wanglab/gogpt-training-data huggingface dataset:
Protein: Actin, gamma-enteric smooth muscle (EC 3.6.4.-) (Alpha-actin-3) (Gamma-2-actin) (Smooth muscle gamma-actin) [Cleaved into: Actin, gamma-enteric smooth muscle, intermediate form] (P63267)
Organism: Homo sapiens (Human)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Myosin-11
- Actin, aortic smooth muscle
- Myosin regulatory light polypeptide 9
- Actin, alpha skeletal muscle
- Myosin-9
- Myosin-10
- Myosin light polypeptide 6
- Actin, alpha cardiac muscle 1
- Myosin light chain 6B
- Calponin-1
Sequence:
MCEEETTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKPEYDEAGPSIVHRKCF
Protein: Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10) (Q61391)
Organism: Mus musculus (Mouse)
Function: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (By similarity). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (By similarity). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (By similarity). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (By similarity). Involved in the degradation of the atrial natriuretic factor (ANF) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08473}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Angiotensin-converting enzyme 2
- Dipeptidyl peptidase 4
- Lysosomal Pro-X carboxypeptidase
- Angiotensinogen
- Meprin A subunit beta
- Meprin A subunit alpha
- Insulin-degrading enzyme
- Angiotensin-converting enzyme
- B-lymphocyte antigen CD19
- Aminopeptidase N
Sequence:
MGRSESQMDITDINAPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDASVEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGQPLLKLLPDIYGWPVASDNWDQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQSLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEVNGKSFSWSNFTNEIMSTVNINIQNEEEVVVYAPEYLTKLKPILTKYSPRDLQNLMSWRFIMDLVSSLSRNYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIISNENKLNNEYLELNYREDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKDQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFADAFHCRKNSYMNPERKCRVW
Protein: Myomesin 2 (G3V7K1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Myozenin 1
- Titin
- Actinin alpha 3
Sequence:
MSLVVVPFYQKRHKHFDQSYRNIQTRYLLDRYASKKQASSQSSSQRSLTERSSSKRASSQSSAEGMTCRLCAKRMSASEEEEVENENRYRSLAASYGEAKRQRFLSELAQLEENVQLARTQARNKLDKYFLEQTVADNLALERSSFEDRLSRAPEILVRLRSHTIWERMSVRLCFTVQGFPTPVVQWYKDGSLICQAGEPGKYRIESRYGVHTLEINRADFEDTATYSAVATNPHGQVSTNAAVVVRRYRGDEEPYHSVGLPIGLPLSSVIPYTHFDVQFLEKFGVTFRREGETVTLKCTLLVTPDLKRVQPRAEWYRDDVLLKESKWTKMFFGEGQASLSFSHLNKDDEGLYTLRIVSRGGVSDHSAFMFVRDADPLVTGAPGAPMDLQCHDANRDYVIVTWKPPNTTTESPVIGYFIDKCEVGTNNWVQCNDAPVKICKYPVTGLFEGRSYVFRVRAVNNAGISRPSRISDAVAALDPVDLRRLQAIHLEGEKEIVIYQDDLEGDVQIPGPPTNVQASEVSRNYVVLSWDPPSPRGKEPLMYFIEKSAVGSGSWQRVNAQTAVRSPRYAVFDLAEGKSYVFRVLSANKHGLSDPSEITPPIQAQDMIVVPSAPGRVLASRNTKTSVVVQWDRPKHEEDLLGYYVDCCVAGTNMWEPCNHKPIGYNRFVVHGLTTGEQYIFRVKAVNAVGTSENSQESEVIKVQAALTVPSHPYGITLLNCDGHSMTLGWKVPKFSGGSAIIGYYLDKREVHHKNWHEINSSPVKERILTVEGLTEGSLYEFKIAATNLAGIGQPSDPSEHFKCEAWTAPEPGPAYDLTFCEVRDTSLVILWKAPVYSGSSPVSGYFVDFKEEDSGEWKTTSEAATPNRYLKVCDLHQGKTYVFRVRAVNASGPGKPSDTSEPVLVEARPGTKEISAGVDEEGNIYLGFDCQEMTDASQFTWCKAYEEIADEERFEVHTEGDHSKLYFKNPDKIDIGTYSVSVSDTDGVSSSFVLDEEELERLMALSNEIKNPTIPLKSELAYEIFDKGQVRFWLQAEHLSPDANFRFIINDREVSDSETHRIKCDRSTGMIEMVMDRFTIENEGTYTVQIQDGKAKNQSSLVLIGDAFRAVLEEAEFQRKEFLRKQGPHFAEYLHWDVTEECEVRLICKVANTKRETVFKWLKDDVLYETETPPPDLEKGICELLIPKLSKKDHGEYKATLKDDRGQDVSVLEVAGKVYEDMILAMSRVCGASASPLKVLCTPEGIRLQCFMKYFTEEMKVSWYHKEAKISSSEHMRIGGSEEMAWLQICEPTEKDKGKYTFEIFDGKDNHQRSLDLSGQAFDEAYAEFQQLKPPVGSPSATPLFSIADRGKVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVVWFKNDKDIELSEHFSVKVEQSKYVSLTIKGVTAEDSGKYSINVKNKYGGEKIDVTVSVYKHGEKIPDISAPQQAKPKLIPASTSAD
Protein: guanylate cyclase (EC 4.6.1.2) (F8VQK3)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Guanylate cyclase soluble subunit beta-1
- cGMP-dependent protein kinase 2
- cGMP-dependent protein kinase 1
- guanylate cyclase
- Nitric oxide synthase 1
- Inosine triphosphate pyrophosphatase
- Bis
- Guanylate cyclase soluble subunit alpha-1
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
Sequence:
MSRRKISSESFSSLSSDYLETSPEEEGECPLSRLCWNGSRSPPGPPGSREAAKAATSAPAASAAAASAAVAAEYKRAQRRGRVNLDSLGESISLLTAPLPQTIHMTLKRTLQYYEHQVIGYRDAEKNFHNISKRCSYADHSNKEEIEDVSGILQCTANVLGLQFQEIQERFGEEFFKICFDENERVLRAVGSTLQDFFNGFDALLEHIRTSFGKQATLESSSFLCKELPEGTLMLHYFHPHHTVGFAMLGMIKAAGKRIYHLNVEVEQIENEKLCFDGSNPSNCSCLTFLIKECETTQITKDNPQGTSQVPADLRISINTFCRAFPFHLMFDSNMVVLQLGEGLRKQLRYDTHRALKFEDCFEIVSPMINATFDRVLLRLSTPFVIRTKPEASGTENEDKVMEIKGQMIHVPESSAILFLGSPCVDKLDELMGRGLHLSDIPIHDATRDVILVGEQAKAQDGLKKRMDKLKATLERTHQALEEEKKKTVDLLYSIFPGDVAQQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPMQVISMLNELYTRFDHQCGLLDIYKVETIGDAYCVASGLHRKSLCHAKPIALMALKMMELSEEVLTPDGKAIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSPTTYQLLKREDSFTFIPRSREELPDNFPKEIPGVCYFLELRTDPKPPKPSLSSSRIKKVSYNIGTMFLRETSL
Protein: T24P13.9 (Transmembrane protein) (Q9LQY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTIPTYNLLCIGSFIFLLCFSITFGRKNLLDKPGGTLYASKPVEAAELRATLVTNTKARDISSNIGLGEVGSQEMHHTYIGTGEDSSLGNKQDNINSVPRKVIRGIVSISFAFPIIKIQVPIPKPNITVAAINQLDEEEMIKGIVITPTKTNELCISLGNYDVELSYS
Protein: Serine protease K12H4.7 (Q9VDX5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- alpha-glucosidase
Sequence:
MKYTLVVLALLAPLTAAASLGEQKPEANAFVKSLRELHRGPPVEPMKTRAKVEERWITQKLDNFDDSNNATWQDRIYINNKYFVDGSPIFIYLGGEWAIDPSGITSGLWKDIAKQHNGSLLYTEHRFFGQSIPITPLSTENLAKYQSVEQALADVINVIATLKQEDKYKDSKVVVSGCSYSATMATWIRKLYPEIIRGSWASSAPLLAKVNFKDYMKVVGESYATLGGQYCYDLIDNATSYYENLFEIGNGTQAVKELNLCSNFNVNSEQDRWQIFSTIANIFAGIAQYQKPEKYDIPTYCSILREFSDDDSVALSKFINWKINEHSGACLSTTFKGAVGYYEWSKENYQDSDLPWIFQTCSEFGWFQSSGSRSQPFGSTFPATLYEDTCEGVFGAKYDSAGIHANIRATNDDFGGLNVNATNIYFVQGALDGWSKVGAGVAQGATIIPYASHCPDTGSISASDSAELVASKKKLIKLVAQWLED
Protein: Beta-defensin 132 (Beta-defensin 32) (BD-32) (DEFB-32) (Defensin HEL-75) (Defensin, beta 132) (Q7Z7B7)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Beta-defensin 127
- Beta-defensin 128
- Defensin beta 118
- Beta-defensin 134
- Beta-defensin 125
- Beta-defensin 129
- Beta-defensin 126
- Beta-defensin 110
- Beta-defensin 1
- Beta-defensin 131A
Sequence:
MKFLLLVLAALGFLTQVIPASAGGSKCVSNTPGYCRTCCHWGETALFMCNASRKCCISYSFLPKPDLPQLIGNHWQSRRRNTQRKDKKQQTTVTS
Protein: Alpha/beta-Hydrolases superfamily protein (At3g24420) (Hydrolase-like protein) (Q9LK01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g15630/MSJ11_3
- F-box/kelch-repeat protein SKIP25
- 2-oxoglutarate
- Protein SMAX1-LIKE 2
- Protein SUPPRESSOR OF MAX2 1
Sequence:
MVVNQKISGLASAMNAKIIGSGERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAIKDQTLYDPSKYNSLDVFSDDLIALMEELKFGPVVFVGHSMSGVIGCAASIKRPDLFTNLLLIAASPRYINSEDYKGGFESKDIDTIITSIGSNYEAWAVDFSSFVVDSRDSLSVQRFEKSLKKMKPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGKSTVEIIEDAIGHFPQMTSHLELLGVMRRLLEF
Protein: Protein disulfide-isomerase (EC 5.3.4.1) (C0H4Y6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Endoplasmic reticulum oxidoreductin, putative
- Endoplasmic reticulum chaperone BIP
- Endoplasmic reticulum chaperone GRP170
- Protein disulfide isomerase
- Small ribosomal subunit protein eS30
- Ran-specific GTPase-activating protein 1, putative
- DnaJ protein, putative
Sequence:
MNRKYFSSLFLFLISFVFESFVRSHGDLFNHFVTDIHDGELDKFITKNDIVLVMFYAPWCGHCKRLIPEYNEAANMLNEKKSEIKLVSIDATSENALAQEYGITGYPTLILFNKKNKINYGGGRTAQSIVDWLLQMTGPVFSHVEGNIEDVLKEKKINVAFYLEYTSEDNDLYKKFNEVGDKNREIAKYFVKKNDKHNKLFCFRTDEKKVEYDEKTPLEEFVTSESFPLFGEINTENYRFYAESPKELVWVCATYEQYNEIKEHVRLAAQELRKKTHFVLLNIPEYAEHAKASLGLTEFPGLAFQSNEGRYLLKNPKESLLNHNAIINFFKDVEAGKIEKSLKSEPIPEDDKNAPVKIVVGNSFVDVVLKSGKDVLIEIYAPWCGHCKKLEPVYEDLGRKLKKYDSIIVAKMDGTLNETPIKDFEWSGFPTIFFVKAGSKIPLPYEGERSLKGFVDFLNKHATNTPISIDGVPEFEDGTSEEL
Protein: V-type proton ATPase subunit B 2 (V-ATPase subunit B 2) (Defective spermatogenesis protein 5) (Vacuolar proton pump subunit B 2) (Q9N5A0)
Organism: Caenorhabditis elegans
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (Probable). In neurons, required for necrotic cell death probably by promoting intracellular acidification. Required for spermatogenesis where it regulates the fibrous body-membranous organelle (FBMO) morphology in spermatocytes and the acidification of FBMO-derived secretory membranous organelles (MOs) as spermatids mature.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22446317}. Note=In spermatocytes at the meiotic I stage, localizes to the cytoplasm and to discrete dots (PubMed:22446317). In spermatids and the residual body, localizes to discrete dots in the cytoplasm (PubMed:22446317). In budded spermatids, localizes near the cell membrane as discrete dots that are adjacent to secretory membranous organelles (MOs) (PubMed:22446317). {ECO:0000269|PubMed:22446317}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- Probable V-type proton ATPase subunit H 2
- Probable V-type proton ATPase subunit G
- V-type proton ATPase subunit E
- Probable V-type proton ATPase subunit H 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
Sequence:
MTEASEINLSDIKGPIDVNTPITNHRTALIQNYSTKPKLTYQTVFGVNGPLVIVHNVKFPMFNEIVKITLPNGQIRMGQVLESSKNKAVVQVFEGTTGVDAKFTTCEFTGDIFRSPVSLDMLGRIFNGSGKPIDKGPPVLPEDYLDINGQPINPFNRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQIVRQGGLVQLPGRNNETVNFAIVFAAMGVNMETARFFKQDFEECGSMDNVCLFLNLANDPTIERIITPRIALTAAEFFAYHCGKHVLVVLTDMSSYAEALREISAAREEVPGRRGFPGYMYTDLATIYERAGRVKGREGSITQIPILTMPNNDITHPIPDLTGYITEGQIYIDKQLHKRLIYPPIDVLPSLSRLMKSAVGEGMTREDHSDLSNQLYACYAMGKDVQAMKAVVGVEALSPDDLLYLEFLAKFEKNFIAQGRYENRTIVESLNIGWELLRIFPREMLKRIPETLLEKYYKRKKQ
Protein: MSL complex subunit 3 (Male-specific lethal 3 homolog) (Male-specific lethal-3 homolog 1) (Male-specific lethal-3 protein-like 1) (MSL3-like 1) (Q8N5Y2)
Organism: Homo sapiens (Human)
Function: Has a role in chromatin remodeling and transcriptional regulation. Has a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:30224647}.
Interaction partners:
- Male-specific lethal 1 homolog
- E3 ubiquitin-protein ligase MSL2
- Histone acetyltransferase KAT8
- Histone H4
- Histone acetyltransferase KAT5
- DNA methyltransferase 1-associated protein 1
- Enhancer of polycomb homolog 1
- Chromatin modification-related protein MEAF6
- Transformation/transcription domain-associated protein
- Inhibitor of growth protein 3
Sequence:
MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAKIVDVIVGKDEKGRKIPEYLIHFNGWNRSWDRWAAEDHVLRDTDENRRLQRKLARKAVARLRSTGRKKKRCRLPGVDSVLKGLPTEEKDENDENSLSSSSDCSENKDEEISEESDIEEKTEVKEEPELQTRREMEERTITIEIPEVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHVMPHANMNVHYIPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQAQYKKVTSSKFFLPIKESATSTNRSQEELSPSPPLLNPSTPQSTESQPTTGEPATPKRRKAEPEALQSLRRSTRHSANCDRLSESSASPQPKRRQQDTSASMPKLFLHLEKKTPVHSRSSSPIPLTPSKEGSAVFAGFEGRRTNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY
Protein: Glucose-6-phosphate exchanger SLC37A4 (Glucose-5-phosphate transporter) (Glucose-6-phosphate translocase) (Solute carrier family 37 member 4) (Transformation-related gene 19 protein) (TRG-19) (O43826)
Organism: Homo sapiens (Human)
Function: Inorganic phosphate and glucose-6-phosphate antiporter of the endoplasmic reticulum. Transports cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocates inorganic phosphate into the opposite direction. Forms with glucose-6-phosphatase the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it plays a central role in homeostatic regulation of blood glucose levels.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:32884905, ECO:0000269|PubMed:33964207}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glucose-6-phosphatase catalytic subunit 1
- Glucose-6-phosphatase 3
- Glucose-6-phosphatase 2
- Sodium-dependent phosphate transport protein 4
- Granulocyte colony-stimulating factor
Sequence:
MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRVTVTSDSPKLWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICAASTAAFFLLRNIRTKMGRVSKKAE
Protein: Hepatocyte growth factor-like protein (Macrophage stimulatory protein) (MSP) [Cleaved into: Hepatocyte growth factor-like protein alpha chain; Hepatocyte growth factor-like protein beta chain] (P26928)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Macrophage-stimulating protein receptor
- Serine protease hepsin
- Kunitz-type protease inhibitor 2
- Kunitz-type protease inhibitor 1
- Hepatocyte growth factor receptor
Sequence:
MGWLPLLLLLVQCSRALGQRSPLNDFQLFRGTELRNLLHTAVPGPWQEDVADAEECARRCGPLLDCRAFHYNMSSHGCQLLPWTQHSLHTQLYHSSLCHLFQKKDYVRTCIMDNGVSYRGTVARTAGGLPCQAWSRRFPNDHKYTPTPKNGLEENFCRNPDGDPRGPWCYTTNRSVRFQSCGIKTCREAVCVLCNGEDYRGEVDVTESGRECQRWDLQHPHSHPFQPEKFLDKDLKDNYCRNPDGSERPWCYTTDPNVEREFCDLPSCGPNLPPTVKGSKSQRRNKGKALNCFRGKGEDYRGTTNTTSAGVPCQRWDAQSPHQHRFVPEKYACKDLRENFCRNPDGSEAPWCFTSRPGLRMAFCHQIPRCTEELVPEGCYHGSGEQYRGSVSKTRKGVQCQHWSSETPHKPQFTPTSAPQAGLEANFCRNPDGDSHGPWCYTLDPDILFDYCALQRCDDDQPPSILDPPDQVVFEKCGKRVDKSNKLRVVGGHPGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSCHEPLTGYEVWLGTINQNPQPGEANLQRVPVAKAVCGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGESIGTSNNTVLHVASMNVISNQECNTKYRGHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWINKVMQLE
Protein: Asialoglycoprotein receptor 1 (ASGP-R 1) (ASGPR 1) (Hepatic lectin 1) (HL-1) (rHL-1) (P02706)
Organism: Rattus norvegicus (Rat)
Function: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Asialoglycoprotein receptor 2
- Thyroglobulin
Sequence:
MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITSQNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHSRLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKYCQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQPDDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN
Protein: Ubiquitin-conjugating enzyme E2 Q1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Q1) (Galactosyl transferase-associated protein) (GTAP) (Ubiquitin carrier protein Q1) (Ubiquitin-protein ligase Q1) (Q7TSS2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Involved in female fertility and embryo implantation. May be involved in hormonal homeostasis in females. Involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18511602}. Cell projection, filopodium {ECO:0000269|PubMed:18511602}. Cytoplasm, cytosol {ECO:0000269|PubMed:18511602}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 Z
- Ubiquitin-conjugating enzyme E2Q-like protein 1
- Ubiquitin-conjugating enzyme E2 Q2
- Ubiquitin-conjugating enzyme E2 J1
- Ubiquitin-conjugating enzyme E2 G2
- Ubiquitin-conjugating enzyme E2 R2
- Ubiquitin-conjugating enzyme E2 J2
- Ubiquitin-conjugating enzyme E2 H
- Ubiquitin-conjugating enzyme E2 G1
- Ubiquitin-conjugating enzyme E2 A
Sequence:
MQQPQPQGQQQPGPGQQLGVQGAAPGAGGGPGGGPGPGPCLRRELKLLESIFHRGHERFRIASACLDELSCEFLLAGAGGAGAGAAPGPHLPSRGSVPGDPVRIHCNITESYPAVPPIWSVESDDPNLAAVLERLVDIKKGNTLLLQHLKRIISDLCKLYNLPQHPDVEMLDQPLPAEQCTQEEVSSEDEDEEMPEDTEDLDHYEMKEEEPAEGKKSEDDGIGKENLAILEKIKKNQRQDYLNGAVSGSVQATDRLMKELRDIYRSQSFKGGNYAVELVNDSLYDWNVKLLKVDQDSALHNDLQILKEKEGADFILLNFSFKDNFPFDPPFVRVVSPVLSGGYVLGGGAICMELLTKQGWSSAYSIESVIMQISATLVKGKARVQFGANKSQYSLTRAQQSYKSLVQIHEKNGWYTPPKEDG
Protein: Cytochrome P450 2C6 (EC 1.14.14.1) (CYPIIC6) (Cytochrome P450 PB1) (PTF2) (P05178)
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:
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 2U1
- Epoxide hydrolase 1
- unspecific monooxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Arachidonate 12-lipoxygenase, 12R-type
Sequence:
MDLVMLLVLTLTCLILLSIWRQSSGRGKLPPGPIPLPIIGNIFQLNVKNITQSLTSFSKVYGPVFTLYFGTKPTVILHGYEAVKEALIDHGEEFAERGSFPVAEKINKDLGIVFSHGNRWKEIRRFTLTTLRNLGMGKRNIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENMKILSSPWTQFCSFFPVLIDYCPGSHTTLAKNVYHIRNYLLKKIKEHQESLDVTNPRDFIDYYLIKWKQENHNPHSEFTLENLSITVTDLFGAGTETTSTTLRYALLLLLKCPEVTAKVQEEIDRVVGKHRSPCMQDRSRMPYTDAHDHEVQRFIDLIPTNLPHAVTCDIKFRNYLIPKGTTIITSLSSVLHDSKEFPDPEIFDPGHFLDGNGKFKKSDYFMPFSAGKRMCAGEGLARMELFLFLTTILQNFKLKSVLHPKDIDTTPVFNGFASLPPFYELCFIPL
Protein: DNA topoisomerase I (EC 5.6.2.1) (DNA topoisomerase 1) (P79994)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGDQLHNDSQIEADFRANDSHKHKDKHKDREHRHKEHKKDKEKDREKSKHSNSEHKDSSEKKHKDKEKTKHKDGSSEKHKDKHKDKDKEKRKEEKIKLSSGDIKIKKEKENGFSSPPRIKDEPDDDGFYASPKEDSKPLKRPREDDDADYKPKKIKTEDVKKAKKRKQEEEEDSKAKKAKNKDKKSPEADKRKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSTKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTSEEKSTITSLSKCDFTHMSQYFKAQTEARKQMSKEEKQKIKEENERLLKEYGYCVMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDSKVPPPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHIKLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTSILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTNPDDNIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQSKIDAKKEQLADARRELKSAKADAKVRRDEKSKKAVESKKKAVQRIEEQLMKLEVQATDREENKQIALSTSKLNYLDPRISVAWCKKWGIPIEKIYNKTQREKFAWAIDMAEEDYEF
Protein: Down syndrome cell adhesion molecule 1, isoform M (Q0E9I3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQHYEEDIHKAFVIRGNSAILKCDIPSFVADFVNVISWHSDEKENFYPGTEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVQPKISVGERRKDAEVPKHGDLSIFCPAQSYPVPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPQIQAFDFGSEAANTGEMAGGFCMVPKGDLPMEIRWTLNSAPIITGEHGFSLSRLNPRTSSLSIDSLEARHRGLYRCIASNKAGSAEYSAELHVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV