wanglab/gogpt-training-data huggingface dataset:
Protein: Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (CRII-7) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin) (Q9QYV0)
Organism: Rattus norvegicus (Rat)
Function: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity). {ECO:0000250}.
Interaction partners:
- Sorting nexin
- Cadherin-1
- SH3 and PX domain-containing protein 2A
Sequence:
MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTQSRSLENQVVQDSPPINLTEVLQTGLPETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVLSPERSYTLELGPGDLQRPLIVSRIQDLLLPGHTCAPSWHAFVPTEAAPDLLLEQHHLRRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGNSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRWALEKALLDGMGSCLFEWPPSRAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASDGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPDIRLGDGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPSGSYMPCNLRDAICGQLQCQWGRNQPLLGSVQDQLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRSKCHGHGVCDSSRHCHCDEGWAPPDCMTQLRATSSLTTGLLLSLLLLLVLVLLGASYWYRARLHQRLCQLKGSSCQYRAAQSGPPERPGPPQRAQQMPGTKQANVSFPVPPSRPLPPNPVPKKLQAELADRSNPPTRPLPADPVVWRPKPQGPTKPPPPRKPLPANPQGRPPLGDLPGPGDGSLQLVVPSRPAPPPPAASSLYL
Protein: Pyrimidine-specific ribonucleoside hydrolase RihB (EC 3.2.2.8) (Cytidine/uridine-specific hydrolase) (P33022)
Organism: Escherichia coli (strain K12)
Function: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. Has a low but significant activity for the purine nucleoside xanthosine.
Interaction partners:
- Cytidine deaminase
- Uridine kinase
- Cytosine deaminase
- Guanine deaminase
- Purine nucleoside phosphorylase DeoD-type
- Adenosine deaminase
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
- Hypoxanthine phosphoribosyltransferase
- Guanosine-inosine kinase
- Xanthine-guanine phosphoribosyltransferase
Sequence:
MEKRKIILDCDPGHDDAIAIMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH
Protein: Glia maturation factor gamma (GMF-gamma) (Q9ERL7)
Organism: Mus musculus (Mouse)
Interaction partners:
- Actin-related protein 2
Sequence:
MSDSLVVCEVDPELKETLRKFRFRKETNNAAIIMKVDKDRQMVVLEDELQNISPEELKLELPERQPRFVVYSYKYVHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNRLVQTAELTKVFEIRTTDDLTETWLKEKLAFFR
Protein: HMG-box transcription factor 1 (C9JQU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVWEVKTNQMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEVDWLTELANIATSPQSP
Protein: Cytochrome P450 2J2 (EC 1.14.14.-) (Albendazole monooxygenase (hydroxylating)) (EC 1.14.14.74) (Albendazole monooxygenase (sulfoxide-forming)) (EC 1.14.14.73) (Arachidonic acid epoxygenase) (CYPIIJ2) (Hydroperoxy icosatetraenoate isomerase) (EC 5.4.4.7) (P51589)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of PUFA. Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools. In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15-lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent. Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone. Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole. Catalyzes the sulfoxidation of fenbedazole.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:8631948}; Peripheral membrane protein.
Interaction partners:
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 4F3
- Cytochrome P450 4A11
- Cytochrome P450 4F2
- Cytochrome P450 3A4)
- Cytochrome P450 4A22
- Cytochrome P450 4F8
- Cytochrome P450 2E1
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 1A2
Sequence:
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVDFEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHIFKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDPHFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFLPGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMPYTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDTFNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLSLKFRMGITISPVSHRLCAVPQV
Protein: Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) (Q66HR2)
Organism: Rattus norvegicus (Rat)
Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules. Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (By similarity). May play a role in cell migration (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15691}. Golgi apparatus {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15691}. Note=Associated with the microtubule growing distal tips. In addition to localizing to microtubule plus-ends, also exhibits some localization along the length of the microtubules. Recruitment to the Golgi apparatus requires the presence of PDE4DIP isoform 13/MMG8/SMYLE. {ECO:0000250|UniProtKB:Q15691}.
Interaction partners:
- CAP-Gly domain-containing linker protein 1
- Dynactin subunit 1
- Microtubule-associated protein RP/EB family member 3
- Serine/threonine-protein kinase PLK1
- Kinesin-like protein KIF17
- Adenomatous polyposis coli protein
- Cyclin-dependent kinase 1
- Cell division cycle protein 20 homolog
- Nuclear migration protein nudC
- Cytoskeleton-associated protein 5
Sequence:
MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETAVAPSLVAPALSKPKKPLGSGSAAPQRPIATQRTTAAPKAGPGMVRKNPGMGNGDDEAAELMQQVKVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY
Protein: Uncharacterized protein (Q57UN4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMEKQWIVSSLLRSSEQGNAEGVNAFSTTTLGLKRQRDSQFYDGDGKPLRGLRREAASLMYNNRYLSEEELHRLEQSLSAGQGNTSVTSTADGKGGGSARRILNGLPALPDMFGVVPSTTSGGKAAKSAGGENGDSRWAVPAMNRWFLVQRNHVVQNRLTEGGNNSNDESAQQLGHQSAHMGGCGYRWVRADALQVESALTGSLVVAAMPVADTGASTGRTEMGSGGAKHKRVQEELQESWISQACLLAPPETEFSVADAYKGSDPFSFFTVSEDEYRILNLESPQFQPSFLSRHNDVEEATPHHFNFDATMKLLTMYERFGNFVVVADRWTYANASGTGPADVNGADETLLPPPVEALMERYKLVSEAVLQYRLHMLRTVLRDGKSGRCDEAVAAAVGCRKPESRASREAVVAKSQKDTDDRLIASSHPLVSLMLKHPILETQRQRQEWLTQKFREIKDDDGKSCNNNDNGNPNKEDTNDEVSATANAASEIAMINGHRRSYLKDLAVMGTSSLSNHLDSSQMQNSRDHGDGGTSFAVGGNARSGSASPLESQLSVPLNICPIPTASPFWYDGLLERVRRERLREDMILESRENVPYHVALMSLQKVGKQAKVLFDRLRTLTQETVAASVEEPEESDVSTRASGTSAVVDTGVGGKEGRGARPGKLATAKQCKKRQQQQLTDPSSEDSYQAVQEEVRRVPAICERLKLCVQAGWFLPPSYLGKGCGSDLKGSNGNTNNENSGGNRGAPVGGSSGGTNIIANRVLSNSSEALLLSLPPNTPRIHRSVEHELEKHLWEDHRALCDDSAEVQQLLGEVRVLYTQNVILRRFAGRCGTLKASLKKLASDASSMKI
Protein: ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein) (P91283)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAQLMKRGFSTSAALAKAQLVKTPIQVHGVEGRYAAALYSAGHKQNKLDQISTDLNNVRSVYKDNKKFQEFVLDPTLKANKKKTAIEAISTKLGLTKETGNFLGLLAENGRLNKLESVVSSFESIMRAHRGELFVQVTSAEELSSSNQKALSDALSKIGKSGQKLTVTYAVKPSILGGLVVTIGDKYVDLSIASRVKKYKDALATAI
Protein: Double-stranded RNA-binding protein 2 (dsRNA-binding protein 2) (AtDRB2) (Q9SKN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds double-stranded RNA. May be involved in RNA-mediated silencing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15821876}.
Interaction partners:
- Endoribonuclease Dicer homolog 1
- Endoribonuclease Dicer homolog 3
- Dicer-like protein 4
- Protein DCL homolog, chloroplastic
- Protein NUCLEAR FUSION DEFECTIVE 2
- Endoribonuclease Dicer homolog 2
- Protein argonaute 1
- RBR-type E3 ubiquitin transferase
- Protein SUO
- Molybdopterin synthase catalytic subunit
Sequence:
MYKNQLQELAQRSCFNLPSYTCIREGPDHAPRFKATVNFNGEIFESPQYCSTLRQAEHSAAEVALNALSNRGPSHSLAARILDETGVYKNLLQEIAQRVGAPLPRYTTFRSGLGHQPVFTGTVELAGITFTGDPAKNKKQAEKNAAMAAWSSLKQLAKETSSSMPEPENIDELEQVIIARALINYRIKENIGTGSSSSAPVPFAKKFFMQNLRPTSPQPSPATTSRILPFICPKQPSRSSRSSLAATSGIDRIMAAALESRSYQRPQQRFANPPYVPMRQFRSQCHGMAPPVTIRTAVPVFSAPPMPPPPCTNNTQLPSSVYVPSLMRTAPPVRIAPPVTIRTAVPVFASAPPVRIRTAVKPTVEAGETRISSVQEKESIPVLPDSLEIGVEGSTITITDCEKTASKETERAEFKDSSKGEPETARERLENLKI
Protein: Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (Q8QZT1)
Organism: Mus musculus (Mouse)
Function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P24752}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetoacetyl-CoA synthetase
Sequence:
MAALVALHGVVRRPLLRGLLQEVRCLERSYASKPTLNEVVIVSAIRTPIGSFLGSLASQPATKLGTAAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPISTPCTTVNKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDGLTDVYNKIHMGNCAENTAKKMNISRQEQDTYALSSYTRSKEAWDAGKFASEITPITISVKGKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTITAANASTLNDGAAALVLMTAEAAQRLNVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLANIKMLEIDPQKVNIHGGAVSLGHPIGMSGARIVVHMAHALKPGEFGLASICNGGGGASALLIEKL
Protein: Succinate-semialdehyde dehydrogenase [NADP(+)] (SSA dehydrogenase) (SSADH) (SSDH) (EC 1.2.1.16) (P38067)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 4-aminobutyrate aminotransferase
- Glutamate decarboxylase
- Transcriptional activator protein UGA3
- NAD-specific glutamate dehydrogenase
- Transcriptional activator protein DAL81
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Citrate synthase, peroxisomal
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MTLSKYSKPTLNDPNLFRESGYIDGKWVKGTDEVFEVVDPASGEIIARVPEQPVSVVEEAIDVAYETFKTYKNTTPRERAKWLRNMYNLMLENLDDLATIITLENGKALGEAKGEIKYAASYFEWYAEEAPRLYGATIQPLNPHNRVFTIRQPVGVCGIICPWNFPSAMITRKAAAALAVGCTVVIKPDSQTPLSALAMAYLAEKAGFPKGSFNVILSHANTPKLGKTLCESPKVKKVTFTGSTNVGKILMKQSSSTLKKLSFELGGNAPFIVFEDADLDQALEQAMACKFRGLGQTCVCANRLYVHSSIIDKFAKLLAERVKKFVIGHGLDPKTTHGCVINSSAIEKVERHKQDAIDKGAKVVLEGGRLTELGPNFYAPVILSHVPSTAIVSKEETFGPLCPIFSFDTMEEVVGYANDTEFGLAAYVFSKNVNTLYTVSEALETGMVSCNTGVFSDCSIPFGGVKESGFGREGSLYGIEDYTVLKTITIGNLPNSI
Protein: Uncharacterized protein, isoform A (EC 3.4.21.-) (Uncharacterized protein, isoform B) (Q9VRS3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE65433p
- Uncharacterized protein
Sequence:
MKVFAVLVLAIATVSADILRQDTPVHPRDSSAVPSIDGRITNGNKAAANQFPYQVGLSFKSSAGSWWCGGSIIANTWVLTAAHCTKGASSVTIYYGSTVRTSAKLKKKVSSSKFVQHAGYNAATLRNDISLIKTPSVTFTVSINKIALPAIASSYSTYAGQTAVASGWGRTSDSSIAVATNLQYAQFQVITNAVCQKTFGSSVVTSGVICVESINKKSTCQGDSGGPLALNNRLIGVTSFVSSKGCEKNAPAGFTRVTSYLDWIKNQSGVFY
Protein: TAP binding protein (A0A023IM54)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLLPLLVVVALGLATVVVSAGPQTIECWFVEDAGGGGLSKKPATLLLRHGPRGPPPRPDLDPKLYFKVDDPAGMLLAAFRRYPAGAHAPHCEMSSYIPFPASAKWARGLSPQQNCSRALDGDWLMVSVSGTVFSLSSLLRPLPEPQREPVFITMATVVLTVLTHHPAPRIHLGKDAVLDLRFAYAPPALEDAPSVASGPPPFGLEWRRQHRGKGHLLLAAIPGLLEKMPPAREKAVAFAAWDDDNDPWGPWTGNGTLWLPAVSPSQEGVYLATVHLPYLQGQVSLELTVHKPPRVSLTPAPIVWAAPGEAPPELLCLVSHFYPEEGLEVEWELRGGPEGSSRKAEGKTWVSTVRHHSDGSVSQSGHLQLPPVTDKQHGVRYACRVRHPSLPSSGRSAEVTLEVAGFSGPSIEDGIGLFLSAFLLLGLFKALGWMAAYLTIPKILKEKASATSLTVPKDEKKSE
Protein: Mediator of RNA polymerase II transcription subunit 29 (Intersex-like protein) (Mediator complex subunit 29) (B4DUA7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLKSNGERRSRNALPAVYARKMAASQQQASAASSAAGVSGPSSAGGPGPQQQPQPPAQLVGPAQSGLLQQQQQDFDPVQRYKMLIPQLKESLQTLMKVAAQNLIQNTNIDNGQKSSDGPIQRFDKCLEEFYALCDQLELCLRLAHECLSQSCDSAKHSPTLVPTATKPDAVQPDSLPYPQYLAVIKAQISCAKDIHTALLDCANKVTGKTPAPPAGPGGTL
Protein: Small ribosomal subunit protein uS4 (40S ribosomal protein S9) (P55935)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P46781}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46781}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P46781}.
Interaction partners:
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL33
- GEO07453p1
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS7A
- Large ribosomal subunit protein eL6
Sequence:
MVNGRIPSVFSKTYVTPRRPYEKARLDQELKIIGEYGLRNKREVWRVKYALAKIRKAARELLTLDEKDEKRLFQGNALLRRLVRIGVLDESRMKLDYVLGLKIEDFLERRLQTQVFKLGLAKSIHHARVLIRQRHIRVRKQVVNIPSFVVRLDSQKHIDFSLKSPFGGGRPGRVKRKNLKKNQGGGGGAAEEEED
Protein: Alpha-2C adrenergic receptor (Alpha-2 adrenergic receptor subtype C4) (Alpha-2C adrenoreceptor) (Alpha-2C adrenoceptor) (Alpha-2CAR) (P22086)
Organism: Rattus norvegicus (Rat)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-11
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Sequence:
MASPALAAALAAAAAEGPNGSDAGEWGSGGGANASGTDWGPPPGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMAYWYFGQVWCGVYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSFYRRPDGAAYPQCGLNDETWYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTRTLSEKRGPAGPDGASPTTENGLGKAAGENGHCAPPRTEVEPDESSAAERRRRRGALRRGGRRREGAEGDTGSADGPGPGLAAEQGARTASRSPGPGGRLSRASSRSVEFFLSRRRRARSSVCRRKVAQAREKRFTFVLAVVMGVFVLCWFPFFFSYSLYGICREACQLPEPLFKFFFWIGYCNSSLNPVIYTVFNQDFRRSFKHILFRRRRRGFRQ
Protein: Beta-lactoglobulin (Beta-LG) (P02756)
Organism: Capra hircus (Goat)
Function: Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Subcellular location: Secreted.
Interaction partners:
- Alpha-lactalbumin
- Kappa-casein
- Lactotransferrin
- Albumin
- Beta-casein
- Lactoperoxidase
- Prochymosin
- Myoglobin
- Glycosylation-dependent cell adhesion molecule 1
Sequence:
MKCLLLALGLALACGIQAIIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGNLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDKEALEKFDKALKALPMHIRLAFNPTQLEGQCHV
Protein: E3 ubiquitin-protein ligase SMURF1 (xSMURF1) (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF1) (SMAD ubiquitination regulatory factor 1) (SMAD-specific E3 ubiquitin-protein ligase 1) (Q9PUN2)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of smad1 and smad5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and rhoa. May play a role in dendrite formation by melanocytes.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
Sequence:
MSNVVTRRGGSSIRVRLTVLCAKNLAKRDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKMDSITISIWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPTDNDAVRGQIVVSLQTRDRIGTLGSVVDCRGLLDNEGALLEDTGPGRPLSCFMDEPAPYTDGPGAAGGGPGRLVESPGQEQRLQAQRVRGPEVREHVQTPQNRSHGFQSQDLPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDDLGSLPAGWEVRTTVSGRIYFVDHNNRTTQFTDPRLHHIINHQSQLKEPNHAIPVQSDGSLEDGDEFPAQRYERDLVQKLKVLRHELSLLQPQAGHCRVEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITSVLDHTFCVEHNAFGRLLQHELKPNGKNLQVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFEQKELELIIGGLDKIDISDWKANTRLKHCLANSNIVQWFWQAVESFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETSGFAVE
Protein: Zinc finger protein (O35745)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPFRCQKCGKSFVTLEKFTIHNYSHSRERPFKCSKAECGKAFVSKYKLMRHMATHSPQKIHQCTHCEKTFNRKDHLKNHLQTHDPNKISYACDDCGKKYHTMLGYKRHLALHSASNGDLTCGVCTLELGSTEVLLDHLKSHAEEKANQAPREKKYQCDHCDRCFYTRKDVRRHLVVHTGCKDFLCQFCAQRFGRKDHLTRHTKKTHSQELMQENMQAGDYQSNFQLIAPSTSFQIKVDPMPPFQLGAAPENGLDGGLPPEVHGLVLAAPEEAPQPMPPLEPLEPLEPLEPLEPMQSLEPLQPLEPMQPLEPMQPLEPMQPLEPLEPLEPMQPLEPMQPLEPMQPMLPMQPMQPMQPMQPMLPMQPMLPMQPMQPMQPMLPMPEPSFTLHPGVVPTSPPPIILQEHKYNPVPTSYAPFVGMPVKADGKAFCNVGFFEEFPLQEPQAPLKFNPCFEMPMEGFGKVTLSKELLVDAVNIAIPASLEISSLLGFWQLPPPTPQNGFVNSTIPVGPGEPLPHRITCLAQQQPPPLPPPPPLPLPQPLPVPQPLPQPQMQPQFQLQIQPQMQLPQLLPQLQPQQQPDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEEEQEEAEEEAEEGAEEGAEPEAQAEEEEEEEEAEEPQPEEAQIAGLVYKKWTV
Protein: PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic (pTAC6) (Plastid-encoded RNA polymerase-associated protein 8) (PEP-associated protein 8) (Q9XI19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein involved in plastid gene expression. Recruited by MTERF5 to the transcriptionally paused region of psbEFLJ. Promotes leaf greening.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:33001465, ECO:0000269|PubMed:35328480, ECO:0000305|PubMed:16326926, ECO:0000305|PubMed:31128276}. Plastid, chloroplast thylakoid {ECO:0000269|PubMed:35328480}. Nucleus {ECO:0000269|PubMed:33001465, ECO:0000269|PubMed:35328480}. Nucleus, nucleoplasm {ECO:0000269|PubMed:35328480}. Note=Translocates to the chloroplast via its transit peptide and then take part of the plastid-encoded RNA polymerase (PEP) complex (PubMed:33001465). When in the nucleus, can bind to PTAC12/HMR/PAP5 (PubMed:33001465). Both localization are observed in the dark or under white light, mainly present in the nucleus of etiolated seedlings while enriched in chloroplast after light exposure (PubMed:33001465, PubMed:35328480). {ECO:0000269|PubMed:33001465, ECO:0000269|PubMed:35328480}.
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Fructokinase-like 2, chloroplastic
- Plastid transcriptionally active 3
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Thioredoxin-like protein CITRX, chloroplastic
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- Fructokinase-like 1, chloroplastic
- Protein PLASTID REDOX INSENSITIVE 2
Sequence:
MASSAASPSLSLLSFTSKPPYPSGSQRLFASFRTDGLFAPLTLKSRRGRGIVVKVDDVDADGGGADEYDMDDEEVEEVDNKKDYDVEYDPLAAAIAAAGGGGDGDIAFVQSKSFISTQGWDSDMVVDYRINEDEFHKLSLMDCDFFIRKPPDPDNDVYDFREMYVTPPDTDIYSIPRVLAPMPQKYIRCAMSDYGCYNVTEPPIDAPRDPLYKSEREISKVFLTKHYRNRRTNDPEFVLDLEEIYVIDSKTKSITRARVLVTVPGGRKRDRKDDLLVIRDNGTSFKIIHVGERDDPTTVIEREEWTKTREDMEKHLRKLRDFSVSNWF
Protein: C-X-C chemokine receptor type 5 (CXC-R5) (CXCR-5) (Burkitt lymphoma receptor 1 homolog) (CD antigen CD185) (Q04683)
Organism: Mus musculus (Mouse)
Function: Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-X-C motif chemokine 13
- Stromal cell-derived factor 1
- C-C motif chemokine 19
- C-C motif chemokine
- C-X-C motif chemokine 10
- C-X-C motif chemokine 9
- C-X-C chemokine receptor type 4
- B-lymphocyte antigen CD19
- Guanine nucleotide-binding protein G
- C-C motif chemokine 5
Sequence:
MNYPLTLDMGSITYNMDDLYKELAFYSNSTEIPLQDSNFCSTVEGPLLTSFKAVFMPVAYSLIFLLGMMGNILVLVILERHRHTRSSTETFLFHLAVADLLLVFILPFAVAEGSVGWVLGTFLCKTVIALHKINFYCSSLLLACIAVDRYLAIVHAVHAYRRRRLLSIHITCTAIWLAGFLFALPELLFAKVGQPHNNDSLPQCTFSQENEAETRAWFTSRFLYHIGGFLLPMLVMGWCYVGVVHRLLQAQRRPQRQKAVRVAILVTSIFFLCWSPYHIVIFLDTLERLKAVNSSCELSGYLSVAITLCEFLGLAHCCLNPMLYTFAGVKFRSDLSRLLTKLGCAGPASLCQLFPNWRKSSLSESENATSLTTF