wanglab/gogpt-training-data huggingface dataset:
Protein: Putative inactive polypeptide N-acetylgalactosaminyltransferase 12 (pp-GaNTase 12) (Inactive UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12) (Inactive protein-UDP acetylgalactosaminyltransferase 12) (Q8IA44)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable inactive glycosyltransferase.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEVFASVLNCCFKYIVLPVWIFIVLLLLHRDLSSWDGLMGPLSHPGLGENGSASYLSVPSWEIDEYTQGWRYYLYNSWLAERIPLRRSLPDLRDHRCQKLEYDEDSDEMKPASIIMIFRNEQLVVLLRTLHSLVERTPKYLYIELILVNDHSDTDFWNDKLSLIFFDNYVHRYIHPKARILHLPEQVGLIKARNLAASEAKAENLVFVDAQVEFTNGWLSPLLDTIAEQSYTLATPILDNLDEQTLAYQRSIERRGMYDWSLTRREVPLSRARRSHLPWPYEVAAVRTSVFAIPAVWFQDISNFDNNLRGFGAAELELSFKVWCTGGRIVQVPCSRVGHLQPKDEDYLKRYGDLHKMGEQKSRNLKRIIEVWTGDLKSAIYKYQPHLLNISEGDLNEPRKLYKQNECQSFKEFINDITPGLNHVAALNRTDYASGHVKTLEFPKKCLTINAKSQNLFLERCSTNNTLQNWTLTYVKDLRVAGNICAEVRPNLRLGYSFCHSLGGRQSWHYDSVSNQLMSNTKCLEFTDELNIFLAICDAANGKQRWILDNINLSVMQSANILV
Protein: Twist-related protein 1 (Q9PVG4)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Snail family transcriptional repressor 1
- Uncharacterized protein.
- Zinc finger E-box-binding homeobox 1
- Zinc finger E-box-binding homeobox 2
- Cadherin-1
- Cadherin-2
- Transcription factor SOX-9
- Paired mesoderm homeobox protein 1
Sequence:
MMQQDESNSPVSPADDSLSNSEEEPDRQQLPSAKRGGRKRRSSRRSAGGAVGAADEPCSPAQGKRGKKCGAGAGGGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH
Protein: DUF833-domain-containing protein (A0A1D8PSD7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MCIAIATTNHPEYPFILLSNRDEFFKRPTMPAHFRDVGNGVKLLSPLDLARQEHGTWIGVTTNGKIAVLVNYRENDQREAISEVSRGILPLDYLCGKESDNEWKDNLAATFRDGRNTIDLKKIGGFSLLYGKLSINPQTGKIHHLNILSNRGDQGKVFKSKETSKDNANGEINLSNDTSDTEDDDIPHKTTFGLSNSLYNKPWDKVKLGESLLSKLIDESIINNYSQDQLIEKCFQLLSHDTYNSKILYSDDFEKKFAELKYSIFIPPIVRNNYYETDSVAVGKYYGTRTQTIILLDKYGNLNYYEKNIHNSDDIDLKDVDITSHYKFNIFNDQKNGC
Protein: Melanocortin-2 receptor accessory protein (B27) (Fat cell-specific low molecular weight protein) (Fat tissue-specific low MW protein) (Q8TCY5)
Organism: Homo sapiens (Human)
Function: Modulator of melanocortin receptors (MC1R, MC2R, MC3R, MC4R and MC5R). Acts by increasing ligand-sensitivity of melanocortin receptors and enhancing generation of cAMP by the receptors. Required both for MC2R trafficking to the cell surface of adrenal cells and for signaling in response to corticotropin (ACTH). May be involved in the intracellular trafficking pathways in adipocyte cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15654338}; Single-pass membrane protein {ECO:0000269|PubMed:15654338}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15654338}; Single-pass membrane protein {ECO:0000269|PubMed:15654338}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context (PubMed:20371771). Upon insulin stimulation, it is redistributed into spotty structures throughout the cytoplasm. {ECO:0000269|PubMed:20371771}.
Interaction partners:
- Adrenocorticotropic hormone receptor
- Pro-opiomelanocortin
- FYVE, RhoGEF and PH domain-containing protein 3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Melanocortin receptor 4
Sequence:
MANGTNASAPYYSYEYYLDYLDLIPVDEKKLKAHKHSIVIAFWVSLAAFVVLLFLILLYMSWSASPQMRNSPKHHQTCPWSHGLNLHLCIQKCLPCHREPLATSQAQASSVEPGSRTGPDQPLRQESSSTLPLGGFQTHPTLLWELTLNGGPLVRSKPSEPPPGDRTSQLQS
Protein: Histone-lysine N-methyltransferase MEDEA (EC 2.1.1.356) (Maternal embryogenesis control protein) (Protein EMBRYO DEFECTIVE 173) (Protein FERTILIZATION-INDEPENDENT SEED 1) (Protein SET DOMAIN GROUP 5) (O65312)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. Required to prevent the proliferation of the central cell of the female gametophyte by repressing target genes before fertilization. After fertilization, it probably also regulates the embryo and endosperm proliferation and anteroposterior organization during seed development. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Interacts with the promoter and repress the transcription of genes such as PHE1 and PHE2, that are paternally active and maternally silenced genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11114524}. Note=Excluded from the nucleolus.
Interaction partners:
- Polycomb group protein FERTILIZATION-INDEPENDENT SEED 2
- Histone-binding protein MSI1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- Polycomb group protein EMBRYONIC FLOWER 2
- Lysine-specific demethylase ELF6
- Polycomb group protein VERNALIZATION 2
- WD-40 repeat-containing protein MSI5
- WD-40 repeat-containing protein MSI4
- Putative E3 ubiquitin-protein ligase RING1a
- Histone H3.1
Sequence:
MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEADHVMDNDNSISNKIVVSDPNNTMWTPVEKDLYLKGIEIFGRNSCDVALNILRGLKTCLEIYNYMREQDQCTMSLDLNKTTQRHNQVTKKVSRKSSRSVRKKSRLRKYARYPPALKKTTSGEAKFYKHYTPCTCKSKCGQQCPCLTHENCCEKYCGCSKDCNNRFGGCNCAIGQCTNRQCPCFAANRECDPDLCRSCPLSCGDGTLGETPVQIQCKNMQFLLQTNKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLNDQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGPEHADWSRGREPRKTGASKRSKEARPAR
Protein: Kallikrein related-peptidase 6 (O54854)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Amyloid-beta precursor protein
- Opalin
Sequence:
MPTKMLTVKTLALCLILAKSAWSEDQDKVVHGGPCLKNSHPFQAALYTSGHLLCGGVLVGPQWVLTAAHCKKPNLEVYLGKHNLRQTETFQRQISVDRTIVHPRYNPQTHDNDIMMVHLKRPVKFSQRIQPLPLKKDCSEKNPDCQILGWGKMENGEFPDTIQCADVQLVSREECERAYPGKITRSMVCAGDKREGNDSCQGDSGGPLVCGGHLRGIVSWGDMPCGSKEKPGVYTDVCTHIRWIQNIIRNK
Protein: Urease subunit beta (EC 3.5.1.5) (Urea amidohydrolase subunit beta) (A0A0H3LDZ7)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01954}.
Interaction partners:
Sequence:
MIPGEIFYGSGDIEMNAAALSRLQMRIINAGDRPVQVGSHVHLPQANRALSFDRATAHGYRLDIPAATAVRFEPGIPQIVGLVPLGGRREVPGLTLNPPGRLDR
Protein: Probable tocopherol cyclase, chloroplastic (Vitamin E pathway gene 1 protein) (Q6K7V6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the synthesis of both tocopherols and tocotrienols (vitamin E), which presumably protect photosynthetic complexes from oxidative stress. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinone and 2,3-dimethyl-5-phytyl-1,4-hydroquinone (DMPQ) to delta- and gamma-tocopherol respectively. Converts also 2,3-dimethyl-5-geranylgeranyl-1,4-hydroquinone (DMGQ) to gamma-tocotrienol (By similarity).
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit D
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 3 subunit A
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Probable tocopherol O-methyltransferase, chloroplastic
- Probable homogentisate phytyltransferase 1, chloroplastic
Sequence:
MDLAAAAVAVSFPRPAPPPRRCAPRRHRRALAPRAASSSPSPSTAVAAPVYAPTPRDRALRTPHSGYHYDGTARPFFEGWYFKVSIPECRQSFCFMYSVENPLFRDGMSDLDRVIHGSRFTGVGAQILGADDKYICQFTEKSNNFWGSRHELMLGNTFIPNNGSTPPEGEVPPQEFSSRVLEGFQVTPIWHQGFIRDDGRSKYVPNVQTARWEYSTRPVYGWGDVTSKQKSTAGWLAAFPFFEPHWQICMAGGLSTGWIEWDGERFEFENAPSYSEKNWGAGFPRKWYWVQCNVFSGASGEVALTAAGGLRKIGLGETYESPSLIGIHYEGKFYEFVPWTGTVSWDIAPWGHWKLSGENKNHLVEIEATTKEPGTALRAPTMEAGLVPACKDTCYGDLRLQMWEKRNDGGKGKMILDATSNMAALEVGGGPWFNGWKGTTVSNEIVNNVVGTQVDVESLFPIPFLKPPGL
Protein: Ubiquitin-like domain-containing protein (Q389D0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSATSPRNIYAPLKVEFDSEVEITIHSAFLQTARLLQCDPMAHVSVSTLHVATDTRRPCGGVTQVGESTRIVKNERPVGSTRRLHFTSKPNFSEIIRFVIPFTQCRRSTMRPESRLLLRKTAAAVSTDDNPDERFVDHQVLITITDAQEQGYGQAVCPFLLHVPSSSTEPQRIMLQPRNKHDKHDPVFKSDVALLAKHGVDDFGFVDISWRVSLIPHGGALITALQPSVSVPTFPIGLVLRATWLVAGNVHQPRTQYTTSVEFGGQDRFLFEGTKPLFLTIQSAAQLERAIVHCTFHDTTTRPQSYDVAVPLPVPPMASFAMERDVWWTTPVRTACGVDLGILLASIRLAQRPLDGSTPFCTVEGCREINNPIHQSQFAHVAKEWGRAPPNTPPGAYYPLFWESEQHIARVAERQWRHDCIVGARPSIEHVRHLLEVLAGRIAVDGGVNGVAAVYFNHAPTTTLQQHQVKQFLVTCAFHAKEMTVQDAARFCFFALRRDMEQAITKEDVVFILDHALIGKTIDMPEKEVSRRVDDIFGDGVYITFDDFMRYFINNYAMWYQFGVPITTGDEQAAQGSMDVAVELGPNAQGTAKEESGEEARGGAAVPVAPRGEEAGSSNSNPQDVGVWRRFIARVQHSNRAFSVTAHVNDSIAEVMVMVQNSTGIRASCQEWRMNGVLLDPKATVGSTKLGLSSRNDASPEVVIIERDESLRLVMLYKEKSVRWELRIQETEKVLRLRALVQQKTLIPLSRCVMRANGQRLQDRHPLQHYQLQNGDVVEVMQE
Protein: Phosphoglycerate mutase protein, putative (EC 5.4.2.-, EC 5.4.2.1) (Q57UA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Triosephosphate isomerase
- phosphopyruvate hydratase
- Phosphoglycerate kinase
- Adenylosuccinate synthetase
- Glucose-6-phosphate isomerase
- Pyruvate kinase
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MAEVHVCRHGQDEDNRDGLLNGRRDRPLTALGREQASEVALRLKNGGVSYDVILASPLQRAYETACAIGRALDLVVETDEELTERDFGILAGKPVADIRKYAGENVLQGDKVLYFLEVEGAETFDECFNRAARLLKRVDERFSGKRVLLVCHGDIGKMVQAVRKNITWRDALLLPYMSNTDIVEL
Protein: Pcsk6 protein (Q8R0Y1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
CTGRSPAQCLSCRRGFYHHQETNTCVTLCPAGLYADESQRLCLRCHPSCQKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEEMPGLPHKVCRRCEENCLSCEGSSRNCSRCKAGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG
Protein: Cytochrome P450 monooxygenase helB2 (EC 1.-.-.-) (Helvolic acid biosynthesis cluster protein B2) (Q4WR18)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Acyltransferase helD2
Sequence:
MALPIILCLAVILWTSWRLLDALFLSPLHRVPGPVLARLTPLRAIYARLPSRVIPAALADFHSYGDIYLSKPRTITISHPRDVRAILASSEFQKIDVYHGLNDPVMANIVTFSDPKLASRRRRQIGPYFNPSYLAKMEELILRCGCRAVADKWGRLIAQQGHGPQKSVKVNYRHDLQLATFDIMSALAFGRWLDSLKEEGESVAIVEWIMATAVYIGVRINFRLLMVFPFSRLVRRWTRAYAEFVQFSKHAVASRKELLAQGCQKPVDLLQAFIDAEDPDSKVKMTTVEVQAESVGMQLAGSETTAASLTWAVHLFTLYPEYYRIAVDEVRGQFGPNHLITYADCSRLVFLEAFVYEMLRYTPITSSFMPRVSFTKGTTLQGHYIPPGTEIAFNLIAMNNREDVWEEPERFLPDRFLKDPDLKRSVFAFSYGTRSCIGRHLAWMEMMTILANLLKDYDWSLPEDSLYGPHHVDEKGIPIRMPSKCHIVFAPTHPDRDCQLVISRPKT
Protein: Chaperonin containing TCP1 subunit 8 (H7C4C8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVL
Protein: PAS domain-containing protein tyrosine kinase family protein (F4K645)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKTTPPAEELLKKIRELEESQEHLKREMSRLKVSAEMKQRSHSASPQRPVRRNSNDGTPMWRKTGAASFRHASPLRKESHAKVAGGGGEGQSAGKFTDKQYLNILQSMAQAVHVFDLNGQIIFWNSMAEKLYGFSASEALGKDPIDILVDVQDASVAQNITRRCSSGESWTGEFPVKNKAGERFSVVTTMSPSYDDDGCLIGIICITNDSALFQDPRGSPAKTRRGQEGETSFSRVTSSVASKLGLDSKEAVVSKLGLDSQQPIQVAIASKISDLVGNKVKSKMRAGDNNAANLEGGSGDSHQSDQGFFDAAFADRREDAATSGADTPRGDFIQSPFGVFLRSDEKASTKPFRDSSDESDGNSVVPKTLTSKAEEWMVKKGLSWPWKGNEREGLEGRRSHSVWPWVRNEQQKQQAYQSNSNHSVKSESQACESIKASSNEPMGYWSSSVNVNSTSSSSSCGSTSSSVMNKVDMDSDCLDYEILWEDLTIGEQIGQGSCGTVYHGLWFGSDVAVKVFSKQEYSEEIITSFRQEVSLMKRLRHPNVLLFMGAVTSPQRLCIVTEFLPRFGLITLANITLPFVLFELRGQNSDLPYQITFAVEVSSVCCRGTRQNWIGGDVSIWPRIFYLAYYSLDSLIQLLYLVYNMLHIFLTYFFAQARGMNYLHHCTPPIIHRDLKSSNLLVDKNWTVKVADFGLSRIKHETYLTTKTGRGTPQWMAPEVLRNEAADEKSDVYSFGVILWELVTEKIPWESLNAMQVIGAVGFMNQRLEVPKNVDPQWISLMESCWHSEPQDRPSFQEIMEKLRELQRKYTIQFQAARAASIENSALKEK
Protein: protein disulfide-isomerase (EC 5.3.4.1) (H7BZ94)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTGDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Protein: MAP kinase-activating death domain protein (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (RabGEP) (O08873)
Organism: Rattus norvegicus (Rat)
Function: Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family. Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (By similarity). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion. Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (By similarity). May link TNFRSF1A with MAP kinase activation (By similarity). May be involved in the regulation of TNFA-induced apoptosis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}. Cell projection, axon {ECO:0000250|UniProtKB:Q80U28}.
Interaction partners:
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 1A
Sequence:
MVQKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHPEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRMPKEKAEGGAGPRGKEGAHAPCASEEAATESSESGSTLQPPSADSTPDVNQSPRGKRRAKAGNRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKPGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQQALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCMASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPESLELKKHLKQALASMSLNTQPILNLEKFHEGQETPLLLGRFSNDLQSTPSTEFNPLIYGNDVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAEKLARTQAVEYFGEWILNPSNYAFQRIHNNTFDPALIGDKPKWYAHQLQPIHYRVYDSNSQLAEALSVPPERDSESDPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPLTHAALGDASEVEIDELQPQKEGEEPGPDSENSQENLPLRSSSSTTASSSPSTIVHGAHSEPADSTEVGDKAATGISKPLPPVPPSICKSTVDRRQTETGEGSVCQRTYDHPYFEPQYGSPAEEDDDEQGESYTPRFSQHASGSRAQKLLRPNSLKLASDSDAESDSRASSPNSTVSNNSTEGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKTTPFPSLKGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGWLNMKKVRRLLESEQLRVFVLSKLSRAVQSEDDARQDVIQDVEISRKVYKGMLDLLKCTVLSLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTENVNTPVGKDPGLAGRGDPKAMAQLRVPQLGPRAPSATGRGPKELDTRSLKEENFVASVGPEVIKPVFDLGETEEKKSQISADSGVSLASASQRTDQDSVIGVSPAVMIRSSSQDSEVSNSSGETLGADSDLSSNAGDGPGGEGSAHLASSRATLSDSEIETNSATSTIFGKAHSLKPKEKPASSPVRSSEDVSQRVYLYEGLLGRDKGSMWDQLEDAAMETFSISKERSTLWDQMQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLISYMLLMKVNKNDIRKKVRRLMGKSHVGLVYSQQINEVLDQLTNLNGRDLSIRSSGSRHMKKQTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRRNGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDMKTGEGGLLQVTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPPRPVSS
Protein: Iron-sulfur cluster repair protein ScdA (Cell wall-related protein ScdA) (P72360)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- nitric oxide dioxygenase
Sequence:
MINKNDIVADVVTDYPKAADIFRSVGIDFCCGGQVSIEAAALEKKNVDLNELLQRLNDVEQTNTPGSLNPKFLNVSSLIQYIQSAYHEPLREEFKNLTPYVTKLSKVHGPNHPYLVELKETYDTFKNGMLEHMQKEDDVDFPKLIKYEQGEVVDDINTVIDDLVSDHIATGELLVKMSELTSSYEPPIEACGTWRLVYQRLKALEVLTHEHVHLENHVLFKKVS
Protein: Ras-related protein RabG2 (Q54FL2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MSDPDVFKILLIGDSAVGKTSLLLRFADNSFQETSVNMTSVDYKNKNIVIDGRTFNLQIWDTAGQERFRTITSSFYRGAHGVLVCYDVTDQLTYNNVRLWMQEIQRYAVLGVSRVLVGNKCDLEDRKLVNTSIAREYADSLGIPFMEASAATGVNVEEAFMAMANEIYRNHMGGSKPSVVNPGSGGTSNTGGKKKFC
Protein: WIZ zinc finger (A0A2R8YFV2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISDGQPHPGLSEALPRVTSATHRISSCCWDGGSLDFRPGSPPPHLLGHFPGTPDGRGPWEHPLVQEAGEGILSERRFEDSVIVRTMKPHAELEGSRRFLHHRGEPRLLEKHAQGRPRFDWLQDEDEQGSPQDAGLHLDLPAQPPPLAPFRRVFVPVEDTPKTLDMAVVGGREDLEDLEGLAQPSEWGLPTSASEVATQTWTVNSEASVERLQPLLPPIRTGPYLCELLEEVAEGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPTALEQHRQLHQASREKIIEEIQKLKQVPGDEGREARLQCPKCVFGTNSSRAYVQHAKLHMREPPGQTTKEPFGGSSGAGSPSPEASALLYQPYGAAVGLSACVFCGFPAPSESLLREHVRLVHAHPHWEEDGEAYEEDPASQPGTSQDAHACFPDTAVDYFGKAEPSLAPMWRENPAGYDPSLAFGPGCQQLSIRDFPLSKPLLHGTGQRPLGRLAFPSTLASTPYSLQLGRNKSTVHPQGLGERRRPWSEEEEEEEEEEDVVLTSEMDFSPENGVFSPLATPSLIPQAALELKQAFREALQAVEATQGQQQQLRGMVPIVLVAKLGPQVMAAARVPPRLQPEELGLAGAHPLDFLLLDAPLGGPLGLDTLLDGDPAMALKHEERKCPYCPDRFHNGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTVSPINILQELLATSAAEQPPSPLGREPGGPPGSFLTSRRPRLPLTVPFPPTWAEDPGPAYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
Protein: Glutathione S-transferase P (EC 2.5.1.18) (GST class-pi) (GSTP1-1) (P09211)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19269317}. Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus {ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.
Interaction partners:
- Epoxide hydrolase 1
- Cytochrome P450 2E1
- Cytochrome P450 3A4)
- Mitogen-activated protein kinase 8
- Cytochrome P450 1A1
- Peroxiredoxin-6
- Cytochrome P450 1B1
- Cytochrome P450 1A2
- Glutathione reductase, mitochondrial
- Cytochrome P450 2C9
Sequence:
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
Protein: Cytochrome P450 2D3 (EC 1.14.14.1) (CYPIID3) (Cytochrome P450-DB3) (Debrisoquine 4-hydroxylase) (P12938)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- UDP-glucuronosyltransferase 1A1
- Cytochrome P450 7A1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B37
- Nuclear receptor subfamily 1 group I member 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Steroid 17-alpha-hydroxylase/17,20 lyase
- UDP-glucuronosyltransferase
Sequence:
MELLAGTGLWPMAIFTVIFILLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQVDLCNMPYSMYKLQNRYGDVFSLQMGWKPVVVINGLKAVQELLVTCGEDTADRPEMPIFQHIGYGHKAKGVVLAPYGPEWREQRRFSVSTLRNFGVGKKSLEQWVTDEASHLCDALTAEAGRPLDPYTLLNKAVCNVIASLIYARRFDYGDPDFIKVLKILKESMGEQTGLFPEVLNMFPVLLRIPGLADKVFPGQKTFLTMVDNLVTEHKKTWDPDQPPRDLTDAFLAEIEKAKGNPESSFNDANLRLVVNDLFGAGMVTTSITLTWALLLMILHPDVQCRVQQEIDEVIGQVRHPEMADQAHMPFTNAVIHEVQRFADIVPMNLPHKTSRDIEVQGFLIPKGTTLIPNLSSVLKDETVWEKPLRFHPEHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPTGQPRPSDYGVFAFLLSPSPYQLCAFKR