wanglab/gogpt-training-data huggingface dataset:
Protein: Kinase suppressor of ras 1 (A0A8I5ZQW6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDRAALRAAAMGEKKEGGGGGASAAADGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCSVSNDLTQQEIRTLEAKLVRYICKQRQSKLSVTPSDRTAELNSYPRFSDWLYIFNVRPEVVQEIPQELTLDALLEMDEAKAKEMLRRWGASAEECSRLQQALTCLRKVTGLGGEHKEDSGWSSAEARESSSGPSVDMLSSLGRAGASTQGPRSISVSALPASDSPVPGLSEGLSDTCIPLHTSGRLTPRALHSFITPPTTPQLRRHAKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDEVAPMRFELPHGSPQLVRRDIGLPVTHRFSTKSWLSQVCNVCQKSMMFGVKCKHCRLKCHNKCTKEAPACRISFLPLARLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNLDSSSNPSSTTSSTPSSPAPFLTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPDISACPQAAPLSSTADSTRLDDQPKTDVLGVPEAEAEEPEAGKSEAEDDEDEIDDLPSSRRHWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVKRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADRWRSRYYGKGRYGHPDFKSSCPLLEE
Protein: Calcium-dependent mitochondrial ATP-magnesium/phosphate carrier protein 3 (AtAPC3) (Mitochondrial ATP-Mg/Pi carrier protein 3) (Q9LY28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi). Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate, sulfate and thiosulfate, and, to a lesser extent, other nucleotides. Binds calcium ions Ca(2+). Mediates also calcium uptake (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:22062157}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Nuclear transport factor 2
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- NAD
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
Sequence:
MESSKPKNRNPMKKPVSITMEHVLLALRETMDEREIRIRSLFDFFDNSNLGFLDYAQIEKGLASLQIPPEYKYARDLFRVCDANRDGRVDYQEFRRYIDAKELELYRIFQAIDVEHNGCILPEELWEALVKAGIEIDDEELARFVEHVDKDNNGTITFEEWRDFLLLYPHEATLENIYHHWERVCLIDIGEQAVIPDGISKHVKRSRLLLAGGLAGAVSRTATAPLDRLKVVLQVQRAHAGVLPTIKKIWREDKLMGFFRGNGLNVMKVAPESAIKFCAYEMLKPMIGGEDGDIGTSGRLMAGGMAGALAQTAIYPMDLVKTRLQTCVSEGGKAPKLWKLTKDIWVREGPRAFYKGLFPSLLGIVPYAGIDLAAYETLKDLSRTYILQDTEPGPLIQLSCGMTSGALGASCVYPLQVVRTRMQADSSKTTMKQEFMNTMKGEGLRGFYRGLLPNLLKVVPAASITYIVYEAMKKNMALD
Protein: Alpha-amylase 1C (EC 3.2.1.1) (P0DTE8)
Organism: Homo sapiens (Human)
Function: Calcium-binding enzyme that initiates starch digestion in the oral cavity. Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Protein: Alpha-1,3/1,6-mannosyltransferase ALG2 (EC 2.4.1.132) (EC 2.4.1.257) (Asparagine-linked glycosylation protein 2 homolog) (GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase) (GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase) (GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase) (Q7KWM5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P43636}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GDP-Man:Man
- DNA helicase
- 1,4-alpha-glucan-branching enzyme
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Man
Sequence:
MVKDEKELNIAILHPDLGIGGAERLIVDLALGLKSVGNNRITMYTSRHDPKRCFKETSNGELDVHVTGGYFPRHIFNRFMVICAIIRNLLAALYIIFFSGQKYDVIVLDQISASIPLFKLFTNSKVLFYCHFPDKLLTSRTSLIKRLYRIPIDLFEEFTTGCADQVLVNSNFTSSIYKQSFKHLKNSPSVLYPIINTNEFDKTKQSHNFSNQPIENNLINPIKLDDKKFFLSINRYERKKDLKLALDAFSVFISNSESGGSGKGKDEIYLVFAGGYDTGLKENVEHLQELKDKAKEYGLENRVIFLITINEEQKQWLLLNCCCLIYTPSFEHFGITPLEGMYAGKPVIAVNNGGPLETVVDGKTGYLCNPTVKDFANAFNKIINDPINSKKMGINGKQRVNDKFSFKPFAQNLNTIVKKL
Protein: Uncharacterized protein (Q4GZ65)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTERELVTLALGNYATLVAAQWANGTTSYDVAHNTLYTERHLRAVCGGAVDNNRSELQSGTDGLIRVPRLVLLDAPHATRLRCKPSLNAAAAVQNEESEGEHEQNETRIYDDDDDDDDDDESESEKDAGGDDAESRYYTRGEVGTGVFLQGDSLAMNSETHETGAFDAQRSTSETAVSSFQKSQPSLKAIKRRLFREKDDLIPWWQYICSGVASDAVHVLHPLHRIGGIPTAGGNDIPLLHNFGFGMSHLRSSVSSNVADVVESLRRQLEDADLLQGLQCFVDGDSAFGGAACNIMEEFWEDAGSKVPATFFCCFQTLPEEVAAAHSDVDFADRRKDEQCLNRLLATAKLSSHDSAVYVPMELAQWRTSFASSSSLNGSTHLAPKAAAWLQDDTATAQVVASFADTTLYGTRDEGKLNTGGCGGPAFYMQDWQAAVRPTRCLRVASALTSMPMPVHDVRLPRGDLWDFLQRNPLLQTSCGEGGGYFAPLTHAVSSGPEKESGRVLGHAVTLRGAGQLHDLTYPRQEALLRYALPLRSGNYLPLITDNSYPISSTFPRDFVLPNELVSSGALQGIDMGSHIVSTYDSAPMLQSIVAQAQKVVRRSRHLHEASYEMDGDEWKEVLEDVMVIRDDYYHPADEDYADNGDDISMN
Protein: DASH complex subunit ask1 (Associated with spindles and kinetochores protein 1) (Meiotically up-regulated gene 181 protein) (Outer kinetochore protein ask1) (Q9P6S5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. Plays a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:20624975}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:20624975}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:20624975}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis (PubMed:11859360). Localizes to cortical microtubules (PubMed:20624975). During metaphase, localizes to the plus-ends of intranuclear microtubules (INMs) (PubMed:18256284). Does not localize to cytoplasmic microtubules (PubMed:18256284). {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}.
Interaction partners:
- DASH complex subunit dad3
- DASH complex subunit dad2
- DASH complex subunit dam1
- DASH complex subunit spc19
- DASH complex subunit duo1
- DASH complex subunit dad1
- DASH complex subunit dad4
- DASH complex subunit spc34
- DASH complex subunit DAD5
- Spindle pole body component alp14
Sequence:
MNNLEQLERLEQSITLALYEIDANFSKCHRTVTTKILPIVEKYAKNCNTIWDSSKFWKQFFEASANVSLSGVEEPVPVESNPSDQDVMSNSTEADLQLHTKNEHLEKRHSFVGKSDFPDAAVQGDNTKNEDFVQSTPKKMDVSLEDISLDDAALTPIPARMQTPLRKPENNPHTGRSALLHRVLDTNWQVQVTPREPKNLQSQEVMDIDSSPFVSPSPISMKMDMPSLNDRNSSHALSLFAEFEHESYDSINPSGMSPPKTIQFSPHTMGVGSSQQANERSLSLQRKLETLNDSNDSFVKEEDSWEL
Protein: Cullin-8 (Cullin-C) (Regulator of Ty1 transposition protein 101) (P47050)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Ubiquitinates the FACT (facilitates chromatin transcription) complex subunit SPT16 in an MMS1-independent manner. Involved in regulation of Ty1 transposition and protects the genome from Ty1 integration upstream of tRNA genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Note=Recruited to chromatin in response to replication fork stalling.
Interaction partners:
- E3 ubiquitin-protein ligase linker protein MMS1
- RING-box protein HRT1
- E3 ubiquitin-protein ligase substrate receptor MMS22
- Regulator of Ty1 transposition protein 107
- Suppressor of kinetochore protein 1
- Cullin-3
- Ubiquitin-conjugating enzyme E2-34 kDa
- Histone acetyltransferase RTT109
- 25S rRNA
- Protein CRT10
Sequence:
MINESVSKREGFHESISRETSASNALGLYNKFNDERNPRYRTMIAELHEFFHLTLAETITETDVKELECNKEKAAKFRKLMPKMLNNCRELTQRKSYIPYNSEFNGNDEKQKKFQLLHQHQIVLSFQEFCDELAKLIIDAHVLSFLTRCDYSYEIIPKNWTSFYKLFQYVMGAVGPIISYVPVNYPMIRKELGFETLTIFQYYDSKLFECMKSHFGREFSTLVSATIHHYIHMFPITNTMLEKEVPMLRIMSNCNFSIEGLSPKDFYMKTLRQYYCEESNLRPRLETFKNFKVLLTRNALLASLFSPEWVSDANDLFISHLLLNKKSISEYIEIGKDTYDEEKERYFKTETHFSLLMFRNAFEAKNMLSKFKEFCDDAVSEKLKAAYGSNHDTERLFDEVVQLANVDHLKIYSDSIEYHLCNLLGSTSKAIEQYVKYFESHLFIIVRKIKTTKKDLPRDMKIKYLNENLPILRLKFVNLPTFPNFFERSIFRKTILQSDQNSSFIKDILPVYKDSLMELFKQRIITNVSQEDEMRYRDQYQPYLSQFFQPVEVMADLRIKYASFLSFYENIEAAVKFGKTYNENNSKSFFPLIFDRERIPKVFQQSNEVKKNFVLPQEMDDTWNQFLRNYHEQNKVEDSDASKKELYPMWNLHHCEVESPYIIQDGTNLIFELTLFQTCVLTLFNESDHLTLQVISEQTKLAYKDLALVLKSFCNYKILTRDIDNTYSINESFKPDMKKVKNGKLRVVLPRTASLQSSNTGGERTSSAHHEGSNSQWTQELLKACITRSVKSERNGLDYDHLFETVKQQIKGFSVGEFKDALAKLLRDKFITRDESTATYKY
Protein: Neutral sphingomyelinase activation associated factor (A0A0G2K4H2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor
- Sphingomyelin phosphodiesterase 3
Sequence:
MAFTRKRQREQQLQLYSKERFSLLLLNLEEYYFEQHTAFHVQHQGSPEERKIRGSLKICSKSVIFEPDAISQPILKIPLRDCLKIGKHGENGANKHFAKAKSLGISLIFSQVYFIKEHNIVAPYKIERGKMEYVFQLEVSGKVEDVVETLLQLHRASCLDKLGDQMAMITAILQSRLARTSFDKNRFQSVSEKLHMECKAEMVTPLVTNPGHVCITDTNLYFQPLNGYPKPVVQITLQDVRRIYKRRHGLMPLGLEVFCTEDDLCSDIYLKFYEPQDRDDLYFYIATYLEHHVAEHTAESYMLQWQRGHLSNYQYLLHLNNLADRSCNDLSQYPVFPWVISDYSSPELDLSNPATFRDLSKPVGALNPERLERLLTRYQEMPEPKFMYGSHYSSPGYVLFYLVRIAPEYMLCLQNGRFDNADRMFNSIAETWKNCLDGATDFKELIPEFYDEDASFLINSLKLDLGKRQGGQMVDDVELPAWASSPQDFLQKNKDALESSYVSEHLHEWIDLIFGYKQKGSEAIGAHNVFHPLTYEGGVDLNSIEDPDDKVAMLTQILEFGQTPKQLFVTPHPRRITPKFKSLSQASSYNASMTDSPVSPGEESFEDLTEESKTLAWNNITKLQLHEQYKIHKESISFSNMALSSCLLLPGDTTVISSSWDNNVYFYSIAFGRRQDTLMGHDDAVSKICWHNDRLYSASWDSTVKVWSGVPAEMPGTKRHQFDLLAELEHDVSVNTINLNAVSTLLVSGTKEGLVNIWDLTTATLLHQISCHSGTVCDAAFSPDSRHVLSTGVDGCLNVIDVQTGMLISSMASEEPQRCFVWDGNSVLSGSRTGELLVWDLLGAKVSERIQGHTGAVTCIWMNEQCSSIITGGEDRQVMFWKLQY
Protein: Protein canopy-1 (Protein D121) (Q2L6L1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the maintenance of the midbrain-hindbrain boundary (MHB) organizer. Contributes to a positive-feedback loop of FGF signaling in the MHB, enabling the MHB to exert its role as an organizer for the tectal and cerebellar development.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16488878}.
Interaction partners:
- Protein canopy homolog 3
- Protein canopy 4
Sequence:
MSPWIKHICLVLVAAFMLVKTTESKKDEALYCSACMAIADEINYSISQTDPKKMIHVGGFRLKPDGSLTDKKVPLARSETYLTELLEEVCKSMSDYALYENPDTKEKSYKRFAPRDNDGGNFPDFKNFKFDGPESSSALKFACESIVEELEDDIISLFASDSDHVAKTLCSEVSDHCKSSVFQHSEL
Protein: LP01646p (Q8MSU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGSRLIVERFANITDGSIIGMRAPYLRVGGNKQFEMMADQFFVYDASITASLGRVPIWPYTLYFRMPHKCNGNAHNCPSRSHPVWEMVMNELDRRDDPTFDESLPGCHMVDSCSNVASGDQFARLLRHNFNRHYNSNRAPLGLHFHASWLKSKKEYRDELIKFIEEMLGRNDVFFVTNLQVIQWMQNPTELNSLRDFQEWKEKCDVKGQPYCSLPNACPLTTRELPGETLRLFTCMECPNNYPWILDPTGDGFSV
Protein: Protein Wnt-4 (P49337)
Organism: Gallus gallus (Chicken)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Plays an important role in embryonic development (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Wnt inhibitory factor 1
- Porcupine O-acyltransferase.
- Frizzled-6
- Frizzled-2
- Notum, palmitoleoyl-protein carboxylesterase.
- Frizzled-4
- Frizzled-3
- Frizzled-1
- Secreted frizzled-related protein 1
Sequence:
MSPEYFLRSLLLIILATFSANASNWLYLAKLSSVGSISEEETCEKLKGLIQRQVQMCKRNLEVMDSVRRGAQLAIEECQYQFRNRRWNCSTLDTLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGELDKCGCDRTVQGGSPQGFQWSGCSDNIAYGVAFSQSFVDVRERSKGASSNRALMNLHNNEAGRKAILNNMRVECKCHGVSGSCEFKTCWKAMPPFRKVGNVLKEKFDGATEVEQSEIGSTKVLVPKNSQFKPHTDEDLVYLDSSPDFCDHDLKNGVLGTSGRQCNKTSKAIDGCELMCCGRGFHTDEVEVVERCSCKFHWCCSVKCKPCHRVVEIHTCR
Protein: Putative NADPH-dependent methylglyoxal reductase GRP2 (EC 1.1.1.283) (Cytoplasmic antigenic protein 2) (P83775)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Glyoxalase 3
- Lactoylglutathione lyase
- Amine oxidase
- Amine oxidase
- Threonine dehydratase
- L-serine ammonia-lyase
- L-serine ammonia-lyase
- Tryptophan synthase
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS3
Sequence:
MSSSTTVFVSGASGFIAQTLVKQLIEKGYKVVGTVRSNEKGDSLKENLKAAKLQSENFTYEIVKDIAVKGAFDDALKKHPEVTVFLHTASPFHFNVTDIEKELLTPAVEGTNNALQAIKTHGPQIKRVVVTSSYAAVGRFADLADPSIPATEESWNPITWEQSLSNPLAGYVGSKKFAEKAAWDFVEKEKPNFTLSVINPVYVFGPQAFEIKNKSQLNTSSEIINGLLNSKPDSKFDNLTGYFIDVRDVAKAHIVAFEKDSIQGQRLILAESPFSTQSILDLIRKDFPQLDSQLPKGDPSQADAWKKAESKIENEKTRELLGFKFIDFKKSIDDSVAQIIG
Protein: Magnetosome protein MamC (Q2W8S0)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Probably involved in magnetite crystal growth (Probable). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (Probable).
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:16303747, ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:27481925, ECO:0000269|PubMed:28790202, ECO:0000305|PubMed:22846572}; Multi-pass membrane protein {ECO:0000255}. Note=Tightly associated with magnetite crystals (PubMed:12496282). Tagged protein forms straight lines with a punctate pattern extending along most of the cell associated with its inner curvature, in the correct position to be associated with magnetite-containing magnetosomes (PubMed:21414040, PubMed:27481925, PubMed:28790202). In a mamE disruption MamC forms 1-2 foci in the cell (PubMed:21414040). {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:27481925, ECO:0000269|PubMed:28790202}.
Interaction partners:
- Magnetosome protein MamD
- Magnetosome protein MamF
- Magnetite biomineralization protein Mms6
Sequence:
MPFHLAPYLAKSVPGVGVLGALVGGAAALAKNVRLLKEKRITNTEAAIDTGKETVGAGLATALSAVAATAVGGGLVVSLGTALVAGVAAKYAWDRGVDLVEKELNRGKAANGASDEDILRDELA
Protein: mitogen-activated protein kinase (EC 2.7.11.24) (D5GW36)
Organism: Acrobeloides sp. PS-1146
Interaction partners:
Sequence:
GMTAPGPPETRNGVEEVHGQIFEVAPRYVNLSYIGEGAYGMVVSAQDTQTRERVAXKKIXPXXHQTFCQRTLREIKILTRFKHENIINXQEIIRSSSIDQMKDIYIVQCLMETDLYKLLKTQRLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVTDPGRDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDVWSVGCILAEMLNNRPLFPGKHYLDQLNLILAVVGSPSQEDLQCIINEKARSYLLSLPMKPKQSWQRLYPNADPRALDLLEKMLTFNPHKRITIEEALAHPYLEQYYDPNDEPACEEPLTSEMEFDELPKEQLKQLIWEEAENFHHHLQAEQAAMMQ
Protein: Inner nuclear membrane protein Man1 (LEM domain-containing protein 3) (Q9WU40)
Organism: Mus musculus (Mouse)
Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest (By similarity).
Subcellular location: Nucleus inner membrane; Multi-pass membrane protein.
Interaction partners:
- Barrier-to-autointegration factor
- Barrier-to-autointegration factor-like protein
- Emerin
- Mothers against decapentaplegic homolog 2
- Prelamin-A/C
- Delta
- Mothers against decapentaplegic homolog 1
- Lamin-B1
- Lamin-B2
- Mothers against decapentaplegic homolog 3
Sequence:
MAAATAAAAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQQQQQQQQQHRAGGRGNKTRNSNNNNTATAMGGRPGSGDLAYLRSPAGLGRLSASAAESPVAGGSGGAAAVPAAGSKVLLGFSSDESDVEASPREQAGGGGGGGARRDRAALQYRGLRAPPAPPAAGEVTGGHPGERRKPHSWWGARRPAGPEPQPPAAGSDGAAEDADEELADGEDRDPEAEEPLWASRAVNGSRLLPYSSCREHYSDSEEEEEEGEEDGDVAPARQVLKDDSLARHRPRRSHSKPFSALTAKSGGSRQETSVQGGGALAMNDRAAAAGSLDRSRNLEEAAAEPGGGGGGGCGCDPVDSIPRYRAGAKKLAPLLSPPSPDGDSTLESPTGPLLKTNNHIGGGAFGVDSPGLYANSLPPGATAAAAPGTLRINHANHTGSNHTYLKTAYGKPKLCEPEEELLQQFKREEVSPTGSFSAHYLSMFLLTAACLFFLILGLTYLGMRGTGVPEDGGLIKNPFDETFGKIQESEKNLLMSTLYKLHDRLAQIAGDHECGSSSQRMLSVQEAAAYLKNLGPEYEDVFNTSLLWIFKNGKDVGIRCVGYGPEEDLTNITDVQFLQSTRPQMPFWCRFRRAFITVTHRLLLLCLGVVLVCVALRYMRYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQETKDLQPYMPLPHVRDSLIQPQDRKKMKKVWDRAVDFLAANESRVRTETRRVGGADFLVWRWIQPSASCDKTLVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGDHWHLAIQEAILEKCSDNDGIVHIAVDRNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQALTCNTPLKPANKHMNSLSHLRLRTGLANSQGSS
Protein: Neurofascin (Q810U3)
Organism: Mus musculus (Mouse)
Function: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Contactin-associated protein 1
- Contactin-1
- Ankyrin-3
- Gliomedin
- Ankyrin-1
- Syntenin-1
- Ankyrin-2
- Sodium channel protein type 8 subunit alpha
- Receptor-type tyrosine-protein phosphatase zeta
- Ezrin
Sequence:
MARQQAPPWVHIALILFLLSLGGAIEIPMDPSIQNELTQPPTITKQSVKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFRSGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPITQDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTSSSQMVLRGMDLLLECIASGVPTPDIAWYKKGGDLPSNKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPKNLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVSVLDVPPRMLSARNQLIRVILYNRTRLDCPFFGSPIPTLRWFKNGQGSNLDGGNYHVYENGSLEIKMIRKEDQGIYTCVATNILGKAENQVRLEVKDPTRIYRMPEDQVAKRGTTVQLECRVKHDPSLKLTVSWLKDDEPLYIGNRMKKEDDSLTIFGVAERDQGSYTCMASTELDQDLAKAYLTVLADQATPTNRLAALPKGRPDRPRDLELTDLAERSVRLTWIPGDDNNSPITDYVVQFEEDQFQPGVWHDHSRFPGSVNSAVLHLSPYVNYQFRVIAVNEVGSSHPSLPSERYRTSGAPPESNPSDVKGEGTRKNNMEITWTPMNATSAFGPNLRYIVKWRRRETRETWNNVTVWGSRYVVGQTPVYVPYEIRVQAENDFGKGPEPDTIIGYSGEDLPSAPRRFRVRQPNLETINLEWDHPEHPNGILIGYILRYVPFNGTKLGKQMVENFSPNQTKFSVQRADPVSRYRFSLSARTQVGSGEAATEESPAPPNEATPTAAPPTLPPTTVGTTGLVSSTDATALAATSEATTVPIIPTVVPTTVATTIATTTTTTAATTTTTTTESPPTTTAGTKIHETAPDEQSIWNVTVLPNSKWANITWKHNFRPGTDFVVEYIDSNHTKKTVPVKAQAQPIQLTDLFPGMTYTLRVYSRDNEGISSTVITFMTSTAYTNNQADIATQGWFIGLMCAIALLVLILLIVCFIKRSRGGKYPVREKKDVPLGPEDPKEEDGSFDYSDEDNKPLQGSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
Protein: Proton-coupled zinc antiporter SLC30A1 (Solute carrier family 30 member 1) (Zinc transporter 1) (ZnT-1) (Q60738)
Organism: Mus musculus (Mouse)
Function: Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (Probable). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells. In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q62720}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q62720}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6M5}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Note=Localization to the plasma membrane is regulated by cellular zinc status. Recruitment to the plasma membrane from an internal pool is stimulated by zinc while in absence of zinc the plasma membrane pool is endocytosed and degraded (By similarity). Localizes to the basolateral surface of enterocytes (By similarity). Localizes to zinc-containing intracellular vesicles in macrophages (By similarity). Localizes in the cytoplasm and to the ER, Golgi and nucleus membranes in keratinocytes (By similarity). {ECO:0000250|UniProtKB:Q62720, ECO:0000250|UniProtKB:Q9Y6M5}.
Interaction partners:
- Transmembrane channel-like protein 8
- Transmembrane channel-like protein 6
- Zinc transporter 6
- Zinc transporter ZIP1
- Zinc transporter ZIP10
- Zinc transporter SLC39A7
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter ZIP6
- Metal cation symporter ZIP14
- Metal cation symporter ZIP8
Sequence:
MGCWGRNRGRLLCMLLLTFMFMVLEVVVSRVTASLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVMGALVNAIFLTGLCFAILLEAVERFIEPHEMQQPLVVLSVGVAGLLVNVLGLCLFHHHSGEGQGAGHGHSHGHGHGHLAKGARKAGRAGVEAGAPPGRAPDQEETNTLVANTSNSNGLKADQAEPEKLRSDDPVDVQVNGNLIQESDNLEAEDNRAGQLNMRGVFLHVLGDALGSVIVVVNALVFYFNWKGCTEDDFCTNPCFPDPCKSSVEIINSTQAPMRDAGPCWVLYLDPTLCIIMVCILLYTTYPLLKESALILLQTVPKQIDIKHLVKELRDVDGVEEVHELHVWQLAGSRIIATAHIKCEDPASYMQVAKTIKDVFHNHGIHATTIQPEFASVGSKSSVLPCELACRTQCALKQCCGTRPQVHSGKDAEKAPTVSISCLELSENLEKKARRTKAEGSLPAVVIEIKNVPNKQPESSL