wanglab/gogpt-training-data huggingface dataset:
Protein: Methanethiol oxidase (MTO) (EC 1.8.3.4) (56 kDa selenium-binding protein) (SBP56) (SP56) (Selenium-binding protein 1) (P17563)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria. Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13228}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13228}. Membrane {ECO:0000250|UniProtKB:Q8VIF7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8VIF7}. Note=May associate with Golgi membrane (By similarity). May associate with the membrane of autophagosomes (By similarity). {ECO:0000250|UniProtKB:Q8VIF7}.
Interaction partners:
- Selenium-binding protein 2
- Sulfide:quinone oxidoreductase, mitochondrial
- 3-mercaptopyruvate sulfurtransferase
- Cystathionine beta-synthase
- Thiosulfate sulfurtransferase
- Putative adenosylhomocysteinase 3
- S-adenosylhomocysteine hydrolase-like protein 1
- Adenosylhomocysteinase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Betaine--homocysteine S-methyltransferase 1
Sequence:
MATKCTKCGPGYSTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYSQVIHRLPMPYLKDELHHSGWNTCSSCFGDSTKSRNKLILPGLISSRIYVVDVGSEPRAPKLHKVIEASEIQAKCNVSSLHTSHCLASGEVMVSTLGDLQGNGKGSFVLLDGETFEVKGTWEKPGDAAPMGYDFWYQPRHNVMVSTEWAAPNVFKDGFNPAHVEAGLYGSRIFVWDWQRHEIIQTLQMTDGLIPLEIRFLHDPSATQGFVGCALSSNIQRFYKNAEGTWSVEKVIQVPSKKVKGWMLPEMPGLITDILLSLDDRFLYFSNWLHGDIRQYDISNPQKPRLAGQIFLGGSIVRGGSVQVLEDQELTCQPEPLVVKGKRIPGGPQMIQLSLDGKRLYATTSLYSAWDKQFYPDLIREGSMMLQIDVDTVNGGLKLNPNFLVDFGKEPLGPALAHELRYPGGDCSSDIWI
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2 (Oligosaccharyl transferase subunit KCP2) (Keratinocyte-associated protein 2) (KCP-2) (Q8N6L1)
Organism: Homo sapiens (Human)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21768116}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22266900}; Multi-pass membrane protein {ECO:0000269|PubMed:22266900}.
Interaction partners:
- Oligosaccharyltransferase complex subunit OSTC
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
Sequence:
MVVGTGTSLALSSLLSLLLFAGMQMYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQAAAPVLTPAKVTGKSKKRN
Protein: Putative NADPH dehydrogenase C23G7.10c (EC 1.6.99.1) (Old yellow enzyme homolog 3) (O94467)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Fumarate reductase
- Pumilio domain-containing protein C4G8.03c
Sequence:
MTIVNEGAENVGYFTPAQKIPAGAAIGVPQTKLFTPLKIRGVEFHNRMFVSPMCTYSADQEGHLTDFHLVHLGAMGMRGPGLVMVEATAVSPEGRISPNDSGLWMESQMKPLRRIVEFAHSQNQKIGIQLAHAGRKASTTAPYRGYTVATEAQGGWENDVYGPNEDRWDENHAQPHKLTEKQYDELVDKFVVAAKRAVEIGFDVIEIHGAHGYLISSTVSPATNDRNDKYGGTFEKRILFPMEVVHSVRKAIPDSMPLFYRVTATDWLPKGQGWEIEDTVALAARLRDGGVDLIDVSSGGNHKDQRIEVKDCYQVPFAEKIKDQVNGILLGAVGMIRDGLTANEILESGKADVTFVAREFLRNPSLVLDSANQLGENVAWPVQYDYAVKGHRKLR
Protein: PHD finger protein 23 (I3L1N0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALTPVPLSQGDLSHPPRKKDRKNRKLGPGAGAGFGVLRRPRPTPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPQAPPSDTDSEEEEEEEEEEEEEEMATVVGGEAPVPVLPTPPEAPRPPATVHPEGVPPADSESKEVGSTETSQDGDASSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGPPKSGEP
Protein: Urease accessory protein F (AtUREF) (E0ZS46)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
Interaction partners:
Sequence:
MERVMECDYPASKKNKVVHPMDCEMKEEPTNAASMNQHSLWSQWQLLDSILPTGGFAHSYGLEAAMQSRMVNNPEELRSFVVQVLENTGSLLLPFVCCANKSPDAATWVKLDQLLEAMLTNEVSRKASMSQGSALLRVAASVFTEIQSLQDLRQTFLGSKIVSFHHAPIFGLICGLVGFDSETTQRAYMFVTMRDVISAATRLNLIGPLAASVLQHQVAEDAERMVQKWKDRGVEEATQTSPLLDALQGCHAYMFSRLFCT
Protein: Smad1 protein (Q9W6N2)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
NSSATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPASSDPGSPFQMPADTPPPAYLPPEDQMTHDTSQPMDTNMMAPGIHPDIHRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSILVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTLRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: ESX-1 secretion system protein EccCa1 (ESX conserved component Ca1) (Snm1 secretory protein) (Type VII secretion system protein EccCa1) (T7SS protein EccCa1) (P9WNB3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ESX-1 secretion system protein EccCb1
- ESX-1 secretion system ATPase EccB1
- ESX-1 secretion system protein EccD1
- ESX-1 secretion system protein EccA1
- 6 kDa early secretory antigenic target
- ESAT-6-like protein EsxB
- ESX-1 secretion system protein EccE1
- ESX-1 secretion-associated protein EspG1
- ESX-1 secretion-associated protein EspH
- ESX-1 secretion-associated protein EspF
Sequence:
MTTKKFTPTITRGPRLTPGEISLTPPDDLGIDIPPSGVQKILPYVMGGAMLGMIAIMVAGGTRQLSPYMLMMPLMMIVMMVGGLAGSTGGGGKKVPEINADRKEYLRYLAGLRTRVTSSATSQVAFFSYHAPHPEDLLSIVGTQRQWSRPANADFYAATRIGIGDQPAVDRLLKPAVGGELAAASAAPQPFLEPVSHMWVVKFLRTHGLIHDCPKLLQLRTFPTIAIGGDLAGAAGLMTAMICHLAVFHPPDLLQIRVLTEEPDDPDWSWLKWLPHVQHQTETDAAGSTRLIFTRQEGLSDLAARGPHAPDSLPGGPYVVVVDLTGGKAGFPPDGRAGVTVITLGNHRGSAYRIRVHEDGTADDRLPNQSFRQVTSVTDRMSPQQASRIARKLAGWSITGTILDKTSRVQKKVATDWHQLVGAQSVEEITPSRWRMYTDTDRDRLKIPFGHELKTGNVMYLDIKEGAEFGAGPHGMLIGTTGSGKSEFLRTLILSLVAMTHPDQVNLLLTDFKGGSTFLGMEKLPHTAAVVTNMAEEAELVSRMGEVLTGELDRRQSILRQAGMKVGAAGALSGVAEYEKYRERGADLPPLPTLFVVVDEFAELLQSHPDFIGLFDRICRVGRSLRVHLLLATQSLQTGGVRIDKLEPNLTYRIALRTTSSHESKAVIGTPEAQYITNKESGVGFLRVGMEDPVKFSTFYISGPYMPPAAGVETNGEAGGPGQQTTRQAARIHRFTAAPVLEEAPTP
Protein: DNA polymerase delta subunit 3 (P47110)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA polymerase delta (DNA polymerase III) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA polymerase zeta processivity subunit
- DNA polymerase delta small subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase zeta catalytic subunit
- Proliferating cell nuclear antigen
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase alpha catalytic subunit A
- Replication factor A protein 1
- DNA polymerase alpha subunit B
- ATP-dependent helicase SGS1
Sequence:
MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
Protein: Chymotrypsinogen B (EC 3.4.21.1) [Cleaved into: Chymotrypsin B chain A; Chymotrypsin B chain B; Chymotrypsin B chain C] (P17538)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Carboxypeptidase A1
- Alpha-1-antichymotrypsin
- Alpha-1-antitrypsin
- Chymotrypsinogen B2
- Carboxypeptidase B
- Pancreatic triacylglycerol lipase
- Bile salt-activated lipase
- Serine protease inhibitor Kazal-type 1
- Serine protease 1
- Alpha-2-macroglobulin
Sequence:
MASLWLLSCFSLVGAAFGCGVPAIHPVLSGLSRIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKSWGRRITDVMICAGASGVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSDTCSTSSPGVYARVTKLIPWVQKILAAN
Protein: Meiotic driver wtf9 (A0A482AQV2)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKYYPLRSSMDEMSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTETTNPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFFVTIGITCPILLITIFCFFETWTQAVAQCIKVTVIFLAQCVKVTVISLAKCVKVTAISLAKCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRSKFGNLNLNKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLMHLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALRRMPKSIRNGIASFLEGTGKAIRGANDNNNNIPLEETEAESEV
Protein: Terephthalate 1,2-dioxygenase, reductase component 2 (TER dioxygenase system) (TERDOS) (TPADO reductase component) (EC 1.14.12.15) (Q3C1D2)
Organism: Comamonas sp
Function: Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). TphA1 probably reduces TphA2A3. It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.
Interaction partners:
Sequence:
MNHQIHIHDSDIAFPCAPGQSVLDAALQAGIELPYSCRKGSCGNCASTLLDGNIASFNGMAVRNELCASEQVLLCGCTAASDIRIHPSSFRRLDPEARKRFTAKVYSNTLAAPDVSLLRLRLPVGKRAKFEAGQYLLIHLDDGESRSYSMANPPHESDGITLHVRHVPGGRFSTIVQQLKSGDTLDIELPFGSIALKPDDARPLICVAGGTGFAPIKSVLDDLAKRKVQRDITLIWGARNPSGLYLPSAIDKWRKVWPQFRYIAAITDLGDMPADAHAGRVDDALRTHFGNLHDHVVHCCGSPALVQSVRTAASDMGLLAQDFHADVFATGPTGHH
Protein: Splicing factor 3b, subunit 2 (A0A8I6A8Y6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAEHPEPPKGELQLPPPPPPGHYGAWAAQELQAKLAEIGAPIQGSREELVERLQTYTRQTGIVLNRPVLRGEDGDKAAPPPMSAQLSGIPMPPPPLGLPPLQPPPPPPPPPPGLGLGFPMAHPPNLGPPPPLRVGEPVALSEEERLKLAQQQAALLMQQEERAKQAAVLMEQERQQEIAKMGTAVPRPPQDMGQLGVRTPLGPRVAAPVGPVVPTPTVLPMGAPVPRPRGPPPPPGDENREMDDPSVGPKIPQALEKILQLKESRQEEMNSQQEEEEMETDTRSSLGQSASETEEDTVSTSKKEKNRKRRNRKKKKKPQRVRAASSESSGDREKDSARSRGSDSPAADVEIEYVTEEPEIYEPNFIFFKRIFEAFKLTDDVKKEKEKEPEKLDKMENSAVPKKKGFEEEHKDSDDDSSDDEQEKKPEAPKLSKKKLRRMNRFTVAELKQLVARPDVVEMHDVTAQDPKLLVHLKATRNSVPVPRHWCFKRKYLQGKRGIEKPPFELPDFIKRTGIQEMREALQEKEEQKTMKSKMREKVRPKMGKIDIDYQKLHDAFFKWQTKPKLTIHGDLYYEGKEFETRLKEKKPGDLSDELRISLGMPVGPNAHKVPPPWLIAMQRYGPPPSYPNLKIPGLNSPIPESCSFGYHAGGWGKPPVDETGKPLYGDVFGTNAAEFQTKTEEEEIDRTPWGELEPSDEESSEEEEEEESDEDKPDETGFITPADSGLITPGGFSSVPAGMETPELIELRKKKIEEAMDGSETPQLFTVLPEKRTATVGGAMMGSTHIYDMSTVMSRKGPAPELQGVEVALAPEELELDPMAMTQKYEEHVREQQAQVEKEDFSDMVAEHAAKQKVGSNLGTLEWQIGVGSVLSALGVRGGWTHC
Protein: 24-methylenesterol C-methyltransferase 2 (24-sterol C-methyltransferase 2) (Sterol-C-methyltransferase 2) (EC 2.1.1.143) (Protein COTYLEDON VASCULAR PATTERN 1) (Q39227)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the methylene group of 24-methylene lophenol to form 24-ethylidene lophenol.
Interaction partners:
- Probable 3-beta-hydroxysteroid-Delta
- Methylsterol monooxygenase 2-2
- Methylsterol monooxygenase 2-1
- Delta
- 24-methylenesterol C-methyltransferase 3
- Cycloeucalenol cycloisomerase
- Cytochrome P450 710A1
- Ergosterol biosynthetic protein 28
- 7-dehydrocholesterol reductase
- Serine carboxypeptidase-like 8
Sequence:
MDSLTLFFTGALVAVGIYWFLCVLGPAERKGKRAVDLSGGSISAEKVQDNYKQYWSFFRRPKEIETAEKVPDFVDTFYNLVTDIYEWGWGQSFHFSPSIPGKSHKDATRLHEEMAVDLIQVKPGQKILDVGCGVGGPMRAIASHSRANVVGITINEYQVNRARLHNKKAGLDALCEVVCGNFLQMPFDDNSFDGAYSIEATCHAPKLEEVYAEIYRVLKPGSMYVSYEWVTTEKFKAEDDEHVEVIQGIERGDALPGLRAYVDIAETAKKVGFEIVKEKDLASPPAEPWWTRLKMGRLAYWRNHIVVQILSAVGVAPKGTVDVHEMLFKTADYLTRGGETGIFSPMHMILCRKPESPEESS
Protein: RNA helicase (EC 3.6.4.13) (F6R6M7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVCFCDSHFPRGDNEELHLPYVSVYFLPKVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIV
Protein: Nucleoside diphosphate kinase homolog 7 (NDK 7) (NDP kinase homolog 7) (3'-5' exonuclease NME7) (EC 3.1.-.-) (Protein kinase NME7) (EC 2.7.-.-) (nm23-H7) (Q5E9Y9)
Organism: Bos taurus (Bovine)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y5B8}. Nucleus {ECO:0000250|UniProtKB:Q9Y5B8}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y5B8}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Y5B8}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37327785}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9Y5B8}. Note=Localizes to centrosomes through its assembly into gamma-tubulin ring complex. The centrosomal content of NME7 varies during the cell cycle, being highest in mitosis and lowest in early G1. {ECO:0000250|UniProtKB:Q9Y5B8}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Cilia- and flagella-associated protein 206
- Guanosine-3',5'-bis
- Ribonucleoside-diphosphate reductase
- Cancer-related nucleoside-triphosphatase homolog
- UMP-CMP kinase 2, mitochondrial
- GTP:AMP phosphotransferase AK3, mitochondrial
- UMP-CMP kinase
- Guanylate kinase
- CTP synthase 2
Sequence:
MNHSERFVFIAEWFDPNASLFRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYEDLHLEDLFIGNKVNIFSRQLVLLDYGDQYTARQLGSKKEKTLALIKPDAVSKAGEIIEIINKAGFTLTKLKMMTLSRKEATDFHIDHQSRPFLNELIQFITSGPIIAMEILRDDAVCEWKRLLGPANSGLARTDAPESIRALFGTDGIKNAAHGPDSFACAAREMELFFPSSGVCGPANTAKFTNCTTCCIVKPHAVSEGLLGKILMTIRDAGFEISAMQMFNMDRINVEEFYEVYKGVVSEYNEMVTEMYSGPCVAMEIQQTNPTMTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLPEDGLLEVQYFFKILDN
Protein: Metallo-peptidase, Clan MA(E), family 32 (Q4QGE5)
Organism: Leishmania major
Interaction partners:
Sequence:
MQAYTQLEKLCHKVHRLTHLLSLGAWDAKTMMPSKGAAARGAALGELHGLITEMITSPSTKALLDEAETAKAELTTVQQANLRELRRIYASQAALPTELRVLKTKLSATTPLIWAKCRSNNDFATFLPALKEMIALARREAQYRSAATGKPLYEALFNQYESGMTLETLEKILLDVKSWLPELLQKILAAQRDAGLEVVAPEAPFPKDKQEALSRHLMEVWGFDFESGRLDVSEHPFTGMVKEDSRITTAYDLQDFAKGLFATIHETGHSKYETNCGPMEMRGQPVCEARSMTIHESQSRFAEVVIGHSSAFLEFLTPLLKEYFGDQPAFSLENVRLMNQTVKPGFIRIRADEVCYPLHILLRYEIERALIEGTMEAEDIPRVWNEKMKAYLGLETEGRDEIGCLQDIHWSMGAFGYFPTYSLGSMFAAQLMVTIKNELGEDTVDKCIRTGQMEPIFEKQREKIWSQGCLYDTEDLILKATGEALNPKHFREYLERRYLRQEG
Protein: Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form] (Q29121)
Organism: Sus scrofa (Pig)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides (By similarity).
Subcellular location: [Polypeptide N-acetylgalactosaminyltransferase 1]: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]: Secreted {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Membrane bound O-acyltransferase domain containing 2
- C1GALT1-specific chaperone 1
- C1GALT1-specific chaperone 1
- alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
- Secreted phosphoprotein 24
Sequence:
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQDKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMLEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQIINKNNRRLAEVWMDEFKTFFYIISPGVTKVDYGDISSRLGLRHKLQCRPFSWYLENIYPDSQIPRHYSSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDCSGSRSQQWLLRNVTLPEIF
Protein: Tyrosine hydroxylase 2 (EC 1.14.16.2) (Q6IVB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKSDSIAQNVPLSGRKRSLIEDARRDRESGSSSPGPSRCGDSFVFEEEKTGKITLNILFALKNEKNAGFFKAGKVFETFETKLLHLESRASRKSKRSSGEDLEFFMRCEVHCSDTDIFINSLKRVADDVRIVQEEKTPWFPKKISDLDTCNHLITKYDPDLDQDHPGFSDSEYRKRRGFISEMAFNYKHGDPLPVVEYTPEENATWEVYRTLRSLYPSHACRQFLEALTQLESERLYGEDQIPQLREVSAFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHPSAPMHSPEPDCCHELLGHIPMLADQEFAQFSQIGLVSLGASDEDIEKLSTDYWFTVEFGLCKQNGAVKAYGAGLLSSYGELLYALSNEPQYKPFDPAETAVQPYQDQSYQPVYFVSESFEDAKQKLRRYSSTIQTPFSIRYDPYTCSMEVLDEPSKIQNALGQMRDDLKILHKALGRLGQK
Protein: Scramblase ANY1 (Antagonizes NEO1 phospholipid flippase protein 1) (CDC50 suppressor 1) (Q03687)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phospholipid scramblase that transports phosphatidylserine (PS) and phosphatidylethalonamine (PE) bidirectionally from one leaflet to the other of the phospholipid bilayer to at least partially collapse the membrane asymmetry established by NEO1 and other flippases. Functions in the trafficking pathway from endosomes to the trans-Golgi network (TGN).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:27811238, ECO:0000269|PubMed:28057802}; Multi-pass membrane protein {ECO:0000269|PubMed:27811238}. Late endosome membrane {ECO:0000269|PubMed:27811238, ECO:0000269|PubMed:28057802}; Multi-pass membrane protein {ECO:0000269|PubMed:27811238}.
Interaction partners:
- Phospholipid-transporting ATPase NEO1
- Protein DOP1
- Protein MON2
- Inositol phosphorylceramide synthase catalytic subunit AUR1
- Phospholipid-transporting ATPase DRS2
- Phospholipid-transporting ATPase accessory subunit CDC50
- Probable phospholipid-transporting ATPase DNF3
Sequence:
MSTTGPLDATLIRDVAVATATKASYDMSDTLYSYLPKVDQFYIPEWLTMQFIANNLISFTPLFSYGTTIISIEKCKTALGFSIDICATMLIASILRISYYLITPYEITLLRQSLVMIFIQLILLRTSLKYRPDEYKYQNLTDVESLSHLIHDIWFEFFSCINRPKFLSEDWKNLIKSLSFTNLLKFSFKIFLAFFYKILKFFDPNFKRIGAFWQWDDDKNFWRFLALFATVQILVTFFISNILNWDSLAQGLGSIIGSLGLLVESLLPLPQIAILYKLKSVQGFKLILLVSWLCGDTLKITYLIFGAKNISALFVIFALFQMSLDFYIGGQYIYYRYYYPKLRHQHHPNDSNSPSDEDESEMYELDLFNTLQKDVEKALKQDSNDTSDSPQDDQVGKSQAQAVTL
Protein: Smr domain-containing protein C1235.03 (O74840)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL27B
- Uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02
- Ribosome biogenesis protein nsa2
- Galactose-specific cell agglutination protein gsf2
- mRNA export factor elf1
Sequence:
MQDWRAALEEYYSRYLDSALVLAIVNDSDDSNTAREILEALSIESQCDSHEEHWDNLRRDEQELLNLKTLDEEINKIDEEDFTWELKDSSLELDPDVYNFLRSMFSDLSAARVQLVQAKCQNDLVRSSDELLNHRAIQESEQIETAADALITSNIGHRSRQRKKKTKKATNSRKPLSKFQSNTEEVNEDPILKPSLSVWENNRLLIEKLTSILNIPSSQINHEFYKNSSAWPITIRNLIHRHQPLSNITNNELMKYQEEATQLAKDTGLSLKICTDVLICSNDYKNALWILCLIKETQHNEMGNIKLSSQTAKSNSSTQTKTCLNDQSSKLVEDDEALSAEDCNRLAEEYLELRNMQYSNSAKEYRRSKSNHLFGGSAMYHAQLGREYHEKALKYRSLAMRSLAHSGTSHSLDLHGATVREAKTIVRERVAAWWAKEADTSPNSIRPFVIVTGRGNHSIGLEARLLPAIVRLLQQDHWRFDAEHGQITVYGINRHSKLNSNA
Protein: Uncharacterized protein YncL (A5A615)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Single-pass membrane protein {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}.
Interaction partners:
- Uncharacterized membrane protein YohP
- Orphan toxin OrtT
- UPF0387 membrane protein YohO
- Uncharacterized protein YniD
- Uncharacterized protein YjeV
Sequence:
MNVSSRTVVLINFFAAVGLFTLISMRFGWFI