wanglab/gogpt-training-data huggingface dataset:
Protein: Chronophin (EC 3.1.3.16) (EC 3.1.3.74) (Protein serine phosphatase) (Pyridoxal phosphate phosphatase) (PLP phosphatase) (Q3ZBF9)
Organism: Bos taurus (Bovine)
Function: Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (By similarity). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
Interaction partners:
- Pyridoxal kinase
- Pyridoxine-5'-phosphate oxidase
- aldehyde oxidase
- aldehyde oxidase
- Aldehyde oxidase 1
- Pyridoxal phosphate phosphatase PHOSPHO2
- Cofilin-1
- Cofilin-2
- SH3 domain binding protein 1
- LIM domain kinase 1
Sequence:
MARCERLRGAALRDVVGRAQGVLFDCNGVLWNGERAVPGAPELLERLAQAGKATLFVSNNSRRARPELALRFARLGFGGLRSEQLFSSALCAARLLRQRLLGPPDTQGAVFVLGGEGLRAELRAAGLRLAGDPSEDPGAAPRVRAVLVGYDEHFSFAKLSEACAHLRDPDCLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITEHFSVDPGRTLMVGDRLETDILFGHRCGMTTVLTLTGVSSLEEAQAYLAAGQHDLVPHYYVESIADLMEGLED
Protein: Slowpoke 2, isoform L (A0A0B4KFK3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDHLLCNMAGNSRNSSYNCLSSWDSYDRIPRVRVEYYVNENTFKERLQLYFIKNQRSSLRIRIADLFLKLLSCVLYIIRVILDKNPTFITCYGCEVGNKTEFIISAKLTEEEFQENPIINWDAILWVNRPTVLWVLQLLLAMVSLTQSLVLTYLGYKGNIWQQILSFHFILELVTTIPFALTIVHPPLRNLFIPIFLNCWLAKRSLENMFNDLHRAMQKSQSALSQQLTILSATLLCLVFTSVCGIQHFQRAGHRHLNLFQSTYYVVVTFSTVGYGDFVPDIWPSQLYMVIMICVALIVLPTQFEQLAFTWMERQKLGGSYSSHRAQSEKHVVVCSTTLHADTIMDFLNEFYAHPLLQDFYVVLLSPMELDTTMRMILQVPIWAQRVIYIQGSCLKDGDLARARMNEAEACFILAARNYADKTAADEHTILRSWAVKDFAPNVPQYVQIFRPEHKLHVKFAEHVVCEDEFKYALLANNCTCPGASTLVTLLLHTSRGQEGQQSPEEWHRLYGKCSGNEIYHIVLGDSRFFGEYEGKSFTYASFHSHRKYGVALVGVRPAELPEFYEETILLNPGPRHIMKKDDTCYYMSITKEENSAFVVNQNQTSDPTAAAKEGSGTGGGGGASSSASHHHTAATASENPTAVIISDSRQNLKDTTVTQTAATITTTTLPPPPQTMGSPSMAGGSGGCGGGGLGLGSAHSMGTSLSITPATLTTTGNHLDVPFANNPNLLSPDVLNQRRGSRRPSILPVPDMFTSSSFSIAGNDDGEEGDESDDEIDDEMPWRSPSEKIACLGGHFPQSRTYSLIMSSSEDSYQRGCSFCSATASASAAAVAVAVAAAPAPAPAPAYPSDSAGESGTNADSAAMPSEEYLPQLRRRVMKKSYSCDSECRSVPGMGMGMAMGVGLGGGTLARLAARRRQLQRCSSCSCSTATTTTTPAVAATTAMAAGSGATAFTSSSSVETRRPVRPVWVYDYSCIVKGFPPVSPFIGVSPTLCYLLKEKKPLCCLQLAQVCEHCSYRNAKEYQWQNKTIILAADYASNGIYNFIIPLRAHFRSKTSLNPIILLLERRPDVAFLDALSYFPLVYWMLGSIDCLDDLLRAGITLAESVVVVNKELSNSAEEDSLSDCNTIVAVQNMFKFFPSIKSITELSQSSNMRFMQFRAHDKYALHLSKMEKERGSHISYMFRLPFAAGAVFSASMLDTLLYQAFVKDYVITFVRLLLGIDQAPGSGFLTSMRITKDDMWIRTYGRLYQKLCSTTCEIPIGIYRTQDTSNADTSHYSINLADEARDNHAQQIERAEIANLVRSRMESLNLPTIDYDDVSEKRNHLSYVIINPSCDLKLEEGDLIYLVRPSPFSAQKTFERHNSRRKSNISFCSNINLGATCGPQMPQMNMNMANTAVGAGSRRGSGIAGLNPMQMQSVQTLAGYGSSSQRCSPPMQQIKSNSLSLPDSPTVVGNQRGRSNSLRIDNDILLRRSSSLRQGLPSVGVSHGRRKSSLEEIGISHFTTLMQATNHSNPIKISLNGSIGMENQISLQVTPPEEPTPMLGVPCMLGGGGGGGINPSGAGSSTGGMLGGGSSLAINTADLGPGPSTSSGASGSLQAQDSLGQQSSQVSSPQHLQGTIV
Protein: Cell wall integrity protein scw1 (Strong cell wall protein 1) (O74452)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a negative regulator of cell wall and septum deposition.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12242222}.
Interaction partners:
- Serine/threonine-protein kinase sid2
- Septation initiation network scaffold protein cdc11
- Protein phosphatase PP2A regulatory subunit B
- Start control protein cdc10
- Cell division control protein 7
- Serine/threonine-protein kinase sid1
Sequence:
MFVGSPSAIEKPLSLSSKTKVGDETEFTEDALRGSSLVPTGILNGDDECHALHMSPQAIHSQAGKAESDGLPTYASVEKSTTPIGRLLSNLNGGLASAPPKVGFGFPRYYALRIEDLPRDLTPREFLCTFLFATNVVSVELNPVSVDNEVAHGLAVFSSRDAAASARDTLLSSDVYSACSMIILDNYRKGSQTNLSDETEGSESSVSFNRLSRNHSPTRPLLGNRDLFRRSSNHVSASMPTANHSESAYRHSKTPLGDSTFQAPNNGGSLHSDRLWSSFPVSYPLTLANVLAKDEVGSPTWSPTPSKSSTNLRQDGVPPILRFNSLSINTNVARNYLSSEKGYSAHTQNSSAQSPHPRVFSANSAFSTTSPPPLTPSTSRDYPFSASTISPSTPFSAYSSSHGIHQRIPASTPTNTNPADQNPPCNTIYVGNLPPSTSEEELKVLFSTQVGYKRLCFRTKGNGPMCFVEFENIPYAMEALKNLQGVCLSSSIKGGIRLSFSKNPLGVRSSSSSHNNHNGNVRNLHSGSMNNYNTDSLLNHTGGHNEVHASPSWGNNLMYGK
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (Q59PS6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- N-acetyltransferase domain-containing protein
- Polyamine acetyltransferase
Sequence:
MGQLLSHPIEEKELDYKSYTNLTYCIGSMQGYRMTMEDAHDVKINEHENLAVFGIFDGHGGKNCSQYLAEHLPKLVFTKLNKIASAVYLKQVKDIDLKDVFDILKNSFFKIDKDLSHHANMVNCGSTATVVTIIANYIVVANTGDSRCIVSRNGHAKPLSFDHKPSNMGERVRIENSNGYILNNRINEVLALSRAFGDFKFKLPYLSSSRNKYIKENQKLLGDKLITLPPELFQVTVEPDIMLYDMQKLDSPEFLVIACDGVWDCFKNGQLVKLIRDKLSLGWRLNKIVEYILNDSLTMANNYTGIGFDNMTLIIVAIHKKEGETMDDWYESMKEKILKEKGITR
Protein: Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.2) (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase) (F1QH99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU368115}.
Interaction partners:
- FAD synthase
- Acid phosphatase 2
- Oculocutaneous albinism II.
- ATPase GET3
- Catenin beta-1
- Catenin, beta 2.
- Tartrate-resistant acid phosphatase type 5
- Tartrate-resistant acid phosphatase type 5
- Riboflavin kinase
- Biliverdin reductase B.
Sequence:
MAASSGKSVLFVCLGNICRSPIAEAVFRKMATDSGVVDKWVIDSGATSDWNTGSTPDARGLACLRKHGIETDHRARQVTKDDFMSFDYILCMDESNLRDLNKKASSVKNSKAKIELLGSYDPEKQLIIQDPYYGSDKDFETVYEQCARCCKAFLEQHS
Protein: GH14758p (Q95SM0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLKTLRRRLGIVSQEPSLFEKSIADNIGYGDTSRQVPMQQIIEAAKMANAHEFIMSLPAQYDTVLGSKGTQLSGGQKQRIAIARAMVRNPKILLLDEATSALDFQSERVVQQALDSACSGRTCIVIAHRLSTIQNANVICVIQAGKIVEQGSHSQLLAKNGIYSKLYRCQTKAS
Protein: Protein P [Includes: DNA-directed DNA polymerase (EC 2.7.7.7); RNA-directed DNA polymerase (EC 2.7.7.49); Ribonuclease H (EC 3.1.26.4)] (Q69028)
Organism: Hepatitis B virus genotype C subtype ayr (isolate Human/Japan/Okamoto/-) (HBV-C)
Function: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery.
Interaction partners:
Sequence:
MPLSYQHFRKLLLLDDEAGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPDWKTPSFPHIHLQEDIINRCQQYVGPLTVNEKRRLKLIMPARFYPNLTKYLPLDKGIKPYYPEYAVNHYFKTRHYLHTLWKAGILYKRETTRSASFCGSPYSWEQELQHGRLVFQTSTRHGDESFCSQSSGILSRSPVGPCVRSQLKQSRLGLQPQQGSLARGKSGRSGSIWSRVHPTTRRPFGVEPSGSGHIDNTASSTSSCLHQSAVRKTAYSHLSTSKRQSSSGHAVELHNIPPSSARSQSEGPIFSCWWLQFRNSKPCSDYCLTHIVNLLEDWGPCTEHGEHNIRIPRTPARVTGGVFLVDKNPHNTTESRLVVDFSQFSRGSTHVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLVGSSGLPRYVARLSSTSRNINYQHGTMQNLHDSCSRNLYVSLLLLYKTFGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHLESLFTSITNFLLSLGIHLNPNKTKRWGYSLNFMGYVIGSWGTLPQEHIVQKLKQCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACIQSKQAFTFSPTYKAFLCKQYLNLYPVARQRSGLCQVFADATPTGWGLAIGHRRMRGTFVAPLPIHTAELLAACFARSRSGAKLIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLYRPLLHLPFRPTTGRTSLYAVSPSVPSHLPDRVHFASPLHVAWRPP
Protein: F9K20.7 protein (Ubiquitin-specific protease family C19-related protein) (Q9ZVA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome regulatory subunit
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
- Nucleobase-ascorbate transporter 2
Sequence:
MGSRYASHQLSNGLFVSGRPEQPKEKPPTMSSVAMPYTGGDIKKSGELGKMFDIPTDGTKSRKSGPITGGSSRSGAQSGPVPNATGRMSGNLASAGSNSMKKTNSGPLSKHGEPLKKSSGPQSGGVTRQNSGPIPILPTTGLITSGPITSGPLNSSGAPRKISGPLDYSGSMKTHMPSVVHNQAVTTLAPEDDFSCMKSFPKPVLWLVILIFVMGFLAGGFILGAVHNAILLIVVAVLFTVVAALFIWNISCERRGITDFIARYPDADLRTAKNGQYVKVTGVVTCGNVPLESSFHRVPRCVYTSTCLYEYRGWGSKPANASHRRFTWGLRSAERHVVDFYISDFQSGLRALVKTGNGAKVTPLVDDSVVIDFKPGNEQASPDFVRWLGKKNLTNDDRIMRLKEGYIKEGSTVSVIGVVQRNDNVLMIVPTTEPLAAGWQWSKCTFPASLEGIVLRCEDSSNVDAIPV
Protein: Platelet glycoprotein IX (GP-IX) (GPIX) (Glycoprotein 9) (CD antigen CD42a) (P14770)
Organism: Homo sapiens (Human)
Function: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein Ib beta chain
- Platelet glycoprotein V
- Platelet glycoprotein Ib alpha chain
- von Willebrand factor
- Integrin alpha-IIb
- Tyrosine-protein kinase Lyn
- GTP-binding protein 1
- Integrin beta-3
- Platelet glycoprotein VI
- Platelet glycoprotein 4
Sequence:
MPAWGALFLLWATAEATKDCPSPCTCRALETMGLWVDCRGHGLTALPALPARTRHLLLANNSLQSVPPGAFDHLPQLQTLDVTQNPWHCDCSLTYLRLWLEDRTPEALLQVRCASPSLAAHGPLGRLTGYQLGSCGWQLQASWVRPGVLWDVALVAVAALGLALLAGLLCATTEALD
Protein: Ras-related protein Rab-3B (EC 3.6.5.2) (P20337)
Organism: Homo sapiens (Human)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q9CZT8}. Note=Colocalizes with GAS8/DRC4 in the Golgi apparatus. {ECO:0000250|UniProtKB:Q9CZT8}.
Interaction partners:
- Polymeric immunoglobulin receptor
- Rab15 effector protein
- Rabphilin-3A
- Ras-related protein Rab-3A
Sequence:
MASVTDGKTGVKDASDQNFDYMFKLLIIGNSSVGKTSFLFRYADDTFTPAFVSTVGIDFKVKTVYRHEKRVKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWATQIKTYSWDNAQVILVGNKCDMEEERVVPTEKGQLLAEQLGFDFFEASAKENISVRQAFERLVDAICDKMSDSLDTDPSMLGSSKNTRLSDTPPLLQQNCSC
Protein: Protein transport protein YOS1 (YIP one suppressor protein 1) (Q3E834)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein transport between endoplasmic reticulum and Golgi apparatus.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15659647}; Multi-pass membrane protein {ECO:0000269|PubMed:15659647}. Golgi apparatus membrane {ECO:0000269|PubMed:15659647}; Multi-pass membrane protein {ECO:0000269|PubMed:15659647}.
Interaction partners:
- Protein transport protein YIP1
- Protein transport protein YIF1
Sequence:
MVLFGLGRLFYVILLLINAVAVLSEERFLRRIGLGRSNDETPVFGQDQNTTKSKVVQLIGAVQTLLRIPLIGINILVIVYELLLG
Protein: Adenylate cyclase type 3 (EC 4.6.1.1) (Q9V9R3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ionotropic receptor 75a
- Odorant receptor 35a
- Ionotropic receptor 75a
Sequence:
MEANLENGQKTIASTSKSHSQRQTTSRRRQNDSDVAGGVGITGGGVVILPQHVLNELYHNYSIKQRRSGLKWFVFAAALFNIWTIGIPWDQSAPTRVINCCMLLAYLALTALLHIGRRSDKPALRRFHQILLIIVPRALWLLSILHFTVYVILQPSFSPRDLLGWAILLNFLVYVTLPLQLIFLGLSIGCITYFICLSLPVGYSHWDSLLSNQLAANAVLIATAALIGLLYYFMGEAKQKRAFLEAKKSLEVKMVIEEQSAEQERLLLSVLPKHVAIKMREDLGSSSSEAFKKIYMSRHENVSILYADIVGFTAISSTYSAQDLVKMLNELFARFDRLAEKYQQLRIKILGDCYYCISGAPDERPDHAVLCVHMGLSMVKAIKYVQQKANSPVDMRVGIHTGAVLAGILGQRQWQFDVYSKDVELANKMESSGKAGRVHISDKTLAFLNGEFEVEAAFGEKREELLRIAGLKTYFITKVVKAFASPCAKKINETQAEIAHPNPNGSTTDIVSDEDDNDATLDDEELLAQNSVSNGHQIGIAVTADEEEQVKLENFKQRLKDELVTRDGHENLTKDTNIFLRFKNPQLEQLYAVYREPYSSLPLLAALLVQCIDVLYSYLVLPRSTLHFINIAAPLVPIAMLVVISLAESFSGMLPKFFVDVSKRFNDITFVRELAAIIIALTIGFSNVIDMFFFVTFVRTEHIVSESEFNVTASLESDINLVVEGMVTAEHLLPASFVEQMRDAVPTERVLYPSYLSNFGVLILIAIAVIAQLTHLTKILLLLSIAALHCYFNIFIMQDLYALEDDFEHQPIISTRYAASGLLLVAALALSTLARHMDHEDRVIFKWKTEVAEQKETANDMRQRNEALVYNVLPVHVAEHFMKNTKRSHDDLYSQSYAEVGVLFASMPNFSDFYSEETVNNQGLECLRFLNEVISDFDALLELPQFQDIIKIKTIGSTYMAASGINVQRTVRNDAPITERWSHLAILVEFALELKHALQSINEQSFNHFVLKMGINHGPITAGVIGARKPHYDIWGNTVNVASRMESTGKAGAIQVTEETCNILRLFGYTFLQRGLVAVKGKGQLMTFYLQGKSQSSAEPVASGVVVLNGQDSSAVESTSELEASDIKMPLLKMNGPEQSLEIDQDRSLRNDSAGQESVAECQSLLE
Protein: Tryptamine benzoyltransferase 1 (OsTBT1) (EC 2.3.1.-) (Q2R0K3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from benzoyl-CoA to tryptamine, to produce benzoyl tryptamine. Serotonin and tyramine serve as acyl acceptors in vitro. Can use p-coumaroyl-CoA, and to a lesser extent caffeoyl-CoA, as acyl donors.
Interaction partners:
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- 4-coumarate--CoA ligase
Sequence:
MEITSSAMLKTTTTPPHPLAGEKVPLSAFDRAAFDVFVPLVFAYRAPAPSSEAVKEGLRVAVAAYPLVSGRIAVDGQGRRRRRRVLHVNNEGVLVLDATVEVDLDAVLAANVATDLYPALPEHSFGAALLQVQLTRFGCGGLVVGLIGHHHVFDGHSMSTFCATWARAVRDSEAFIVPSPSLDRAITGVPRSPPAPVFDHRSIEFKVGNKSSDSSGAAAAAAVEKIANIGVRFTAKFVAELKARVGGRCSTFECVLAHAWKKITAARGLKPEEFTRVRVAVNCRRRANPPAPADLFGNMVLWAFPRLQVRRLLSSSYRDVVGAIRAAVARVDAEYIQSFVDYVEVADARGEELAATAAEPGETLCPDLEVDSWLGFRFHEMDLGTGPPAAVLSPDLPIEGLMILVPVGGDGGGVDLFVALADDHAQAFEQICYSLEEHAMIHSHL
Protein: Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Q55AW9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P) (By similarity). Has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32368}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32368}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inositol 5-phosphatase 4
- 1-phosphatidylinositol 4-kinase
- phosphoinositide 5-phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- Phosphatidylinositol 3-kinase VPS34-like
- Probable phosphatidylinositol phosphate kinase DDB_G0267588
- PIPK domain-containing protein
- 1-phosphatidylinositol-5-phosphate 4-kinase
Sequence:
MNIELINTNERFILINNGNKDKSLNIDKHSVKASISVGVPKNNEKVLTRIENVKGIIGCIQLVSGHYLMIFKEHNHVATVTGKKIYQMKDVELIPFFPNQQSLVSIPDQDAEEQHLSMIRWLLSSENFYFSYDYDFTLTLQRQYSTTTTTTSGSSLGERCDSRFFWNEKYVTILSKEHGLGDWILPITMGFVESKTLGGTCQFTLISRRNLNRSGTRYNVRGIDKKGNVANNVETEQIIEIKENTFTSFVQVRGSIPLLWSQFPTLKYKPSVKFYGDEKENSQALEQHFKQLHQLYGSTTVVNLIDRKGAELKLGEAYEERVKSLKDVHYVWFDFHSICKGMRYDKLSILMDQLKDDLKQYGFFFVEDGKIVQKQQGVFRTNCIDNLDRTNVVQSLITRHSLENQMASVLNKQIPSTTFKGDQFEYVFKNIWADHGDAISTQYSGTGALKNDFTRTGKRNFQGVLRDGENSVKRYYLNNFKDGFRQDSYFLFTNPSVDLTTAKQHESKPPSPLIWIFSFVFAAIFLANLYLPSATSSIGGFISQTTVLVGSVFFALKLAMKYQASIVDKPTLFKLDSIYKN
Protein: Gamma-adducin (Adducin-like protein 70) (Q9QYB5)
Organism: Mus musculus (Mouse)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping. Binds to calmodulin (By similarity). Involved in myogenic reactivity of the renal afferent arteriole (Af-art), renal interlobular arteries and middle cerebral artery (MCA) to increased perfusion pressure. Involved in regulation of potassium channels in the vascular smooth muscle cells (VSMCs) of the Af-art and MCA ex vivo. Involved in regulation of glomerular capillary pressure, glomerular filtration rate (GFR) and glomerular nephrin expression in response to hypertension. Involved in renal blood flow (RBF) autoregulation. Plays a role in podocyte structure and function. Regulates globular monomer actin (G-actin) and filamentous polymer actin (F-actin) ratios in the primary podocytes affecting actin cytoskeleton organization. Regulates expression of synaptopodin, RhoA, Rac1 and CDC42 in the renal cortex and the primary podocytes. Regulates expression of nephrin in the glomeruli and in the primary podocytes, expression of nephrin and podocinin in the renal cortex, and expression of focal adhesion proteins integrin alpha-3 and integrin beta-1 in the glomeruli. Involved in cell migration and cell adhesion of podocytes, and in podocyte foot process effacement. Regulates expression of profibrotics markers MMP2, MMP9, TGF beta-1, tubular tight junction protein E-cadherin, and mesenchymal markers vimentin and alpha-SMA (By similarity). Promotes the growth of neurites.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62847}. Cell membrane {ECO:0000250|UniProtKB:Q62847}; Peripheral membrane protein; Cytoplasmic side. Cytoplasm {ECO:0000269|PubMed:33992672}. Note=Full-length protein and the cleavage fragment 358-706 localize mainly to the cytoplasm, while cleavage fragment 1-357 translocates from the cytoplasm to the nucleus. {ECO:0000269|PubMed:33992672}.
Interaction partners:
- Protein 4.1
- Dematin
- Ankyrin-2
- Alpha-adducin
- Ankyrin-1
- Ankyrin-3
- Tropomodulin-3
- Tropomodulin-1
- Tropomodulin-4
- Tropomodulin-2
Sequence:
MSSDTSPAVVTTPPPPSMPHKERYFDRINESDPEYLRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPSGLLALQQIADYIVTSSFSGFSSPSLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTDLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGVNMASHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLVREKPRHKSDVEIPATVTAFSFEDDSAPLSPLKFMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSSGTPIKIEDPNQFVPLNTNPTEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFDDDDQGPPAPPNPFSHLLEGELEEYTKTIERKQQGLDDAEQGSLSDDAASVSQIQSQTQSPQSVPERLEENHELFSKSFTSMDAPVMIMNGKDEMHDVEDELAQRVSRLTTSTTIENIEITIKSPERTEEVLSPDGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
Protein: Lamin tail domain-containing protein 2 (Q8IXW0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRWLRPAGRRREQESVSGHLGPPAGAPAAPETPTCLPDTTPHPAPVVCSADPQLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEVAGLPPKRSSHSQEKLLQNQVQKLIQELKEQKERAQWEKEHLEERLLQTTRTLQEMEAELQNLQKSCLLQLARSSWVGRMLRSQTGSVEVVTAETLMDPSDLSENIQAPTGEGFRLEDVDWNSVARRYPNLFTNMEPSSKQKQPRPWPQLDTGSPESSGKHSERHHKTVEWGSLPCLNTSSSGGADSDSSSCRPGLPSFVQVIGHPPRDHRASSEQALVQAGSYSRDSEDLQKTHSPRHGEPVLSPQPCTDPDHWSPELLQSPTGLKIVAVSCREKFVRIFNPSQESTADLSGMVLKQLVRGFPERLYRFPPGTLLAPRHHVTVWGEATRSAKKPLRASSSREPVPLLSIRGCATLLLSPKGEVLSEHRIPRRETPAPRVFADGTDLSIDRFPLPEAGPGADTRKPPRPPRPLRKGRVREPRVSRRRPGTRGLLPPVSSGKLFHAREGPARPENPEIPAPQHLPAIPGDPTLPSPPAEAGLGLEDCRLQKEHRVRVCRKSVDRSCPLVALSVQNTAESRFGFRFLSCLPVTADTCRGA
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 (Complex I-15 kDa) (CI-15 kDa) (NADH-ubiquinone oxidoreductase 15 kDa subunit) (O43920)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}. Mitochondrion intermembrane space {ECO:0000305}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 6
Sequence:
MPFLDIQKRFGLNIDRWLTIQSGEQPYKMAGRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFVECLLRQKTMRRAGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP
Protein: Ribosomal lysine N-methyltransferase 5 (EC 2.1.1.-) (Q12367)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L1 (RPL1A and RPL1B) at 'Lys-46'.
Interaction partners:
- Ribosomal lysine N-methyltransferase 2
- Ribosomal lysine N-methyltransferase 1
- Ribosomal lysine N-methyltransferase 3
- Protein-lysine N-methyltransferase EFM2
- Histidine protein methyltransferase 1
- Carnosine N-methyltransferase
- Uncharacterized protein YMR209C
- Protein-lysine N-methyltransferase EFM4
- Ribosomal lysine N-methyltransferase 4
- Protein arginine N-methyltransferase 2
Sequence:
MAFKLWLLDEETIYEHVFERYTQLEGQSGKLAQDLGIQDRRGGVLEITFEPSGLEGGRKKKRVRRRNKASSVEEDQNVAVDSYHVSVGQSISSLRSSRDNGNSTTGYVLWSTTPFFINWLLYSTSAAPFRLGSQVEVTCGSSCEGHKLELPRLVDLTGADRGKRGILELGAGISGILPVILGNFVDTYVSTDQKGILNKLKDNIMENLSQLTRKRCISRSLRLELPTVEPVGDADITAASLPSKSTLHLEVAALDWEKINLQDKKTHSLHPELSLIGETCSSVYVIAMDVIYNEYLIDPFLKTLKQLKHWLQTTYNLQFHVLVGIHLRSQEVTTLFLEKAIIEYDFTVYDIVDQVIQESRFNFYLIT
Protein: RAS protein activator like 2 (Q0VAV5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFTGLESDSPLPPEDLDAVVPVSGAVAGGMLDRILLESVCQQQSWVRVFDVKGPPTHRLSCGQSPYTETTSWERKYCILTDSQLVLLNKEKEMPVEGQDQQTDSTKGRCLRRTVSVPSEGQFPEYPQEGTTKLEVPAERSPRRRSISGTSTSEKPNSMDTANTSPFKVPGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSLRNADDRSRGLPKLKESRSHGSLLSPCSAVECLDLGRGEPVSVKPLHSSILGQDFCFEVTYLSGSKCFSCSSASERDKWMENLRRTVQPNKDNCRRAENVLRLWIIEAKDLAPKKKYFCELCLDDTLFARTTSKTKADNIFWGEHFEFYSLPPLHSITVHIYKDVEKKKKKDKNNYVGLVNIPTASVTGRQFVEKWYPVSTPTPNKGKTGGPSIRIKSRFQTITILPMEQYKEFAEFITSNYTMLCSVLEPVISVRNKEELACALVHILQSTGRAKDFLTDLVMSEVDRCGEHDVLIFRENTIATKSIEEYLKLVGQQYLHDALGEFIKALYESDENCEVDPSKCSSSELMDHQSNLKMCCELAFCKIINSYCVFPRELKEVFASWKQQCLNRGKQDISERLISASLFLRFLCPAIMSPSLFNLMQEYPDDRTSRTLTLIAKVIQNLANFAKFGNKEEYMAFMNDFLEHEWGGMKRFLLEISNPDTISNTPGFDGYIDLGRELSVLHSLLWEVVSQLDKGENSFLQATVAKLGPLPRVLADITKSLTNPTPIQQQLRRFAEHSSSPNVSGSLSSGLQRICEDPTDSDLHKLKSPSQDNTDSYFRGKTLLLVQQASSQSMTYSEKDEKENSLPNGRSISLMDLQDTHAAQAEHASVMLDVPMRLAGSQLSITQVASIKQLRETQSTPQSAPQVRRPLHPALNQPGSLQPLSFQNPVYHLNNPVPAMPKASADSSLENLSTASSRSQSNSEDFKLSGPSNSSMEDFTKRSSHSEDFSRRHTVPDRHIPLALPRQNSTGQSQIRKLDHSGLGARAKAPPSLPHSASLRSTGSMSVASAALMAEPVQNGSRSRQQSSSSRESPVPKVRAIQRQQTQQVQSPVDSATMSPVERTAAWVLNNGQYEEDVEETEQNQDEAKHAEKYEQEITKLKERLRVSSRRLEEYERRLLVQEQQMQKLLLEYKARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVIDAKQKIIDAQEKRIVSLDSANTRLMSALTQVKERYSMQVRNGISPTNPTKLSITENGEFKNSSC