wanglab/gogpt-training-data huggingface dataset:
Protein: Small proline-rich protein 2A1 (small proline-rich protein 2A) (Q9CQK8)
Organism: Mus musculus (Mouse)
Function: Gut bactericidal protein that selectively kills Gram-positive bacteria by binding to negatively charged lipids on bacterial membranes, leading to bacterial membrane permeabilization and disruption. Specifically binds lipids bearing negatively charged headgroups, such as phosphatidic acid, phosphatidylserine (PS), cardiolipin (CL), and phosphatidylinositol phosphates, but not to zwitterionic or neutral lipids (By similarity). Induced by type-2 cytokines in response to helminth infection and is required to protect against helminth-induced bacterial invasion of intestinal tissue. May also be involved in the development of the cornified envelope of squamous epithelia; however, additional evidences are required to confirm this result in vivo (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:34735226}. Secreted, extracellular space {ECO:0000269|PubMed:34735226}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:34735226}. Note=Present in intestinal secretory epithelial cells and is secreted into the intestinal lumen. {ECO:0000269|PubMed:34735226}.
Interaction partners:
Sequence:
MSYYQQQCNQPCRPPPVCPPPKCPEPCPPQVWPGPCRPVMCFEPCLPSVWPGPCRPVVCYEQCPPQPWQSTCPPVQFPPCQQK
Protein: UPF0053 inner membrane protein YgdQ (P67127)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized lipoprotein YgdR
- Magnesium and cobalt efflux protein CorC
- Protein tas
- DNA mismatch repair protein MutH
- Lysophospholipid transporter LplT
Sequence:
MLFAWITDPNAWLALGTLTLLEIVLGIDNIIFLSLVVAKLPTAQRAHARRLGLAGAMVMRLALLASIAWVTRLTNPLFTIFSQEISARDLILLLGGLFLIWKASKEIHESIEGEEEGLKTRVSSFLGAIVQIMLLDIIFSLDSVITAVGLSDHLFIMMAAVVIAVGVMMFAARSIGDFVERHPSVKMLALSFLILVGFTLILESFDIHVPKGYIYFAMFFSIAVESLNLIRNKKNPL
Protein: Glia maturation factor (Q9VJL6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inhibits Arp2/3-mediated actin nucleation. Together with flr, promotes Arp2/3-nucleated actin filament array disassembly. Promotes debranching. Regulates lamellipodial protrusion dynamics possibly by facilitating lamellipodial retraction. In egg chambers, enhances the retraction dynamics of cellular extensions in border cells and thus together with flr plays an important role in directional migration of border cell clusters.
Subcellular location: Cell projection, lamellipodium {ECO:0000269|PubMed:25308079}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25308079}. Nucleus {ECO:0000269|PubMed:25308079}. Cytoplasm, cell cortex {ECO:0000269|PubMed:25308079}. Note=Colocalizes with F-actin and Arp2/3-nucleated actin arrays. {ECO:0000269|PubMed:25308079}.
Interaction partners:
- Actin-related protein 2
- Twinfilin
- Actin-related protein 2/3 complex subunit
- Actin-related protein 3
- Drebrin-like protein
- Actin-related protein 2/3 complex subunit 2
- IP01243p
- Cofilin/actin-depolymerizing factor homolog
- IP04855p
- Actin-interacting protein 1
Sequence:
MSDNQICDISNEVLEELKKFRFSKSKNNAALILKVDREKQTVVLDEFIDDISVDELQDTLPGHQPRYVIYTYKMVHDDQRISYPMCFIFYTPRDSQIELQMMYACTKSALQREVDLTRVYEIRELDELTEEWLKAKLK
Protein: DNA replication licensing factor mcm7 (EC 3.6.4.12) (Minichromosome maintenance protein 7) (O75001)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Required for the progression of S phase.
Subcellular location: Nucleus {ECO:0000269|PubMed:11606526}.
Interaction partners:
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm5
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- Cell division control protein 18
- Cell division cycle protein cdt1
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm2
- DNA replication complex GINS protein psf3
Sequence:
MALPTIDLKIPEYEECQHKITDFLSHFKQEQVQDGQQNQDISMSDAGDEPFLKSKYMDILQKISNRESNVINVDLNDLYEFDPSDTQLLHNIESNAKRFVELFSQCADALMPPPTVEINYRNEVLDVIMQQRVQRNENIDPEHKGFPPELTRGYDLYFRPVTRNKKPFSVRDLRGENLGSLLTVRGIVTRTSDVKPSLTVNAYTCDRCGYEVFQEIRQKTFLPMSECPSDECKKNDAKGQLFMSTRASKFLPFQEVKIQELTNQVPIGHIPRSLTVHLYGAITRSVNPGDIVDISGIFLPTPYTGFRAMRAGLLTDTYLECHYVSQIIKNYTNIEKTPQSEAAIAELNQGGNVYEKLAKSIAPEIYGHEDVKKALLLLLVGGVTKELGDGMRIRGDINICLTGDPGVAKSQLLKYISKVAPRGVYTTGRGSSGVGLTAAVMRDPVTDEMVLEGGALVLADNGICCIDEFDKMDESDRTAIHEVMEQQTISISKAGITTTLNARTSILAAANPLYGRYNPKVAPIHNINLPAALLSRFDILFLILDTPSRETDEHLAQHVTYVHMHNEQPKMDFEPLDPNMIRHYISSARQYRPVVPKDVCDYVTGAYVQLRQNQKRDEANERQFAHTTPRTLLAILRMGQALARLRFSNRVEIGDVDEALRLMSVSKSSLYDDLDPSSHDTTITSKIYKIIRDMLNSIPDVEGNERSLTLRAIRERVLAKGFTEDHLINTIQEYTDLGVLLTTNNGQTIMFLDPDLHMEN
Protein: Csr1p (A0A1D8PM73)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Low-affinity Zn
- Zinc-regulated transporter 1
- pH-regulated antigen PRA1
Sequence:
MEPISNQPNFNFSCPALDDLDFCKDVFCNDLDDCFYLNCDDNENSNTCDVNCCDSQVDEICCTNDKCLEPKSEQPPSCEKSEHLECCDDPHCESYNVCHSDLGDSSSVVCTDPNCSEIDTCCSSLPQPTLPSHSENNLCQPQLSKRPIFEDLITNVHLSCKQTQAEEINSVYPPKKKIKRESDFDIHFPHECHQDYKNPFTATATTNHQLHQSCFHTTIPDRKNTSLEYDEKLMSDFDFVIQFNNFNQLLNTATKHEQQGQHEQQKQQNQFVKETTDFNQVSTNRPTSYSCQWENCFKRLNNNTFLNHVIEDHLEKEEIVKSENSNYQCEWNECNFTDNDFNSLINHLKSHQPSNSVETTGCSSLLNNVTNNYALTPLSCTLSNDASPVVALQSPQAPDLNITSVKIVPKNKRKSCKPKVKKEDQEMDLEHTCNWQIGTDDNGDPIYCNIKHQSPGDLHSHLLDVHIGSGKHEYHCCWRGCERHNGKVFTQKQKLIRHIHIHTNFKPCKCDICGASFAVESVLQQHYRVHSGEKPFKCPICDKTFATSSSLSIHTRVHTGERPLVCKWPGCNKRFSESSNLAKHMRIHTKKFNCEACGQSFDKKGVFNRHVLEHSVEK
Protein: Androgen receptor (Q9I8F5)
Organism: Pimephales promelas (Fathead minnow)
Interaction partners:
Sequence:
MEACESPEAVFHGSYQSLFQNVRVKRANNESLDISSSKKCGFLQETASREMRLSKLSPRRGILRSPEKECESTISVIQLAASRIHFLKSSTESKSDSSLSSSGSGLADATESSDSRAGFLRGAESGQKGYGAAEVHKHELGSGRDASVASCSRACSSGITISETARELCKAVSVSLGLAMESSELGEVGPHHAPPLTTESSSDEMYMPLLDCSVSEPGAGAKDREYALAMGQRDRGLELRGRDKVLGMFKSSDLVQLAGDVTTSQYSNASKSHLTSALQEVHEFASMSGDIANPSSEGTAASDMDATHAASCQFEQLLPASMAHFVHPEFENGPSQSFAKPSAMSGEFTENYANQYNVKIKAEMMPRDLNGTWAYPHRYADDSNGQYGPPKQRTTYATDHETPFISNPYEYGQSGSLVPRERPPPEQWYPVGMLGRPPYPNVPCVKNEVGEWLDVTSLTDGRFDAGRSDIFPMEFFLPPQRTCLICSDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKLRRKNCPSCRLRRCFEAGMTLGARKLRKIGQVKGPDEVGSVQGPSESAQCLSPKPCLTFHSQLIFLNILEAIEPEVVNAGHDHAQPDSAAALLTSLNELGERQLVKVVKWAKGLPGFRNLHVDDQMTVIQHTWMGVMVFALGWRSYKNANARMLYFAPDLVFNDRRMHISSMYEHCIQMKHLSQEFVLLQVTQEEFLCMKALLLFSIIPVEGLKSQKYFDELRLTYINELDRLINYGRKSNCAMRFQQLTRMMDSLQPIVQKLHQFTFDLFVQARSLPTKVSFPEMIAEIISVQVPKILAGLSKPILFHK
Protein: DnaJ homolog subfamily C member 7 (K7EJV7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRAL
Protein: Sulfotransferase 2B1 (EC 2.8.2.2) (Alcohol sulfotransferase) (Hydroxysteroid sulfotransferase 2) (Sulfotransferase family 2B member 1) (Sulfotransferase family cytosolic 2B member 1) (ST2B1) (O00204)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol. Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648}. Microsome {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Nucleus {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Note=Phosphorylation of Ser-348 is required for translocation to the nucleus. {ECO:0000269|PubMed:21855633}.
Interaction partners:
- Cytochrome P450 7A1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Steryl-sulfatase
- Aldo-keto reductase family 1 member C3
- Cytochrome P450 3A7
- Cytochrome P450 7B1
- Cytochrome P450 3A5
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cholesterol side-chain cleavage enzyme, mitochondrial
Sequence:
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS
Protein: Mitotic spindle checkpoint component mad2 (O14417)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. It interacts with the anaphase promoting complex/cyclosome (APC/C) thereby inhibiting APC/C-dependent proteolysis, a step required for exit from mitosis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Spindle assembly checkpoint serine/threonine-protein kinase bub1
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 4
- Spindle assembly checkpoint component mad1
- WD repeat-containing protein slp1
- Spindle assembly checkpoint protein bub3
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
Sequence:
MSSVPIRTNFSLKGSSKLVSEFFEYAVNSILFQRGIYPAEDFKVVRKYGLNMLVSVDEEVKTYIRKIVSQLHKWMFAKKIQKLILVITSKCSGEDLERWQFNVEMVDTADQFQNIGNKEDELRVQKEIQALIRQITATVTFLPQLEEQCTFNVLVYADKDSEVPTDWVDSDPRILRDAEQVQLRSFSTSMHKIDCQVAYRVNP
Protein: Nucleolar protein 11 (Q9H8H0)
Organism: Homo sapiens (Human)
Function: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22916032}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 4 homolog
- WD repeat-containing protein 43
- WD repeat-containing protein 75
- U3 small nucleolar RNA-associated protein 15 homolog
- HEAT repeat-containing protein 1
- Small subunit processome component 20 homolog
- Ribosomal RNA small subunit methyltransferase NEP1
- Something about silencing protein 10
- Nucleolar complex protein 4 homolog
- DDB1- and CUL4-associated factor 13
Sequence:
MAALEEEFTLSSVVLSAGPEGLLGVEQSDKTDQFLVTDSGRTVILYKVSDQKPLGSWSVKQGQIITCPAVCNFQTGEYVVVHDNKVLRIWNNEDVNLDKVFKATLSAEVYRILSVQGTEPLVLFKEGAVRGLEALLADPQQKIETVISDEEVIKWTKFFVVFRHPVLIFITEKHGNYFAYVQMFNSRILTKYTLLLGQDENSVIKSFTASVDRKFISLMSLSSDGCIYETLIPIRPADPEKNQSLVKSLLLKAVVSGNARNGVALTALDQDHVAVLGSPLAASKECLSVWNIKFQTLQTSKELPQGTSGQLWYYGEHLFMLHGKSLTVIPYKCEVSSLAGALGKLKHSQDPGTHVVSHFVNWETPQGCGLGFQNSEQSRRILRRRKIEVSLQPEVPPSKQLLSTIMKDSEKHIEVEVRKFLALKQTPDFHTVIGDTVTGLLERCKAEPSFYPRNCLMQLIQTHVLSYSLCPDLMEIALKKKDVQLLQLCLQQFPDIPESVTCACLKIFLSIGDDSLQETDVNMESVFDYSINSVHDEKMEEQTEILQNGFNPEEDKCNNCDQELNKKPQDETKESTSCPVVQKRAALLNAILHSAYSETFLLPHLKDIPAQHITLFLKYLYFLYLKCSENATMTLPGIHPPTLNQIMDWICLLLDANFTVVVMMPEAKRLLINLYKLVKSQISVYSELNKIEVSFRELQKLNQEKNNRGLYSIEVLELF
Protein: Chloride anion exchanger (Down-regulated in adenoma) (Protein DRA) (Solute carrier family 26 member 3) (Q924C9)
Organism: Rattus norvegicus (Rat)
Function: Mediates chloride-bicarbonate exchange with a chloride bicarbonate stoichiometry of 2:1 in the intestinal epithelia (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P40879}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q9WVC8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P40879}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in sperm membranes. Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). {ECO:0000250|UniProtKB:Q9WVC8}.
Interaction partners:
- Na
- Na
- Cystic fibrosis transmembrane conductance regulator
- Na
- Sodium/hydrogen exchanger 3
- Carbonic anhydrase 2
- Sodium/hydrogen exchanger 2
Sequence:
MIEAIGNQYVVARPVYSTKAFGEEFKKTYGHHKTFLDHLKGCCSCSSQKAKKIALSLFPIASWLPAYKIKEWLLSDIVSGISTGLVAVLQGLAFALLVNIPPAYGLYAAFFPVITYFFLGTSRHISVGPFPVLSMMVGVVVTRVASGSDTSPALSSSSAENDSMIEEKVMVAASVTVLSGIIQLLLGVLQIGFVVIYLSESLISGFTTAAAIHVLVSQLKFMLQLTVPAHSDPFSIFKVLESVFSQIQKTNIADLVTSVIILVVVFVVKEINQRYRSKLPVPIPIELIMTVIATGISYGCNFEQRFGVAVVGNMSLGFQPPITPSVEVFQDTIGDCFGIAIVGFAVAFSVASVYSLKYDYPIDGNQELIALGVSNIFTGAFKGFAGSTALSRSGVQESTGGKTQVAGLLSAVIVLIVIVAIGFLLQPLQKSVLAALALGNLKGMLMQFAEIGRLWKKDKYDCLIWIMTFIFAIVLGLGLGLAASVAFQLLTIVFRTQFPKCSTLANVGRSNIYKNKKNYADVYEPEGVKIFRCPSPIYFANIGFFKQKLIDAVGFNPLRILRKRNKALKKIRKLQKQGLIQVTPKGFICTSDGFKDSDEELDNNQIEELDQPINTTDLPFEIDWNADLPLNITIPKISLHSLILDFSAVSFLDISSMRGLRTILQEFIRIKVDVYIVGTDDDFIDKLARCEFFDDEVTDSIFFLTIHDAILHIWMKKDYSTSKFNSSQEKERKFDFTINTNGGLRNRECQVPVETKF
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2 (B17.2-like) (B17.2L) (Mimitin) (Myc-induced mitochondrial protein) (MMTN) (NDUFA12-like protein) (Q8N183)
Organism: Homo sapiens (Human)
Function: Acts as a molecular chaperone for mitochondrial complex I assembly. 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 {ECO:0000269|PubMed:15774466}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 4
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
Sequence:
MGWSQDLFRALWRSLSREVKEHVGTDQFGNKYYYIPQYKNWRGQTIREKRIVEAANKKEVDYEAGDIPTEWEAWIRRTRKTPPTMEEILKNEKHREEIKIKSQDFYEKEKLLSKETSEELLPPPVQTQIKGHASAPYFGKEEPSVAPSSTGKTFQPGSWMPRDGKSHNQ
Protein: Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1) (Lectomedin-2) (O94910)
Organism: Homo sapiens (Human)
Function: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:35907405}; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
Interaction partners:
- Teneurin-2
- Teneurin-4
- Teneurin-1
- Teneurin-3
- Netrin receptor UNC5A
- Netrin receptor UNC5C
- Netrin receptor UNC5D
- UNC5C-like protein
- CMP-sialic acid transporter
- Vascular endothelial growth factor B
Sequence:
MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELVFPQEEYPRKNSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGPGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEDKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGGGEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL
Protein: 5'-deoxynucleotidase YfbR (EC 3.1.3.89) (5'-deoxyribonucleotidase) (Nucleoside 5'-monophosphate phosphohydrolase) (P76491)
Organism: Escherichia coli (strain K12)
Function: Essential component of the deoxycytidine triphosphate (dCTP) pathway for de novo synthesis of thymidylate. Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates (dAMP, dGMP, dTMP, dUMP, dIMP and dCMP) and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01100, ECO:0000305}.
Interaction partners:
- 5'/3'-nucleotidase SurE
- Pyrimidine 5'-nucleotidase YjjG
- GMP/IMP nucleotidase YrfG
- Protein UshA
- Cytidylate kinase
- Purine nucleoside phosphorylase DeoD-type
- Thymidylate kinase
- Thymidine phosphorylase
- Uridine phosphorylase
- Thymidine kinase
Sequence:
MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEIFVPSFHLSLDEISQDSPL
Protein: Protein Wnt (Q3C2H6)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
- Porcupine O-acyltransferase.
- Low-density lipoprotein receptor-related protein
- Wnt inhibitory factor 1
- Notum, palmitoleoyl-protein carboxylesterase.
- Frizzled-1
- Frizzled-4
- Cerberus
- Frizzled-3
- Secreted frizzled-related protein 1
- Secreted frizzled-related protein 2
Sequence:
MLPRSRTQLGLFFILLCPANIIGLWWAVGSPLVMDPNSICRKTKRLAGKQAELCQLEPEIVQEVAKGTKLGVRECQYQFRFRRWNCTSHSKYFGKILQQDIRETAFVYAITAAGVSHAITQACSMGELLQCGCELTRSRAPPSPTAGPGTEGTAWEWGGCGDDVQFGYEKSQQFMDAKSKKGKNDIRALIDLHNNEAGRLAVRSYMRTECKCHGLSGSCTLRTCWRKMPHFREVGDRLLERFNGAFKVMGGNDGKTLIPVGDNIKPPDKQDLIYSADSPDFCSANRKTGSLGTRGRVCNSTAMDTSGCDLLCCGRGHRDETVVLEENCLCRFHWCCVVQCRKCSVRQELSLCI
Protein: Rab5-prov protein (Q7T0S5)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MASRGTSARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTETFARAKNWVKELQRQASPNIVIALSGNKADLSSKRAVDFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNAQSTTGRNRGVDLQENNPPSRSQCCN
Protein: Tissue-resident T-cell transcription regulator protein ZNF683 (Homolog of Blimp-1 in T-cell) (Hobit) (Zinc finger protein 683) (I7HJS4)
Organism: Mus musculus (Mouse)
Function: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T-cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T-cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection. Also plays a role in the differentiation of both thymic and peripheral NKT cells. Negatively regulates the accumulation of interferon-gamma (IFN-gamma) in NKT cells at steady state or after antigenic stimulation. Positively regulates granzyme B production in NKT cells after innate stimulation. Associates with the transcriptional repressor PRDM1/BLIMP1 to chromatin at gene promoter regions.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHLRVHSGERPFQCALCQKRFTQLAHLQKHHLVHTGERPHQCQVCHKRFSSSSNLKTHLRLHSGAKPSQCGLCPSYLTPNVYPKLHHRLRAPQLRGLTHTHLPLASLTCLAQWHQGALDLVEKKMGWTVDKVSSESKGKQG
Protein: Ingression protein fic1 (Cdc15-interacting C2 domain-containing protein 1) (O94701)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the ingression of the plasma membrane during cytokinesis, leading to the separation of the daughter cells. Unlike its S.cerevisiae ortholog INN1, it does not play an essential role, probably because the actinomyosin ring is connected to the cell cortex by many more proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum and the cell tip. {ECO:0000269|PubMed:19139265}.
Interaction partners:
- Cell division control protein 15
- Septation protein imp2
- LIM domain-containing protein C4F6.12
- Probable Rho-GTPase-activating protein 7
- cytokinesis protein 3
- Myosin type-2 heavy chain 2
- Cell division control protein 12
- Myosin regulatory light chain 1
- Myosin type-2 heavy chain 1
- Rho1 guanine nucleotide exchange factor 3
Sequence:
MSKNPLGTLVVRIWKAKNLPNKALVGKQSPYCVCRVGEVVKRTQTDKRSGQEPSWNAVLEFNIPSESYHIMKITVFHEGFRKHPHLIGDTVLSFEKAMKEELQSEWYELKNEFQFAGELSVQFKFIPTDPLYFDRASSKPVLQFPYSSVAALTPVPKKPSKPSKPRKKVPVSHPLPPTPPSREEHVSVPRESSLFTYEDDPLPSFPSPYMVDDYYTQDVFVSDNVNDYSYGVQNPTNPRLSVEDYDANHSSLPPVPPPHLILPTASSSQIFH