wanglab/gogpt-training-data huggingface dataset:
Protein: Lipid A 1-phosphatase (EC 3.1.-.-) (O24866)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Removes the 1-phosphate group from tetra- and probably hexaacylated lipid A species, has no requirement for the Kdo moiety of lipid A. Has no 4'-phosphatase activity. Has no activity on phospholipids (phosphatidylglycerol, phosphatidylethanolamine or cardiolipin). This enzyme has to act before EptA can attach phosphoethanolamine to the 1-position of lipid A. Absence of the 1-phosphate group renders the bacteria partially resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune response, and plays a role in the long-term colonization of the host's stomach (By similarity).
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:15489235, ECO:0000305|PubMed:16740959}; Multi-pass membrane protein {ECO:0000255}. Note=Activity depends on msbA function when expressed in E.coli, strongly suggesting this protein acts in the periplasm (MsbA flips the lipopolysaccharide precursor across the inner cell membrane). {ECO:0000269|PubMed:15489235}.
Interaction partners:
- Phosphoethanolamine transferase EptA
- DUF374 domain-containing protein
- Large ribosomal subunit protein uL6
Sequence:
MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGIFAPFPKVPKQPSVPLMFHFTEHYARFIPTILSVAIPLIQRDAVGLFQVANASIATTLLTHTTKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRYSFKKYFWLLPLVPLTMLARIYLDMHTIGAVLTGLGVGMLCVSLFTSPKKP
Protein: Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34) (D3ZAZ5)
Organism: Rattus norvegicus (Rat)
Function: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis. Promotes insulin-mediated membrane ruffling. In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (By similarity). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB/SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}.
Interaction partners:
- Breast cancer anti-estrogen resistance protein 1
- Enhancer of filamentation 1
Sequence:
MAAGKFASLPRHMPVNHQFPLASSMDLLSSKSPLAEHRTEAYPDVSIHGTLPRKKKGPPPIRSCDSASHMGTLPHSKSPRQSSPLTQDLILEKPLPDWKGDSFAFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSFAEGRPDVVKRLSLTTGGIQARDHSLPRGNLLRNKDKSGSQPACLDHVQDRKAATLKAHQSESHLPIGCKLPPQSPSVDTSPCPNSPVFRTGSEPTLSPALVRRFSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPPSPSPWLNSEANYCELNPAFAVGCDRGAKLLSQALDSHEMLLTAKQNGASGPRNSGINYSILDGDDQGRHWDPLAVQTDEGQEDETKFVPPVMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDMKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAMELKDTMGDLYSFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASSVSVPLLMPLVTLMERQAVTFEGTDMWEKNDESCEIMLSHLATARFMAEASESYRMNAERVLADFQPDEEMTEILKTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL
Protein: Defective proboscis extension response 18 (RE24718p) (Q9VXK1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein epsilon
Sequence:
MRLPKGYRTLSPASNAAQTLPLSYNSQTSLSLLRLLTIALVIGSQVQVLYTTSVETKSPSASEQSRNGENRSLLFDDYNKTKSTLSTADYLSATRATLYAFSSQDQDEDHSQMPIEASNAPHSPIPTKMSRGKIPMETPGSMEFSSNSLPIKNVGTTDQLTTVTMPTTAFASLKVDRSTMKQPIDSTRTRNHWTASGFARVTERPRSKHHHEHHWGPFFEEPINSATSGDNLVSAVHLFTEAVLNCRVGMLKDKTVMWVRRTAEKVSLLTVGNVTYSGDPRIRVKFQYPNNWRLLINPTQTEDAGVYMCQVSTHPPRVFTTNLTVLEPPLRIIDEHERDVGDRYYKSGSTVDLQCQISRSFFQKERQTILKSTDSANDAVQKLINETTSELNLIGNVNQTQHKFSGQDLEKYFTKFITWAKDEEPLQGMTNRRLSVSDVWLTSRISIGDAKLSDSGNYSCSLGRLFTVIVQVQVLTGELPAAVQHNIGSRTEIYSLAMLGHLLVLIFLFTCLKTENRHF
Protein: Cytospin-A (Renal carcinoma antigen NY-REN-22) (Sperm antigen with calponin homology and coiled-coil domains 1-like) (SPECC1-like protein) (Q69YQ0)
Organism: Homo sapiens (Human)
Function: Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21703590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21703590}. Cell junction, gap junction {ECO:0000269|PubMed:21703590}. Note=Colocalizes with acetylated alpha-tubulin, gamma-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microtubule organizing center.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 8
Sequence:
MKKASRSVGSVPKVSAISKTQTAEKIKPENSSSASTGGKLVKPGTAASLSKTKSSDDLLAGMAGGVTVTNGVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKESSSTRERLRERTRLNQSKKLPSAGQGANDMALAKRSRSRTATECDVRMSKSKSDNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTSSDDALDAPSSSESEGIPSIERSRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRPNYGEIPVQEHLLRTSSASRPASLPRVPAMESAKTLSVSRRSSEEVKRDISAQEGASPASLMAMGTTSPQLSLSSSPTASVTPTTRSRIREERKDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET
Protein: Lipopolysaccharide core galacturonosyltransferase RgtA (LPS core GalA transferase RgtA) (EC 2.4.1.-) (Dodecaprenyl phosphate-beta-galacturonate:lipopolysaccharide core alpha-galacturonosyltransferase RgtA) (Dodecaprenyl-P-GalA:LPS core galacturonosyltransferase RgtA) (Galacturonic acid transferase RgtA) (GalAT RgtA) (Q1MJ96)
Organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium leguminosarum bv. viciae)
Function: Involved in the modification of the lipopolysaccharide (LPS) inner core. Catalyzes the transfer of a galacturonic acid (GalA) residue to the 4-position of the outer Kdo (3-deoxy-D-manno-octulosonic acid) residue of the LPS inner core, using dodecaprenyl phosphate-GalA as the donor substrate. GalA addition by RgtA is required for RgtB activity.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:16497671, ECO:0000305|PubMed:16497674}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLERATRTIKTAGLLLAAYFVLNIVLRIVLPHSLELDEAEQSFFSQYLLAGYGPQPPFYNWMQYAVVSVTGISIGALIVPKNILLFLSYLFYGLAGRRVLKDEALAAVGMLALITLPQVSYMAQQDLTHTTALLFASSLFLYGFFRTLDRPDMASYLLLGLATGIGLISKYNFALMPVVALIAILPDAEWRRRALDWRMLAAITVALVIVLPHAVWLQGNLAFASSDTLVKMAAGSEPAGAVRIGKGLLAFLVAIIAFAALPVVIFAATFRRDFVRALSAGNRWTGMMERMMLASLAGIALIVLFTGSTTVRERWLDPFLLVLPIYFLAKMQAAGLDLSAGLRRFRPVLPVLMACVLIALGFRVVGAGLIGTYSRPNVPMAGFAREMTRQAEPALVIASDTYIGGNMRLQFPDVPVVIPDFPAPGIPAYAEAKGPVLIVWRGKKTATAADAVMPERFSSALTAAGIALQEIGSLSLPYYFGRQGDNFALGYAWVRPETR
Protein: Leucine-rich repeat protein kinase family protein (F4IVP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- LRR receptor-like Serine/Threonine-kinase
Sequence:
MQIICSMIFLLVMMVMKVSGFSDFEALLELKKGFQGDPSRKVLTSWDAKALSSDRCPLNWYGVTCSSGGVTSIDLNGFGLLGSFSFPVIVGLRMLQNLSIANNQFSGTLSNIGSLTSLKYLDVSGNLFHGALPSGIENLRNLEFVNLSGNNNLGGVIPSGFGSLAKLKYLDLQGNSFSGEVMSLFSQLISVEYVDISRNNFSGSLDLGLAKSSFVSSIRHLNVSGNSLVGELFAHDGIPFFDSLEVFDASSNQLSGSVPVFSFVVSLKILRLQDNQLSASLPPGLLQESSTILTDLDLSLNQLEGPIGSITSSTLEKLNLSSNRLSGSLPLKVGHCAIIDLSNNKISGELSRIQNWGDSVEIIRLSSNSLTGTLPGQTSQFLRLTSLKAANNSLQGVLPFILGTYPELKEIDLSHNQLSGVIPSNLFISAKLTELNLSNNNFSGSLPLQDASTVGNLSLTNIGLSHNSLGGVLSEELTRFHNLISLDLSYNNFEGNIPDGLPDSLKMFTVSANNLSGNVPENLRRFPDSAFHPGNALLNVPISLPKDKTDITLRKHGYHMKTSVKAALIIGLVVGTALLALVCVMFHFMLRKQHDEEKSDVTGEKSIVPKTEPSSSNVIAAKNSVQENESSSSTTSTPSIKAKLPVSSSRFSQYSDSENSSPFLKEPNEELHSESRKDEILSSQVSSSTPSLPKIQNSPDNPTSRQTSMRLDGNLYIFDSSLKLTAEELSRAPAEAIGRSCHGTLYRAVLNSDSVLAVKWLREGTAKGKKEFAREIKKLGNINHPNLVSLQAYYWGPKEHEKLIISRYMDAPCLAFYLQEAGQLNLPPLLLENRLKITLDIASCLSYLHNGEAIPHGNLKSTNVLLKPPELTAHLTDYSLHRLITPEATSEQVLNAAALGYCPPEFASSSKPYPSLKSDVYAFGVILLELLTGKVSGDIVCSDPGVVELTEWVLLLVGQNRATECFDPSIVGSQGSRNPFGVLTDVLQVALSCISPAPERPDMKLVSQELSRIVLKRTAI
Protein: Carbonic anhydrase 7 (EC 4.2.1.1) (Carbonate dehydratase VII) (Carbonic anhydrase VII) (CA-VII) (Q9ERQ8)
Organism: Mus musculus (Mouse)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTGHHCWGYGQDDGPSNWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPYRLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKDTKAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFRPPQPLKGRVVKASFQA
Protein: La protein homolog (La autoantigen homolog) (La ribonucleoprotein) (P33399)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone that binds nascent RNA polymerase III transcripts, stabilizing these RNAs against exonucleases. Required for the 3' endonucleolytic cleavage that matures tRNA precursors and for efficient folding of certain pre-tRNAs. Cooperates with GCD14 in the maturation of a subset of RNA polymerase III transcripts. Functions also in the assembly of certain RNA polymerase II-transcribed RNAs into RNPs. Binds and stabilizes newly synthesized U6 snRNA as well as precursors of U3 snRNA from degradation. Facilitates efficient Sm protein binding, thus assisting formation of the U4/U6 snRNP. Required for Ty3 normal transposition frequency.
Subcellular location: Nucleus {ECO:0000269|PubMed:10564276, ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}. Note=Imported into nucleus by the nuclear transport factor SXM1.
Interaction partners:
- Importin beta SMX1
- Exportin-T
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP14
- RNA exonuclease 1
- Eukaryotic translation initiation factor 4E
- Bud site selection protein 20
- LSM2-LSM8 complex subunit LSM8
- Eukaryotic initiation factor 4F subunit p150
Sequence:
MSEKPQQEEQEKPQSRRNSFAVIEFTPEVLDRCLKQVEFYFSEFNFPYDRFLRTTAEKNDGWVPISTIATFNRMKKYRPVDKVIEALRSSEILEVSADGENVKRRVPLDLTAARNARIEQNQRTLAVMNFPHEDVEASQIPELQENLEAFFKKLGEINQVRLRRDHRNKKFNGTVLVEFKTIPECEAFLKSYSNDDESNEILSYEGKKLSVLTKKQFDLQREASKSKNFSGRSRSFNGHKKKNLPKFPKNKKKNGKEESKEDSSAIADDDEEHKE
Protein: E1B protein, small T-antigen (E1B 19 kDa protein) (E1B-19K) (P03246)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates.
Subcellular location: Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina.
Interaction partners:
Sequence:
MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRRQEQSPWNPRAGLDPRE
Protein: Polycystin-2-like protein 2 (Polycystin-2L2) (Polycystic kidney disease 2-like 2 protein) (Polycystin-L2) (Q9NZM6)
Organism: Homo sapiens (Human)
Function: May function as a subunit of a cation channel and play a role in fertilization.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9JLG4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Polycystin-1-like protein 3
Sequence:
MAEASRWHRGGASKHKLHYRKEVEITTTLQELLLYFIFLINLCILTFGMVNPHMYYLNKVMSSLFLDTSVPGEERTNFKSIRSITDFWKFMEGPLLEGLYWDSWYNNQQLYNLKNSSRIYYENILLGVPRVRQLKVRNNTCKVYSSFQSLMSECYGKYTSANEDLSNFGLQINTEWRYSTSNTNSPWHWGFLGVYRNGGYIFTLSKSKSETKNKFIDLRLNSWITRGTRVIFIDFSLYNANVNLFCIIRLVAEFPATGGILTSWQFYSVKLLRYVSYYDYFIASCEITFCIFLFVFTTQEVKKIKEFKSAYFKSIWNWLELLLLLLCFVAVSFNTYYNVQIFLLLGQLLKSTEKYSDFYFLACWHIYYNNIIAITIFFAWIKIFKFISFNKTMSQLSSTLSRCVKDIVGFAIMFFIIFFAYAQLGFLVFGSQVDDFSTFQNSIFAQFRIVLGDFNFAGIQQANPILGPIYFITFIFFVFFVLLNMFLAIINDTYSEVKADYSIGRRLDFELGKMIKQSYKNVLEKFRLKKAQKDEDKKTKGSGDLAEQARREGFDENEIQNAEQMKKWKERLEKKYYSMEIQDDYQPVTQEEFRELFLYAVELEKELHYINLKLNQVVRKVSAL
Protein: Short transient receptor potential channel 1 (TrpC1) (Transient receptor protein 1) (TRP-1) (Q9QX01)
Organism: Rattus norvegicus (Rat)
Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Seems to be also activated by intracellular calcium store depletion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P48995}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Stromal interaction molecule 1
- Transient receptor potential cation channel, subfamily C, member 5
- Transient receptor potential cation channel subfamily V member 4
- Short transient receptor potential channel 4
- Polycystin-2
- Voltage-dependent T-type calcium channel subunit alpha-1H
- Bone morphogenetic protein receptor type-2
- Calcium release-activated calcium channel protein 1
- Voltage-dependent T-type calcium channel subunit alpha-1G
- Calcium release-activated calcium modulator 2 protein
Sequence:
MMAALYPSTDLSGVSSSSLPSSPSSSSPNEVMALKDVREVKEENTLNEKLFLLACDKGDYYMVKKILEENSSGDLNINCVDVLGRNAVTITIENESLDILQLLLDYGCQKLMERIQNPEYSTTMDVAPVILAAHRNNYEILTMLLKQDVALPKPHAVGCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVEVEFWNDYEELARQCKMFAKDLLAQARNSRELEVILNHTSSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCKKIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKKNTMGPALERIDYLLILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHDFADRKDWDAFHPTLVAEGLFAFANVLSYLRLFFMYTTSSILGPLQISMGQMLQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAIFVTRFSYGEELQSFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWVCSHTSKGKVRRQNSLKEWRNLKQKRDENYQKVMCCLVHRYLTSMRQKMQSTDQATVENLNELRQDLSKFRNEIRDLLGFRTSKYAMFYPKN
Protein: Kinesin-like protein KIN-10B (Q5E913)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AAA-type ATPase family protein
- Carbon-sulfur lyase
- Kinesin-like protein KIN-10A
- At5g67310
- Metallothionein-like protein 2B
- Probable E3 ubiquitin-protein ligase ARI14
- Kinesin-like protein KIN-10C
- Kinesin-like protein KIN-12F
Sequence:
MVDSKTPAKTKLLDSSSISNVRVVLRVRPFLPREISDESCDGRSCVSVIGGDGGDTSEVAVYLKDPDSCRNESYQLDAFYGREDDNVKHIFDREVSPLIPGIFHGFNATVLAYGATGSGKTFTMQGIDELPGLMPLTMSTILSMCEKTRSRAEISYYEVYMDRCWDLLEVKDNEIAVWDDKDGQVHLKGLSSVPVKSMSEFQEAYLCGVQRRKVAHTGLNDVSSRSHGVLVISVTSQGLVTGKINLIDLAGNEDNRRTGNEGIRLQESAKINQSLFALSNVVYALNNNLPRVPYRETKLTRILQDSLGGTSRALMVACLNPGEYQESLRTVSLAARSRHISNNVSLNPKVETPKVKIDMEAKLQAWLESKGKMKSAHRMMAIRSPLMGTNQTSISQSSVKKLLCHRSAIAESAKLAGTGQRDAFVTARNLFGVETLAASHLWEPIRNLQLASPTKEDERDTSGEENLLVSEASLRDNTLDVEKKYTELSPLREALSPIDSNAKPNSAHGSSPFLKPMTPKTPFLSTNPEIMQMEGTCQKFNAWSNNLKTSLIKEYIHFLNTANREELRELKGIGQKMAEYIIELRETSPLKSLTDLEKIGFTSRQVHNLFKKATEGVLEKPVSASTTP
Protein: Obscurin-like protein 1 (O75147)
Organism: Homo sapiens (Human)
Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24793695}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons (PubMed:21572988).
Interaction partners:
- Cullin-7
- Coiled-coil domain-containing protein 8
- Titin
- Myomesin-1
- F-box/WD repeat-containing protein 8
- Cullin-9
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase RBX1
Sequence:
MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPVVVWEKGGQQLAASERLSFPADGAEHGLLLTAALPTDAGVYVCRARNAAGEAYAAAAVTVLEPPASDPELQPAERPLPSPGSGEGAPVFLTGPRSQWVLRGAEVVLTCRAGGLPEPTLYWEKDGMALDEVWDSSHFALQPGRAEDGPGASLALRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPPESPPADPDEAPAPVVEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHWEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCAARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIAVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLIIHRLKADDDGIYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETLEAGVEGRWSRDGEELPVICQSSSGHMHALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPILAEMFKGHKNTVLLTWKPPEPAPETPFIYRLERQEVGSEDWIQCFSIEKAGAVEVPGDCVPSEGDYRFRICTVSGHGRSPHVVFHGSAHLVPTARLVAGLEDVQVYDGEDAVFSLDLSTIIQGTWFLNGEELKSNEPEGQVEPGALRYRIEQKGLQHRLILHAVKHQDSGALVGFSCPGVQDSAALTIQESPVHILSPQDRVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESELLVVKMDGRKHRLILPEAKVQDSGEFECRTEGVSAFFGVTVQDPPVHIVDPREHVFVHAITSECVMLACEVDREDAPVRWYKDGQEVEESDFVVLENEGPHRRLVLPATQPSDGGEFQCVAGDECAYFTVTITDVSSWIVYPSGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLQKEDTVRRLVLPAVQLEDSGEYLCEIDDESASFTVTVTEPPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKDGLEVEESEALVLERDGPRCRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLHFGAPGRVELRCEVAPAGSQVRWYKDGLEVEASDALQLGAEGPTRTLTLPHAQPEDAGEYVCETRHEAITFNVILAEPPVQFLALETTPSPLCVAPGEPVVLSCELSRAGAPVVWSHNGRPVQEGEGLELHAEGPRRVLCIQAAGPAHAGLYTCQSGAAPGAPSLSFTVQVAEPPVRVVAPEAAQTRVRSTPGGDLELVVHLSGPGGPVRWYKDGERLASQGRVQLEQAGARQVLRVQGARSGDAGEYLCDAPQDSRIFLVSVEEPLLVKLVSELTPLTVHEGDDATFRCEVSPPDADVTWLRNGAVVTPGPQVEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSARLHVRETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHDSRLSMAQDGHIHRLFIHGVILADQGTYGCESHHDRTLARLSVRPRQLRVLRPLEDVTISEGGSATFQLELSQEGVTGEWARGGVQLYPGPKCHIHSDGHRHRLVLNGLGLADSGCVSFTADSLRCAARLIVREVPVTIVRGPHDLEVTEGDTATFECELSQALADVTWEKDGNALTPSPRLRLQALGTRRLLQLRRCGPSDAGTYSCAVGTARAGPVRLTVRERTVAVLSELRSVSAREGDGATFECTVSEVETTGRWELGGRPLRPGARVRIRQEGKKHILVLSELRAEDAGEVRFQAGPAQSLALLEVEALPLQMCRHPPREKTVLVGRRAVLEVTVSRSGGHVCWLREGAELCPGDKYEMRSHGPTHSLVIHDVRPEDQGTYCCQAGQDSTHTRLLVEGN
Protein: Phosphoglucomutase (PGM) (EC 5.4.2.2) (Glucose phosphomutase) (Q9P931)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P37012}.
Interaction partners:
- Alpha-1,4 glucan phosphorylase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase, putative
- UTP--glucose-1-phosphate uridylyltransferase
- Hexokinase
- Ribose-5-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-epimerase
Sequence:
MSVQTVSIQPFGDQKPGTSGLRKKVKIFQQENYTESFLTSIFLSIPEGAQDAFLVIGGDGRYYNSDVIQKIAKIGAAYGVKKLIVGQNGILSTPAASNLIRKRKATGGILLTASHNPGGPDNDFGIKYNLTNGAPAPEQVTNKIYEVSKSLTSYKYIDLPEVDTTTVGTRSYGPLEVEVVHSTEDYVSMMKEIFDFDLIRSFLKKHPDFKVLFDGMHGVTGPYGIDIFVNELGLPSSSTMNCIPKPDFGGGHPDPNLVYAHELVEAVDKNGIHFGAASDGDGDRNMIYGANTFVSPGDSLAIIAHHAKLIPWFQKHGVDGLARSMPTSGAVDRVAKAQGLQSYEVPTGWKFFCNLFDNKKMSICGEESFGTGSNHIREKDGVWAIVAWLNVIAGVAEQKPNETPSIASIQAEFWETYGRTFFTRYDYENVDSDGANKLIAALSEKAVDNKSSFVGSTISGRKVVDSGNFAYTDLDGSVTKNQGLYVKFDDGSRLVVRLSGTGSSGATIRLYVEKYEGDKSKYQMATQDYLKDNVGLALELLKFKEFVGREEPDVKT
Protein: Protocadherin 1 isoform 1 (Q2TJI8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
YCRQREAKSGYQAGKKETKDLYAPKPSGKAAKGSKSKGKKSKSPKPVKPVEDEDDTGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQVGQPFRLSTPQPPPHPYHGAIWTEVWE
Protein: Endochitinase (EC 3.2.1.14) (Soluble cell wall protein 2) (P29029)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Chitinase is required for cell separation during growth of S.cerevisiae.
Subcellular location: Secreted {ECO:0000269|PubMed:9748433}. Secreted, cell wall {ECO:0000269|PubMed:9748433}. Note=Most of the enzyme is secreted, but a significant amount of chitinase is also found associated with the cell wall through binding of C-terminal domain to chitin.
Interaction partners:
- Protein DSE2
- Metallothionein expression activator
- Sporulation-specific chitinase 2
- Protein EGT2
- Transcriptional factor SWI5
- Probable secreted beta-glucosidase SUN4
- Probable family 17 glucosidase SCW11
- Protein DSE1
- Glucan endo-1,3-beta-D-glucosidase 1
- Chitin deacetylase 2
Sequence:
MSLLYIILLFTQFLLLPTDAFDRSANTNIAVYWGQNSAGTQESLATYCESSDADIFLLSFLNQFPTLGLNFANACSDTFSDGLLHCTQIAEDIETCQSLGKKVLLSLGGASGSYLFSDDSQAETFAQTLWDTFGEGTGASERPFDSAVVDGFDFDIENNNEVGYSALATKLRTLFAEGTKQYYLSAAPQCPYPDASVGDLLENADIDFAFIQFYNNYCSVSGQFNWDTWLTYAQTVSPNKNIKLFLGLPGSASAAGSGYISDTSLLESTIADIASSSSFGGIALWDASQAFSNELNGEPYVEILKNLLTSASQTATTTVATSKTSAASTSSASTSSASTSQKKTTQSTTSTQSKSKVTLSPTASSAIKTSITQTTKTLTSSTKTKSSLGTTTTESTLNSVAITSMKTTLSSQITSAALVTPQTTTTSIVSSAPIQTAITSTLSPATKSSSVVSLQTATTSTLSPTTTSTSSGSTSSGSTSSDSTARTLAKELNAQYAAGKLNGKSTCTEGEIACSADGKFAVCDHSAWVYMECASGTTCYAYDSGDSVYTQCNFSYLESNYF
Protein: Zinc finger protein 386 (Kruppel-like) (Q6AYY1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEMEQLTFRDVAVDFSPDEWECLDPPQQRLYRDVMVENYRNLVSVALSHHCTQNFSPEQILKYSFTKGTNGSCGLKSLYLREDCIYIDESKAHHGRDMQCLITSNTKDVIDSRDQEHKTALTITPVRPDTLDEPSIYNCKYPQESFQHDLTLKESLEDLIDGLMFHPNSSIDKELRSRGLISTSDQIETFYTERSLLFSQQIAISYDPKHNSIDYGLPAIDPLSHSPNGDTDVWESPFMYKETSKDFSSESLLNNCNDIILEKSSQYNKICNDFDHCSSPNKYQYTLPKKPFNCDNFFTQCSKLSIHQYVQDNCYKSIDCDTMFNKTLNVITHKIQHSQKSYKCNECGKAFKYCSSYRKHRIIHTGEKPFKCKVCGKSFTQCASLKKHQRIHTGEKPYKCEECGRSFNHYSILGQHQRIHTGEKPYKCKQCGKSFTQCSSLQKHQVIHTGEKPFRCAECGKSFTQNSTLSQHQRIHTGEKPYKCEQCGKAFTQCSSLRKHQRIHTGEKPYKCEECGRAFNCRSSFTKHKRIHTGEKPYKCKDCDKAFIHCTNLTQHRRIHTGEKPYKCNECGKSFSQCSNLRKHERIHT