wanglab/gogpt-training-data huggingface dataset:
Protein: Cold-regulated 413 inner membrane protein 2, chloroplastic (AtCOR413-IM2) (Cold-regulated 413 thylakoid membrane 2) (AtCOR413-TM2) (F4I1G5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18643950}; Multi-pass membrane protein {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18643950}.
Interaction partners:
- Universal stress protein A-like protein
Sequence:
MASLCLSSSRIVSLHHQKPFLALKLRPRPSNISGLGHSTSVVCFNPLRLSADRQRTATVSARAEKRRKRGSSVVCYATPMLSVHNLQWISTISCVALMFARGTGIHKSFVVPLFALQAPMGIVSWMKGEYGIWAAFLALLTRLFFSFPVELELPFIALLLVIVAPYQVMSIRGKQEGAILSLAISCFLAFQHFSRAGTLQKAFDQNSVLATVAIIGVTVVSFLFLI
Protein: Inner membrane protein YiaB (P11286)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YiaA
- Inner membrane protein YigG
- Probable D,D-dipeptide transport system permease protein DdpC
- Inner membrane protein YgjV
- O-acetyltransferase WecH
- UPF0060 membrane protein YnfA
Sequence:
MKTSKTVAKLLFVVGALVYLVGLWISCPLLSGKGYFLGVLMTATFGNYAYLRAEKLGQLDDFFTHICQLVALITIGLLFIGVLNAPINTYEMVIYPIAFFVCLFGQMRLFRSA
Protein: Paraflagellar rod protein, putative (Q586U8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTQSAQSTTLFQRNKHIYIQEEDKLKDILSDEAFHEKVISWLESTITELDLQFEICDQKLAELQQNISVESGNYWCSKTVIKHCNLHLDVKNISSSGADTEQHATIPEVVHAVSSLQLLKTQPFITPKQKRFIEQCEAELSSVVFEPRELGFISNALRVKLREGSNARSLLGSLAEFQNTIEVLSPDVDKCEQLLEASISNGEMALAEEISERQLKIYERILQLITDQYPIITNHYVESRVNDRRQRWAIFRMADKDITAVIEGKNRQIEACEEDLLKIKEQIENYNNDDTHQRKRYETDRGLSDEFLQKNREQQQGVWNRMFELAREMQQCQVELSKLAQKRRKEIERRLQMEEREAGRRSGHESFLKAVSEHAQKLQNIVTNAIKAKDLATSLNNFVLDGCDTIASKVDKRQNTFSEMLRAIQSHHFKRYSDYYLAASRYLYRKERRLMQLDEEIRDNEIKKELHTESLDVNAKKYVEANKILLLKRRELGHQIVAIRANLDKASEDIEPTLSSLRFAGVEYVHPSEIAKKVNLNRHSTILDYREKVTPSTTFDEKVKVEEEKTLLQIRAAIEQENSERASYRRTQLPMLEAKYRTPLQRQVGALLDRRLNDTPSAGSPSASYPKAVTHPLPGHQKVPGTHGAGGEEPDRAAATLSAKPSHLVSSRRNSLEEMGDGVGGDASTASHGVQLGINDVLRVEGRSLRALYPYKARAPDELTFDEGEVIVCVSRAQEEGWLKGVCNQRTGLFPINYVAPCDEDD
Protein: Double-strand-break repair protein rad21 homolog A (SCC1 homolog) [Cleaved into: 64-kDa C-terminal product (64-kDa carboxy-terminal product)] (Q6TEL1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Double-strand-break repair protein rad21 homolog: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetitive regions. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX gene expression, including that of RUNX1 and RUNX3. May play a role in embryonic gut development, possibly through the regulation of enteric neuron development.
Subcellular location: [Double-strand-break repair protein rad21 homolog A]: Nucleus {ECO:0000250|UniProtKB:O60216}. Nucleus matrix {ECO:0000250|UniProtKB:O60216}. Chromosome {ECO:0000250|UniProtKB:O60216}. Chromosome, centromere {ECO:0000250|UniProtKB:O60216}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before prophase, scattered along chromosome arms. During prophase and prometaphase, most cohesins dissociate from the arms of condensing chromosome, possibl through PLK1-mediated phosphorylation (By similarity). A small amount of cohesin remains in centromeric regions and is removed from chromosomes only at the onset of anaphase. At anaphase, cleavage by separase/ESPL1 leads to the dissociation of cohesin from chromosomes and chromosome separation (By similarity). {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:O93310}.; SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60216}. Nucleus {ECO:0000250|UniProtKB:O60216}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein.
- Structural maintenance of chromosomes protein
- Stromal antigen 1a.
- Nipped-B-like protein B
- Extra spindle pole bodies-like 1, separase.
- Structural maintenance of chromosomes protein.
- Cohesin subunit SA
- Sister chromatid cohesion protein PDS5 homolog A
- Stromal antigen 2a.
Sequence:
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEDNREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFTLNQSRVEEITMREEVGNISLMTDNDFGDFGMDDREMMREENAFGDIIHESSAANLLLEAEPGPAHLPDKTPNLDYDDFGDNNLENSDGGILMDKILSNEDGGGIFDDPPAITDSVMMPQDHGDDDDDFDNFSPAGGPDSPDSGPVEPLPNTTDQTDQTEQTTLVPNEDEAFALEPIDITVKETKAKRKRKLIVDSLKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNGRLLKMFTRCLTPLVPDELRKRRKGGEADSLEDFLKELENPEVPREEVLGHRSDVIDQTIMEEPSMLQASSMEGSRTALDESMMPPPSRQRGLKRKSLETLEKDAVLPPMGVLEQTLQPLDQSVLSHQLEMPQVELPPEDTTNLSRLIPELDLLDEKSKDKDKDDSDEEGEEGQGGDQDQEERRWNKRTQQMLHGLQRVVAKTGAQSISLLELCRNNNKKQAAAKFYSFLVLKKQQAIDLTQTEPYSDIIAAPGPRFHIV
Protein: Anaphase-promoting complex subunit 3 (20S cyclosome/APC complex protein apc3) (Nuclear alteration protein 2) (Nuclear scaffold-like protein p76) (P10505)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Interacts with spindle apparatus, chromosomes, or nuclear envelope, and interconnect nuclear and cytoskeletal functions in mitosis, so the elongation of the spindle in anaphase is blocked.
Subcellular location: Nucleus.
Interaction partners:
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 2
- Mitotic spindle checkpoint component mad3
- Mitotic spindle checkpoint component mad2
Sequence:
MTDRLKCLIWYCIDNQNYDNSIFYSERLHAIEDSNESLYLLAYSHFLNLDYNIVYDLLDRVISHVPCTYLFARTSLILGRYKQGISAVEACRSNWRSIQPNINDSISSRGHPDASCMLDVLGTMYKKAGFLKKATDCFVEAVSINPYNFSAFQNLTAIGVPLDANNVFVIPPYLTAMKGFEKSQTNATASVPEPSFLKKSKESSSSSNKFSVSESIANSYSNSSISAFTKWFDRVDASELPGSEKERHQSLKLQSQSQTSKNLLAFNDAQKADSNNRDTSLKSHFVEPRTQALRPGARLTYKLREARSSKRGESTPQSFREEDNNLMELLKLFGKGVYLLAQYKLREALNCFQSLPIEQQNTPFVLAKLGITYFELVDYEKSEEVFQKLRDLSPSRVKDMEVFSTALWHLQKSVPLSYLAHETLETNPYSPESWCILANCFSLQREHSQALKCINRAIQLDPTFEYAYTLQGHEHSANEEYEKSKTSFRKAIRVNVRHYNAWYGLGMVYLKTGRNDQADFHFQRAAEINPNNSVLITCIGMIYERCKDYKKALDFYDRACKLDEKSSLARFKKAKVLILLHDHDKALVELEQLKAIAPDEANVHFLLGKIFKQMRKKNLALKHFTIAWNLDGKATHIIKESIENLDIPEENLLTETGEIYRNLET
Protein: Small ribosomal subunit protein uS19m (37S ribosomal protein S19, mitochondrial) (Q9US30)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein mL41
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS33
Sequence:
MFWTSVARARSVWKGPNVVDFGVNVQQCIKGNVPIKTAVRSATILPRMVGAQFMVHNGKSYANVKITEDMIGHKLGEFAPTRKAFHYRQTKNR
Protein: Neural cell adhesion molecule 2 (N-CAM-2) (NCAM-2) (Neural cell adhesion molecule RB-8) (R4B12) (O35136)
Organism: Mus musculus (Mouse)
Function: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
Subcellular location: [Isoform Long]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Major prion protein
- Neural cell adhesion molecule L1
- Neural cell adhesion molecule 1
Sequence:
MSLLLSFYLLGLLVRSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIMMPQKSFNATAERGEEMTLTCKASGSPDPTISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTLVCEAEGEPVPEITWKRAIDGVMFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDIEYAPKFVSNQTMYYSWEGNPINISCDVTANPPASIHWRREKLLLPAKNTTHLKTHSVGRKMILEIAPTSDNDFGRYNCTATNRIGTRFQEYILELADVPSSPHGVKIIELSQTTAKISFNKPESHGGVPIHHYQVDVKEVASETWKIVRSHGVQTMVVLSSLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA
Protein: Lysozyme 1 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase 1) (Invertebrate-type lysozyme 1) (cv-lysozyme 1) (P83673)
Organism: Crassostrea virginica (Eastern oyster)
Function: Has antibacterial activity against the Gram-positive bacteria L.garvieae, M.luteus and Enterococcus sp., and the Gram-negative bacteria E.coli and V.vulnificus. Weak antibacterial activity against the Gram-negative bacterium A.hydrophila. No antibacterial activity detected against the Gram-positive bacterium S.iniae or against the Gram-negative bacterium E.ictaluri. Shows some chitinase activity but no isopeptidase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:15364284}.
Interaction partners:
Sequence:
MNGLILFCAVVFATAVCTYGSDAPCLRAGGRCQHDSITCSGRYRTGLCSGGVRRRCCVPSSSNSGSFSTGMVSQQCLRCICNVESGCRPIGCHWDVNSDSCGYFQIKRAYWIDCGSPGGDWQTCANNLACSSRCVQAYMARYHRRSGCSNSCESFARIHNGGPRGCRNSNTEGYWRRVQAQGCN
Protein: Protein THYLAKOID RHODANESE-LIKE, chloroplastic (Q6ETQ7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9M158}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly localized to the non-appressed regions of the thylakoid membrane. {ECO:0000250|UniProtKB:Q9M158}.
Interaction partners:
Sequence:
MAATTTILSSAAPTPLTAPPRARARAPAARRRRLRARDILGAALGLANGGASAALAAPLSYEETLRLSTDSGGGGGGGGGGEFALPDLGLGGVLDFVAQNPLAAAAGVAAVALPLVLAQVLGGASKPYGVVSAAAAYRALVEEPGAQLVDIRPPGDARQSGAPDLREAKKKAAAVPYDGEDKNGFLKKLSLRFKDPENTTLVILDKFDGNSELVAELVTANGYKAAFAVKDGAEGRRGWLSSSLPWTAPKKGFSLSDLIGDGTDGLPVTLGLAAATGLGILAYTEIETVLQFLGSAAIVQLVASKLIYAEDRKRTLKQIDDFFNKKVAPKELVDEIKEIGQALLPSTGTKSQPAITEAAPATAEAAPAAATATAAPPAAPVEETSTEAAPAEPTPLSPYTNYPDLKPPSSPSPLAPAEATKNESESESAATESAPAVNSAPVAEAAPEAAPPAAPRPLSPYPNYPDLKPPSSPSPSAP
Protein: BZIP-type transcription factor (C8VBM8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- MYB family conidiophore development protein FlbD
- C2H2-type domain-containing protein
- FlbE
- C2H2 type master regulator of conidiophore development brlA
- Eukaryotic translation initiation factor 3 subunit D
- Protein fluG
- Developmental regulator flbA
- Conidiophore development regulator abaA
Sequence:
MTSISSRPIPLDLNAMDSLNRQSLAQSASPAGQDTPGMRGSISTDFFKFFGAGGQAKKTTRDGQPAKRRGPKPDSKPALTRRQELNRQAQRTHRERKEQYIRALESEVARLREAYTQEISAANLAVHQHREMANSISEENNMLKEILVAHNINYDAELERRRAERQMGSGFHSSPVGAGSVGSQTGIASLTAHTYSTPPTTVSSGMSPKFNGVEKFDFSSVPDVGPNNQGIATVPCDALAAIDRRPPIQGAGIFEDNPQLQIDFILALESPCRDHTDYLCRRSITEADDEDMPFSGHALMATCPPPSYIANTTSEQTYPHKTYDLPHANLTTLLNLSRQLVTEGQVTPIMALQALKNHEMYTKLTRDDVKLIMDTLENKVRCYGFGAVLEDFELMDCFSSVLGSKVEGSGPVGVAFSRHADETMYS
Protein: Zinc finger protein ZAT4 (Q9SHD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in stress responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- B3 domain-containing protein REM17
- Homeobox-leucine zipper protein-like protein
- Putative F-box/kelch-repeat protein At1g20940
- At1g80245 component)
- 2-oxoglutarate
Sequence:
MERYKCRFCFKSFINGRALGGHMRSHMLTLSAERCVITGEAEEEVEERPSQLCDDDDDTESDASSSSGEFDNQKMNRLDDELEFDFAEDDDVESETESSRINPTRRRSKRTRKLGSFDFDFEKLTTSQPSELVAEPEHHSSASDTTTEEDLAFCLIMLSRDKWKQQKKKKQRVEEDETDHDSEDYKSSKSRGRFKCETCGKVFKSYQALGGHRASHKKNKACMTKTEQVETEYVLGVKEKKVHECPICFRVFTSGQALGGHKRSHGSNIGAGRGLSVSQIVQIEEEVSVKQRMIDLNLPAPNEEDETSLVFDEW
Protein: Interferon phi 3 (Type I interferon 3) (A8E6E3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDLHRVAWLCTFFCFVQVWSLPTNCNLQKNLMKRTYTLLETAGGLFPMQCLDDRVSIPFPQNVFEYNEDQVTGVEKAVYQTLQNIDALFENFGDPDQWDAEKLDDFRGIVYRQIKYSTCIMNKTEVAQDFPSREASLKVYFETISSTLKEKNSSYCAWEIVRSEILRTLEFILKNNSDIML
Protein: Protein lon-8 (G5EGH7)
Organism: Caenorhabditis elegans
Function: Secreted protein that is involved in larval elongation, early adult growth and male tail development.
Subcellular location: Secreted {ECO:0000269|PubMed:17374156}.
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- Transmembrane protein RAM-5
- Cuticle collagen lon-3
Sequence:
MRNSRFCAILAVISAISVSYVLAQRSQQSVIADLGKLIVDNCPPMLCTGLDCAVVTERNGCQLCACPIGSPSRGCDPMPFILWHDLIVNGCPNVTLNSRDPAQKVHRWFRRVNRFTNTDQCEPYIFPYCPELDFNLWRSPRTKQECELYCYSIDEQRKRGII
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1 (EC 2.7.8.11) (Phosphatidylinositol synthase 1) (AtPIS1) (PI synthase 1) (PtdIns synthase 1) (Q8LBA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 5, chloroplastic
- Phosphatidylinositol 4-kinase beta 2
- Phosphatidate cytidylyltransferase 4, chloroplastic
- Phosphatidate cytidylyltransferase 3
- Phosphatidate cytidylyltransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- Phosphatase IMPL1, chloroplastic
- Phosphatidylinositol 4-kinase alpha 1
Sequence:
MAKKERPRPEKLSVYLYIPNIVGYMRVLLNCVAFAVCFSNKPLFSVLYFFSFCCDAVDGWVARRFNQVSTFGAVLDMVTDRVSTACLLVILSQIYRPSLVFLSLLALDIASHWLQMYSTFLAGKSSHKDVKDSTSWLFRLYYGNRIFMCYCCVSCEVLYIILLLIAKNQSENLLNVVVATLTQISPLSFLLALTLFGWSMKQTINVIQMKTAADVCVLYDIEKQQKP
Protein: Reticulocyte binding-like protein 5 (W7FCZ9)
Organism: Plasmodium falciparum (isolate 7G8)
Interaction partners:
Sequence:
MIRIKKKLILTIIYIHLFILNRLSFENAIKKTKNQENNLTLLPIKSTEEEKDDIKNGKDIKKEIDNDKENIKTNNAKDHSTYIKSYLNTNVNDGLKYLFIPSHNSFIKKYSVFNQINDGMLLNEKNDVKNNEDYKNVDYKNVNFLQYHFKELSNYNIANSIDILQEKEGHLDFVIIPHYTFLDYYKHLSYNSIYHKSSTYGKYIAVDAFIKKINETYDKVKSKCNDIKNDLIATIKKLEHPYDINNKNDDSYRYDISEEIDDKSEETDDETEEVEDSIQDTDSNHTPSNKKKNDLMNRTFKKMMDEYNTKKKN
Protein: Sulfotransferase (EC 2.8.2.-) (Q6P2U4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTEAELYSSYKGVLVPSYVHPAESLKYYEDFTFRPDDILIITFPKSGTTWMQEIVPLVVSEGDLTPVLTVPNWDRVPWLEEHRAILLSLEQRASPRIFATHFHHQMMNPSYFKIKPRVLYVMRNPKDVFISSYHFHEMASFLVSPGTQDEFLEKFLDGTIMFGSWFDHVKSWLNAGEQEHILYLCYEDMISDLKASVDKIATFLGKSLSSEVVEKIADHCVFKNMKQNKMSNYSLVPEEFMDQKKSEFLRKGIVGDWKNHFSTAQEQKFNAVYQEKMKDVKFSFPWD
Protein: FI02818p (GEO01603p1) (Sickle) (Q9VVP8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cell death protein Grim
- Peroxisomal targeting signal 1 receptor
- Cell death protein rpr
- Peroxin-19
Sequence:
MAIPFFEEEHAPKSEPSGDQVDSPMAFSIDPGHDQVDFEGPPSAAEELPPPGATSEPVAPPSAEEQLLAWKFLAITMCKVLKQFYQQHKSSGKSSKLKATVQIQPQAQ
Protein: Neurofilament light polypeptide (NF-L) (68 kDa neurofilament protein) (Neurofilament triplet L protein) (P07196)
Organism: Homo sapiens (Human)
Function: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity).
Subcellular location: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}.
Interaction partners:
- Neurofilament medium polypeptide
- Neurofilament heavy polypeptide
- Alpha-internexin
- Superoxide dismutase
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Kinesin light chain 3
- Kinesin light chain 1
- Kinesin light chain 2
- Kinesin light chain 4
Sequence:
MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKDKEEAEEEEAAEEEEAAKEESEEAKEEEEGGEGEEGEETKEAEEEEKKVEGAGEEQAAKKKD
Protein: Histone deacetylase 2 (HD2) (EC 3.5.1.98) (A0A8I6AP99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
Interaction partners:
Sequence:
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAVLELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKEAEDKRTGVEISRLNNRQK
Protein: Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Asparagine-linked glycosylation protein 12 homolog) (hALG12) (Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase) (Mannosyltransferase ALG12 homolog) (Membrane protein SB87) (Q9BV10)
Organism: Homo sapiens (Human)
Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:12217961}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Glc:Glc
- Alpha-1,2-mannosyltransferase ALG9
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- BAR/IMD domain-containing adapter protein 2
- BAR/IMD domain-containing adapter protein 2-like 1
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
Sequence:
MAGKGSSGRRPLLLGLLVAVATVHLVICPYTKVEESFNLQATHDLLYHWQDLEQYDHLEFPGVVPRTFLGPVVIAVFSSPAVYVLSLLEMSKFYSQLIVRGVLGLGVIFGLWTLQKEVRRHFGAMVATMFCWVTAMQFHLMFYCTRTLPNVLALPVVLLALAAWLRHEWARFIWLSAFAIIVFRVELCLFLGLLLLLALGNRKVSVVRALRHAVPAGILCLGLTVAVDSYFWRQLTWPEGKVLWYNTVLNKSSNWGTSPLLWYFYSALPRGLGCSLLFIPLGLVDRRTHAPTVLALGFMALYSLLPHKELRFIIYAFPMLNITAARGCSYLLNNYKKSWLYKAGSLLVIGHLVVNAAYSATALYVSHFNYPGGVAMQRLHQLVPPQTDVLLHIDVAAAQTGVSRFLQVNSAWRYDKREDVQPGTGMLAYTHILMEAAPGLLALYRDTHRVLASVVGTTGVSLNLTQLPPFNVHLQTKLVLLERLPRPS
Protein: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I) (P0C384)
Organism: Oryza sativa (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01351}.
Interaction partners:
Sequence:
MFPMVTGFMSYGQQTIRAARYIGQSFIITLSHTNRLPITIHYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPLVDWRFEKDIKRKQLLNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALSRLPISIMGDYTIQTIRNSTQSKIDEEKSWNSRTITDY
Protein: SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin-conjugating enzyme E2 9) (Ubiquitin-protein ligase 9) (Q95017)
Organism: Caenorhabditis elegans
Function: Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1, Polycomb protein sop-2, and intermediate filament proteins, such as ifb-1. Required for embryonic development, fertility, vulval morphogenesis, inhibition of vulval cell fates, lifespan, and neuromuscular activity.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:25475837}.
Interaction partners:
- Small ubiquitin-related modifier
- SUMO-activating enzyme subunit uba-2
- E3 SUMO-protein ligase gei-17
- SUMO-activating enzyme subunit aos-1
- Ran GTPase-activating protein 2
- Nuclear Pore complex Protein
- Sentrin-specific protease
- Proliferating cell nuclear antigen
- UBC core domain-containing protein
- Asparagine synthetase
Sequence:
MSGIAAGRLAEERKHWRKDHPFGFIAKPVKNADGTLNLFNWECAIPGRKDTIWEGGLYRIRMLFKDDFPSTPPKCKFEPPLFHPNVYPSGTVCLSLLDENKDWKPSISIKQLLIGIQDLLNHPNIEDPAQAEAYQIYCQNRAEYEKRVKKEAVKYAAELVQKQMLE