTCPSKKTFIRTASELSQQEKDYIHKRQETTNKNLIDFLSKRANLSDFDAKSFINDNAPNHNITIGLSFSGGGYRAMLAGAGQILGLDGRYEDANKHGLGGLLDSSTYVVGLSGGNWLVGSLALNDWLSVGDIVNGKSTIWQLQDSILNPSGMRIDKTIAYYYGLAQAVQAKEDAGFQTSVTDTWGRALSYQFFEEDDSGTGGANITWSSIRNLSSFQDHSMPYPIVVANGRTPGTYIINENSTIFEISPYELGSWDPSLKSFSDIQYLGSSVNNGNPNNTDICVNNFDNAGFIMGTSSSLFNQILLQLDNYSINSIIKMILEKVLTDVSDEEYDIAVYEPNPFFGADSAGIKSITTNDTLYLCDGGEDLQNVPFYPLIQNERGVDVIFAFDNSADTNSSWPNGTSIQETYKRQFSKQGKGTPFPFAPDYKTFLDKNMGDKPVFFGCNSSDLEDLVAWHENDKINVTDVPLVVYTSNTRMSYNSNFSTFKLSYSDQEKFGAIRNGFETVTRNNLTDDENWSTCVGCAIIRRQQERLGEEQSDECKKCFQEYCWTGGFKDAASVSSVSGISGLAAKTHTSGGTSSTTQQTSTTTGSSSNGGSSSTGSSSSSKKKNGGDLVNGGVPSSIFLVFNSLLGLIIAYL
Protein: Repressible alkaline phosphatase (EC 3.1.3.1) (Fructose-2,6-bisphosphate 6-phosphatase) (EC 3.1.3.54) (Membrane-bound repressible alkaline phosphatase) [Cleaved into: Soluble alkaline phosphatase (EC 3.1.7.6) (Farnesyl diphosphatase)] (P11491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase.
Subcellular location: [Repressible alkaline phosphatase]: Vacuole membrane; Single-pass membrane protein. Note=The full-length version is found in lysosome-like vacuoles.; SUBCELLULAR LOCATION: [Soluble alkaline phosphatase]: Cytoplasm. Note=The truncated version of the protein is soluble.
Interaction partners:
- Acid phosphatase PHO11
- Repressible acid phosphatase
- Acid phosphatase PHO12
- Thiamine biosynthetic bifunctional enzyme
- Folic acid synthesis protein FOL1
- Low molecular weight phosphotyrosine protein phosphatase
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Constitutive acid phosphatase
- GTP cyclohydrolase 1
Sequence:
MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGFFLMVEGSRIDHAGHQNDPASQVREVLAFDEAFQYVLEFAENSDTETVLVSTSDHETGGLVTSRQVTASYPQYVWYPQVLANATHSGEFLKRKLVDFVHEHKGASSKIENFIKHEILEKDLGIYDYTDSDLETLIHLDDNANAIQDKLNDMVSFRAQIGWTTHGHSAVDVNIYAYANKKATWSYVLNNLQGNHENTEVGQFLENFLELNLNEVTDLIRDTKHTSDFDATEIASEVQHYDEYYHELTN
Protein: Putative ATP-dependent RNA helicase, DEAD boxfamily protein (Q1ZR46)
Organism: Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Interaction partners:
Sequence:
MSFQSLNLHPNLLKALTELGYSTPTDVQQQAIPLALKGDDVMAGAQTGTGKTAAFALPLLQRLMTLPSQAEQVSTAIENNHKSRNNIRALILTPTRELAQQVYDSITTYAKYTEIKVAVAYGGTSMNVQVKALNAGAEILVATPGRLLDHVFNGSVSLSEVETFVLDEADRMLDMGFIVDIQRIMKRMPAERQTLFFSATFSKQVKKLAFDILTNPKMVEVTPANTAAETVEQMVYPVDKHRKAELLAYLIGSRNWRQVLVFTKTKQGSDQLAKDLGLDGIKASSINGDKSQGARQRALDDFKSGKTRVLVATDVAARGLDIEQLEYVVNFDMPFKAEDYVHRIGRTGRAGMTGHAITLMSLDEEWALKAIEELLDSRLPQQWLEGYEPDPALIETQSVHRGAAAEKRRAKSKSKIHQNRGKHRNRR
Protein: Anaphase-promoting complex subunit 2 (20S cyclosome/APC complex protein apc2) (Q874R3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome.
Interaction partners:
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 13
Sequence:
MNDTDLSTFTGRSLLIDQLSSVTQGTPVLDFIDKLRIHFYTTIRQNLLKIDLKNICSLHDLTDQLSDFWLVYEQSVLESPILSPELDRILTCFRCLCRRYLPISVIESVLTEYLDQVLKVWLESKTNPCLDMEKFFQLCEKFKQLGLSSVLKERFVYVLQLHVGSLLTTRYAMSWEQSVYHEALEWIRTEFGVLVEHVFSLSNPAVLVQLDHLVSQILAHLRSDNILDIVLHYPNSLGAIEDLRLVARQKQQRQYLTETFVKDCTSSILTASSDSSYILLFYVSTIRCFVALDPPGVLLDKAAKPIRSFLNEREDAYKCLVSLLFVDGEKGLRSELSQIPTENIDSTTDRFDNYHWMPDPIDAAPDFKKPTDRDVVGSLISIFKSKEPLVKELQLLLADRLLQLTDYHYEVEAKNIEFLKYRFGETVLQMCSVMLNDIENSRFIDQSIHMENYVSKGLHVTILSRLFWPTLSVRYFHLPGPLKKELDAYAEEYRERKRKRELVFLPNLGSVELEIELEDRTLTLTVTPEQAAFISLFEETSTLHIEKAAELLDQPKEIVERHLKFWLHHRVLTDIGDDRYRVRETEAETATETVLDEIQGVSAVQSEAESSAAEMRVYWSFVVGMLTNLGALELERIHNMLTMFIPPPNGYTRTQSELREFLALMIKEEKLEFTGGAYKLK
Protein: VPS37 C-terminal domain-containing protein (O44158)
Organism: Caenorhabditis elegans
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004633}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004633}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog
- Tumor susceptibility gene 101 protein
- Multivesicular body subunit 12A
- Vacuolar protein-sorting-associated protein 36
- Charged multivesicular body protein 3
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Charged multivesicular body protein 6
- Vacuolar-sorting protein SNF8
- Vacuolar protein-sorting-associated protein 25
- Signal transducing adapter molecule 1
Sequence:
MFSQNPYESHVDVAVSAASANLRNMTNEQLISLLDDDALLESIIVNLPQVRSMPTDKESALAANKSLAEWNLAQKPRIDAAKTQTVDLYDQVKKLQGEVAVLKSQLDSVSSSKSLDTTSSLMQVAAQEADDDAEALFTQFENGEISVEIFLKQFKDKKTIAHLRKIKSDRLAALLREQTYSSYAQPTVPPPMPHAQPGYPTGNHMPGIGNIQFGSGYSGYPNISQPSAGRHPFF
Protein: Par-1, isoform H (EC 2.7.11.-, EC 2.7.11.26) (A1ZBL7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQTSSHRQMHHSSNNNNKEEPPQPASQFGNRRTSTRKSTSSSKHYPTLVQPLRKDELSLLRDSLLRNGSIMRKNPERRPVTISELKPVNTGQGTSGSVLPITAEDAAGGSSSSITQLMAFQLPVDRSAKTDDLAAESSASAAAAVAPKEGRNEFYIVGDGYHRTDHCYYRSPNGDFHKLPSDSFHKMSEGCFVRMADGVFRRLEVPTKAQISRRSSRAEEIGDATSQGNGSAATNVKSQLMRFLKRSKSHTPATIAKLQREKEEARAERKQRLSNALRQKNLAATNAASAAAANSSYASGGGGGTVSSRNNKIVVTMIENGGLPIVATSKAERPKAKESASSSDKARNSRGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGAETLRVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETNSGSAAPAGKGHTKSASVSSPRPSTDGCVSVSNDPLGTRMASAVKSSRHFPRNVPSRSTFHSGQTRARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPNQ
Protein: DNA polymerase subunit gamma-2, mitochondrial (DNA polymerase beta subunit) (DNA polymerase gamma 35kD subunit) (DNA polymerase gamma subunit 2) (Q9VJV8)
Organism: Drosophila melanogaster (Fruit fly)
Function: As accessory component of the DNA polymerase gamma complex is involved in the replication of mitochondrial DNA. Does not bind DNA. Essential for mitochondrial DNA maintenance and larval development.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9153213}.
Interaction partners:
- DNA polymerase subunit gamma-1, mitochondrial
- Glutamyl-tRNA
- DNA polymerase alpha catalytic subunit
- DNA primase large subunit
- DNA polymerase alpha subunit B
- DNA polymerase delta subunit 2
- DNA primase small subunit
- DNA polymerase delta subunit 3
- DNA polymerase delta catalytic subunit
- Single-stranded DNA-binding protein, mitochondrial
Sequence:
MSRIQRCFKSLASAGFFRTVEDNKLELLSHGREYAKLLQQHWTRLRPLAAHLGATKEPINPVNIQRFSFPQSQQFRNNFQKLVKDHPRKAKCPTLLKHQSTCSGPTSNSLFGIKGPTLHLTTDFLVEPHRALEHFYNMQRESKIWWMRLSSNPSRYRIVPCDLAEDLNPNDYQAIDIRTSYGDAGEVTVEQLSLVRIVDDKDFRLPDARTGEIVQPTVIRSVIELETTTCALLLDGCDHGRDSQSLLLHRVLAPYQCGIACVESDSELSADLSDLCQHLKHVLNHAGLRLSEGDGIRTTKNASHLAEHLLETDMLGIPYTLVINEQTLRNGLMQLRSRDTRLAETIHISDVPDYLLNIFKN
Protein: Cytosolic sulfotransferase 3 (EC 2.8.2.-) (SULT1 ST3) (Q7T2V2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a variety of xenobiotic and endogenous compounds, including dopamine, T3 (triiodo-L-thyronine), T4 (thyroxine), estrone, DHEA (dehydroepiandrosterone), flavonoids, isoflavonoids and other phenolic compounds.
Subcellular location: Cytoplasm.
Interaction partners:
- AP2-associated kinase 1a.
- ATP-dependent RNA helicase DDX51
- peptidylprolyl isomerase
- Tumor protein p63-regulated 1-like
- Lysophosphatidic acid receptor 2a
- Uncharacterized protein LOC550501 precursor
Sequence:
MEISDFSSMKLNSRPELIDFEGISMIHYFTDNWEKVKNFQARPDDILIATYPKAGTTWVSYILDLLYFGNESPERQTSQPIYMRVPFLEACFEGIPFGTELADNLPTSPRLIKTHLPVQLVPKSFWEQNSKVVYVARNAKDNAVSYFHFDRMNMGQPEPGDWNTFLQKFMEGRNVFGPWYDHVNGYWKKKQTYSNILYMFYEDMVENTGREVERLCSFLGLSTSAAERERITKGVQFDAMKQNKMTNYSTIPVMDFKISPFMRKGKVGDWRNHFTVAQNEQFDEVYKQKMKNTTVKFRTEL
Protein: RNA binding protein, putative (Q384T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCTYVNIHVCYILTFLYFDFLLGQQCVPMPSRAVLRKKARRESKRRKDETEGKTTAFKLQAMEQLGKSHKADATKHVASDRKVQCNKRPRGETVKEKDTDVCEVLEGASRKERKRFEAKRRFERQLGALNRSLAAVTSNTDGTSRDAAPSAEEAHQRHDPKYKNGTFWRDRKERRRRTVFLGNVPAKLTEQDVTSLISDTLRKGWTPPEEDGIADVDVVIEEEVVESVDFIKSMPRAKRRHMYVTMCSIKAAESATKLLDGKMMEGIALRCNFAADKVQRGEAIQRRSASGSEH
Protein: Mitochondrial intermediate peptidase (MIP) (EC 3.4.24.59) (P35999)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:8831696}.
Interaction partners:
- Intermediate cleaving peptidase 55
- Mitochondrial-processing peptidase subunit alpha
- Presequence protease, mitochondrial
- Probable alcohol acetyltransferase
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- Frataxin homolog, mitochondrial
- Import motor subunit, mitochondrial
- Rhomboid protein 1, mitochondrial
- Mitochondrial inner membrane protease ATP23
Sequence:
MLRTIILKAGSNASIPSPSRQNKLLRFFATAGAVSRTSPGSIKKIFDDNSYWRNINGQDANNSKISQYLFKKNKTGLFKNPYLTSPDGLRKFSQVSLQQAQELLDKMRNDFSESGKLTYIMNLDRLSDTLCRVIDLCEFIRSTHPDDAFVRAAQDCHEQMFEFMNVLNTDVSLCNILKSVLNNPEVSSKLSAEELKVGKILLDDFEKSGIYMNPDVREKFIQLSQEISLVGQEFINHTDYPGSNSVKIPCKDLDNSKVSTFLLKQLNKDVKGQNYKVPTFGYAAYALLKSCENEMVRKKLWTALHSCSDKQVKRLSHLIKLRAILANLMHKTSYAEYQLEGKMAKNPKDVQDFILTLMNNTIEKTANELKFIAELKAKDLKKPLTTNTDEILKLVRPWDRDYYTGKYFQLNPSNSPNAKEISYYFTLGNVIQGLSDLFQQIYGIRLEPAITDEGETWSPDVRRLNVISEEEGIIGIIYCDLFERNGKTSNPAHFTVCCSRQIYPSETDFSTIQVGENPDGTYFQLPVISLVCNFSPILIASKKSLCFLQLSEVETLFHEMGHAMHSMLGRTHMQNISGTRCATDFVELPSILMEHFAKDIRILTKIGKHYGTGETIQADMLQRFMKSTNFLQNCETYSQAKMAMLDQSFHDEKIISDIDNFDVVENYQALERRLKVLVDDQSNWCGRFGHLFGYGATYYSYLFDRTIASKIWYALFEDDPYSRKNGDKFKKHLLKWGGLKDPWKCIADVLECPMLEKGGSDAMEFIAQSHKS
Protein: Mitochondrial SSU ribosomal protein (Q386Q7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial SSU ribosomal protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
Sequence:
MRRCSFASTCRYRSADDVPLGLGSAYVWTCRNITSRGQFNPIHNFSYAMERGVRARDVKAFEKLITNPGPLRVAYTPDYLDWLHRCYKAKGTYMDARAVAEKKFNGNIVSSELSAAVNRREGKRGDTRGDTVDNDHHNLPGAPPPGMFLRPAHSFRRLAGELKRRRAQSILDEVARAQGMLDLFERQPHFPAIHIDRCSRFHLVELFKEMVLERSLDSNMIWEKALLYRAILSERKPSYPTSFHYIFTAVEDTVFAPTISTPMEMAGSGGEGHDRSSHPLAAKCPTLEAYYYYVYLVKKYYIDNAVEAHVVLRCHREPNAADLLFSNPPPKDDTEIMKAVELLRNADIQRGVAAAAAVSDPTLPPGGEGSVIGNSDNKKNSEKTSEGSRGRPARPPVLPGAYPPIDMLWRCEENLPLLKVLLFGEFNLIVSENPFVKFPSAHGFLTRPYSTDSSRTLADGMSLANVMAEKRGHLLPSLPRNTATSIDARAQDIRRLQQKHHRDDIVSFQKLLRSTHAEDSPSAFSSYSDWSYFNPRAVRAEERDRLTRKAVEALKLYDSATNDIYRHSFEDVQACHTQRVTERDRTMPPYLPTLPHFVAIIKKDPHISFLLHIGLPDRNSSEEGSAKHKELEKRIYYLARALYHTALEYHNETVRRVNRQKVNVAASLLDNFVEQEWTTILRDKHDVTDVTKTLNDTQNDKKQLARRLGRYMLFANRSLDDTGFPTDARADDYTRWMAPPSVGKVSL
Protein: Pbx4 homeodomain protein (Pbx4/Lazarus homeodomain protein) (Pre-B-cell leukemia transcription factor 4) (Q9PW77)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-B1b
- Homeobox protein Hox-B1a
- Homeobox protein Hox-A1a
- Homeobox protein Hox-B7a
- Homeobox protein Hox-B2a
- Homeobox protein Hox-C9a
Sequence:
MDDQTRMLASMGGLGGLSQADVGDPDSVRKQQSLGQPQQDIGDILQQIMAITDESLDEAQARKHALNCHRLKPALFSVLCEIKEKTVLSIRGVQEEDPPDPQIMRLDNMLLAEGVSGPEKGGGSAAAAAAAAAAGGSPNDGSIEHSDYRAKLAQIRQIYHSELEKYEQACSEFTNHVMNLLREQSRTRPISPKEIERMVAIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEVLNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAVKTAVDAANVSAQASQANSPATPNSGGYPAPCYTPDGRL
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha1 (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) (Platelet-activating factor acetylhydrolase alpha 1 subunit) (PAF-AH alpha 1) (O35263)
Organism: Rattus norvegicus (Rat)
Function: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit alpha
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophosphatidylcholine acyltransferase 1
- Lysophosphatidylcholine acyltransferase 2
- Platelet-activating factor acetylhydrolase.
- Lysophosphatidylcholine acyltransferase 2B
- Cholinephosphotransferase 1
- Lysophosphatidylcholine acyltransferase 4
- Choline/ethanolaminephosphotransferase 1
Sequence:
MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAP
Protein: Carbonic anhydrase 14 (F7F6N9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGFLDLNSTSQSTRGLPFLLEAGHHWTYEGPHGQDHWPASYPECGGNAQSPIDIQTDGVIFDPDLPTVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQKGTLKGSEHQINSEATAAELHVVHYDSESYGSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSHLHEVRYKDQKTSVPPFNVRELLPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQVGPLYTTGEMLGLGMGISAGCLCLLLTIYFIAQKIRRKRLGNRKSVVFTSARATTEA