wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium-transporting ATPase type 2C member 1 (ATPase 2C1) (EC 7.2.2.10) (ATP-dependent Ca(2+) pump PMR1) (Ca(2+)/Mn(2+)-ATPase 2C1) (Secretory pathway Ca(2+)-transporting ATPase type 1) (SPCA1) (Q80XR2)
Organism: Mus musculus (Mouse)
Function: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway (By similarity). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity). Plays a primary role in the maintenance of Ca(2+) homeostasis in the trans-Golgi compartment with a functional impact on Golgi and post-Golgi protein sorting as well as a structural impact on cisternae morphology. Responsible for loading the Golgi stores with Ca(2+) ions in keratinocytes, contributing to keratinocyte differentiation and epidermis integrity (By similarity). Participates in Ca(2+) and Mn(2+) ions uptake into the Golgi store of hippocampal neurons and regulates protein trafficking required for neural polarity. May also play a role in the maintenance of Ca(2+) and Mn(2+) homeostasis and signaling in the cytosol while preventing cytotoxicity (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P98194}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:19793975}; Multi-pass membrane protein {ECO:0000255}. Note=During neuron differentiation, shifts from juxtanuclear Golgi position to multiple Golgi structures distributed over the neural soma with a predominance in the apical dendritic trunk. {ECO:0000269|PubMed:19793975}.
Interaction partners:
Sequence:
MKVARFQKIPNVENETMIPVLTSKRASELAVSEVAGLLQADLQNGLNKSEVSHRRAFHGWNEFDISEDEPLWKKYISQFKNPLIMLLLASAVISILMRQFDDAVSITVAIVIVVTVAFVQEYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVDLSVDESSLTGETAPCSKVTAPQPAANGDLASRSNIAFMGTLVRCGKAKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVSLAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEMTVTHILTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNTLMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMKGAYEQVIKYCTTYNSKGQTLALTQQQRDLYQQEKARMGSAGLRVLALASGPELGQLTFLGLVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAIAIASRLGLYSKTSQSVSGEEVDTMEVQHLSQIVPKVAVFYRASPRHKMKIIKSLQKNGAVVAMTGDGVNDAVALKAADIGVAMGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLATLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKILVSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCSNKMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVSEIIKKVERSREKVQKNAGSASSSFLEV
Protein: Lysine-specific histone demethylase 2 (EC 1.-.-.-) (Q10135)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the SWM histone demethylase complex that specifically demethylates H3K9me2, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Has a role in regulating heterochromatin propagation and euchromatic transcription. Also has a gene activating role.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16990277}.
Interaction partners:
- SWM histone demethylase complex subunit phf2
- Lysine-specific histone demethylase 1
- SWM histone demethylase complex subunit phf1
- Uncharacterized RNA-binding protein C23E6.01c
- Histone H3.1/H3.2
- Switch-activating protein 1
- Squalene synthase
- Silenced mating-type M-specific polypeptide Mi
- JmjC domain-containing protein 4
- RbAp48-related WD40 repeat-containing protein prw1
Sequence:
MPLGRSSWICCAKYFVNTKSRFNEILPPRFTLIVSFYSMNTSENDPDGHYDFPEMTEHHSDRASSYANANNVNSTQPQLVSSEQALLAILGGGLQSITPNSVNQNAYSRSTYRTDGGLNSQPVSSLNNQWGNYNPAFLPSRYDSSFHPYTISQAANQPFPQHLLGNSNAGVAQQSGMRTIGLPPTVGSSFPQQKSSTYENFFDANSPSSQQFPSTYPSRSQNPLSSSGDGSTAIHAGPIQHQNSNAFSNYPYPLDASHLSSQQLLSMYRDQVSHGVTPSTFRNHESFMPTQLVSATELSKSVDNAVLPIPPTTAPAVVSPPASSFPLMSSAATSGNISSPALFDSELGARPEGSVAIEPSRVLLQWSSQSSSHTIPSAGASIPTSSLKSFFEHAAEAARKCNLDPRALESFEQHMLSDRLHDPVVLFHYFQIRNSICWLWIKNPTHAISRVEAQGVCVDRCLFQLASLAYEFLVRYGYINYGCLSFDSSFTNETNTGTTSSSASKQKTIAVVGAGLTGLICARQLTGLFSQYSSSFLSKNELPPKVIILEAKERTGGRIYSRALPVSHTSATQINHHTSNSNSISSNSTSLNPKDVTDPSHIPSAIDLGFQFLFSPMDDILLNLLNKQLGIEVTEMTGSDLVYDETDTKVLDMVEVKKLNILWEKLLEYVSVCFFINVEESVRISWISQFQLFIDEMFPDHLSKSLSLNASHEFSFKKTMLILIDEVSSYAKLGNSQKKFLIWCFKVAELDDTLYPLNTVDTDFSKDILIPKVARRGLSQLPWALQSYPSPLNIHYEKFVSKVTIENDKCTLDCKDNSSYEVDQVVIACSPSHFSSNIEFSPGLPNFVTENIKSIDFKPGKKVILRYAAAFWRKNIRSFGIIPKSLSQEMNNDENDGKSCFVLRIWNMLPETGVPILVADINPQMTSSSSNETSHLIQELHSLIVDHFQNDSNSSADLLDAWVTNWSRNGVYDGLNSYPNFANDKQQYEKRFRQSQLSYNLGRLHIAGDYIFSCVGCRTLQRSFLSGLSVCTGIIDSLAPISLTIPIIGETSRKELDQFLRNSKVNNFDPNAEAQRHLSYQARYRLKKQERLDEHKEEQEQLVTELLGYLPEPPSKPNANPFLLYQKMQWHVCRALADEDKRRLTGDSTAKATINETRAKLGKTWRQLDDLGKKPWIDEIAAQREAYAGKILRYQRLTKEYEMRAEQIRNDYAAKCQDEPIPDDEARLFMQAQREEEQRKQTQDDNISKSREASDEEYHDDGSSDSGYNGTRY
Protein: Gap junction protein (Q9R140)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
Sequence:
MDWGTLHTVIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLTFVSTSALLVAMHVAYYRHETARKFIRGEKRNEFKDLEDIKRQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTVFMISASVICMLLNVAELCYLLLKLCFRRSKRTQAQRNHPNHALKESKQNEMNELISDSGQNAITSFPS
Protein: Aspartate aminotransferase (EC 2.6.1.1) (A0A140VK69)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Protein: Doublesex- and mab-3-related transcription factor dmd-3 (Doublesex-like 3 protein homolog) (Q9XWN9)
Organism: Caenorhabditis elegans
Function: Transcriptional activator which promotes male-specific development. Acts partially redundantly with the transcription factor mab-3 to coordinate tail tip cell fusion and retraction and thereby regulate male tail tip morphogenesis. This is most likely through the regulation of downstream effectors such as eff-1. May also negatively regulate the expression of other proteins implicated in male tail morphogenesis including nhr-25, vav-1 and arl-1 in tail tip cells. In males, plays a role in the development of ray A-neurons by negatively regulating the activity of the transcription factor ast-1. Plays a role in the male-specific differentiation of PHC sensory neurons into densely connected hub sensory neurons. Plays a role in male mating behavior.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. Perikaryon {ECO:0000269|PubMed:22069471}.
Interaction partners:
- NAB transcription cofactor mab-10
- Sex-determining transformer protein 1
Sequence:
MNIEEILPELFGEKRVYYCQRCLNHGLREKRKNHKLSCTFRFCQCSNCIMVERRRQLNSRLMQIDGSRDEKPMTTLTMALTCSEEDQMECTSQSETTNESSGEDKDDGKPKERRPNCQRCAQHSVVNRLKGHKRACPFRDCFCAKCQVVVERQKLMADQIKLRRRQKREKNNLNSEREAPIAHSMTPSPIDTVTTTTTPTSETSTPMCLKCAQQVIGYQQLLSLLDPSATLQDPMITLSAVLSACPHKNE
Protein: Galectin-16 (A8MUM7)
Organism: Homo sapiens (Human)
Function: Binds lactose with high affinity. Strong inducer of T-cell apoptosis.
Interaction partners:
Sequence:
MSFLTVPYKLPVSLSVGSCVIIKGTLIDSSINEPQLQVDFYTEMNEDSEIAFHLRVHLGRRVVMNSREFGIWMLEENLHYVPFEDGKPFDLRIYVCHNEYEVKVNGEYIYAFVHRIPPSYVKMIQVWRDVSLDSVLVNNGRR
Protein: Cadherin-8 (P55286)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
- Catenin delta-1
- Catenin alpha-2
- Cadherin-12
- Catenin alpha-1
- Junction plakoglobin
- Cadherin-20
- Cadherin-4
- Cadherin-7
- Cadherin-13
Sequence:
MPERLAEMLLDLWTPLIILWITLPPCIYMAPMNQSQVLMSGSPLELNSLGEEQRILNRSKRGWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDVTGDIHAIKRLDREEKAEYTLTAQAVDWETSKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGIIRLRKPLDFETKKSYTLKVEAANVHIDPRFSGRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNITIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHYFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIIISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEAYVLPIGLSMGALIAILACIILLLVIVVLFVTLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET
Protein: Protein bicaudal D (P16568)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein is essential for differentiation. It may play a role in localizing of Nanos (a maternal determinant) activity in oocytes. During oogenesis, plays a specific role, together with Rab6 but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in oskar mRNA localization and in the anterodorsal secretion of grk. Plays a role in the biogenesis of annulate lamellae containing nuclear pore complex components.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Egalitarian, isoform B
- Ras-related protein Rab6
- Dynactin subunit 2
- Dynein light intermediate chain
- Dynactin subunit 1
- Maternal effect protein oskar
- Lissencephaly-1 homolog
- Dynein heavy chain, cytoplasmic
- FI20148p1
- Dynactin subunit 1
Sequence:
MSSASNNGPSADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEGGQKKDELEQQLRALISQYANWFTLSAKEIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDHKTDDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRSEGGDALEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDTMSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEMEMDREMRHVRRPMPAQRGTSGKSSFSTRPSSRNPASSNANPF
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (A0A8I6AVY6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYNVITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVNVGDIVIIKGKEFIPADTVLLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLHLHYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGHVPEPEDYGCSPDEWQSSQFGDEKTFNDPSLLENLQNNHPTAPIICEFLTMMAVCHTAVPERDGEKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSSRKRMSVVVRTPSGKLRLYCKGADTVIYERLAESSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFEEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCRLLRRNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWVGLLSIPVASLLLDVLYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
Protein: Kelch-like protein 7 (Q8IXQ5)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Subcellular location: Nucleus {ECO:0000269|PubMed:16918702}. Cytoplasm {ECO:0000269|PubMed:27392078}. Note=Colocalizes with CUL3 in punctate structures at the perinuclear region of the cytoplasm. {ECO:0000269|PubMed:27392078}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Kelch-like protein 9
- Gigaxonin
- Ectoderm-neural cortex protein 1
- Kelch-like protein 12
- Kelch-like protein 13
- Kelch-like protein 20
- Kelch-like protein 21
- Kelch-like ECH-associated protein 1
Sequence:
MAASGVEKSSKKKTEKKLAAREEAKLLAGFMGVMNNMRKQKTLCDVILMVQERKIPAHRVVLAAASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPFMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVDGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIRCPFEKRRDAACVFWDNVVYILGGSQLFPIKRMDCYNVVKDSWYSKLGPPTPRDSLAACAAEGKIYTSGGSEVGNSALYLFECYDTRTESWHTKPSMLTQRCSHGMVEANGLIYVCGGSLGNNVSGRVLNSCEVYDPATETWTELCPMIEARKNHGLVFVKDKIFAVGGQNGLGGLDNVEYYDIKLNEWKMVSPMPWKGVTVKCAAVGSIVYVLAGFQGVGRLGHILEYNTETDKWVANSKVRAFPVTSCLICVVDTCGANEETLET
Protein: Something that sticks like glue, isoform A (Q9XZ21)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD24014p
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor 73
- Cleavage and polyadenylation specificity factor subunit 4
- Probable cleavage and polyadenylation specificity factor subunit 2
- polynucleotide adenylyltransferase
- Factor interacting with poly
- Symplekin
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Stromalin-2
Sequence:
MSVHYKFKSTLNFDTITFDGLHISVGDLKREIVQQKRLGKIIDFDLQITNAQSKEEYKDDGFLIPKNTTLIISRIPIAHPTKKGWEPPAAENAFSAAPAKQDNFNMDLSKMQGTEEDKIQAMMMQSTVDYDPKTYHRIKGQSQVGEVPASYRCNKCKKSGHWIKNCPFVGGKDQQEVKRNTGIPRSFRDKPDAAENESADFVLPAVQNQEIPEDLICGICRDIFVDAVMIPCCGSSFCDDCVRTSLLESEDSECPDCKEKNCSPGSLIPNRFLRNSVNAFKNETGYNKSAAKPAAVKNEEKPPVEKEVEKKPVAEVEPEETEVKPEKQKESETNGSNPPKSESPEPPATTEPSQKEKDKYDSDYEDNITIKMPQPAADSTTVPSKRSPSYSHRSESSHRRDRSDYVSDHDHKHQRPSKSESVNKDRSLLPLPIGTLPSYQGHMMAESEEARRSSAYKPPYMQMQRGPPPMHMMSHHMPAYNNGFNNMGQRPPLSYVPYQNQSVHPMRAPYGSAGGGMNMNMSQPFQSPNLASIYQGVAAKVGSGPIDDPLEAFNRIMKEKERKKVDRFRSSDRHRSRSPDRQRHRFKSPMYEKDNSRDNLKDKRPRSRERKREHSYERHIRHPRSSRQPNDGSKSPGGRIKRSGHRRSASPKPGYKSDYRDKPYNKPSAPKTEAVEPPPPGFEPLQLTDEDGYRNKHPTSSEASQSSKGDSSKKRGENRHEEAPRKRHRSRSISKEPKPNDSNYRSLTPPAKITTPKMTAAQLRQRESSPKTPEKSHDDYLTAKARIMASQPVINDTEMETNVGKENKAKSPLSKDRKKKKKDKDKAERKKNKKDKRAKKEKGDRQKKSSSVNRSDSDINNSSLMNESNYKVLSPRAQSPSIEINAAQLSPTHNATENVNPKSHSILTVGAASDDNLGPRSKLSEANSVNLSKWEIDENILGLEDSSKKAAGASDDPSEITSDVLRKAENAIFAKAINAIRPMEFQVIINSKDNSKDRSVVRSDKDRSSSPRRNNSSRSVKDRLGTKISNDRSRSRDKSKGRRRAARSSDDDANRGRSDRHGSRKRDNRSRDRAAPSEKRQERSYKRSSPEDDKLRRQNKEQSESKHGKHDQNNSDDSDRRAAKNTKSSDSRVVSSVTAVVAPPKPCRPDNPFRKFVDTSSSSSLVVKYDNTIQKEGASSDNGMEHRKQRDKKLKKHSKYSSTDSLKSEKRKDPKSKKKSKILKKKKKSKK
Protein: Nudix hydrolase 14, chloroplastic (AtNUDT14) (EC 3.6.1.21) (ADP-sugar diphosphatase) (AtASPP) (Q9SZ63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use ADP-glucose, ADP-mannose and ADP-ribose as substrates. Regulates the intracellular ADP-glucose levels linked to starch biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16774931, ECO:0000269|PubMed:18815383}.
Interaction partners:
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Probable starch synthase 4, chloroplastic/amyloplastic
- Nudix hydrolase 23, chloroplastic
- Nudix hydrolase 1
- Alpha-glucan phosphorylase 1
- Alpha-glucan phosphorylase 2, cytosolic
- Phosphoglucomutase, chloroplastic
- ADP-glucose pyrophosphorylase family protein
- ADP-glucose pyrophosphorylase family protein
Sequence:
MAGFTLLPSRLLAFPSRALPRRLHHHHAKLILRCKMSSSSSSLTQSITLPSQPNEPVLVSATAGISSSDFRDAIDSSLFRNWLRNLESESGILADGSMTLKQVLIQGVDMFGKRIGFLKFKADIFDKETGQKVPGIVFARGPAVAVLILLESDGETYAVLTEQVRVPTGKIVLELPAGMLDDDKGDFVGTAVREVEEEIGIKLKKEDMVDLTAFLDPSTGYRIFPSPGGCDEEMSVFLYRGQVEKETIRQLQGKETGLREHGEFIKVRLIPYRELWRKTADAKVLMSIGLYEMAQREGLVSSQRLKPNS
Protein: Dihydrolipoamide acetyltransferase, putative (EC 2.3.1.12) (Q38C09)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- pyruvate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- 3-methyl-2-oxobutanoate dehydrogenase
Sequence:
MRRSLAFLVNFSPIYMPALSPSMDSGIIVEWKKKVGDLVKENDVFCTIQTDKAVVDFTNTFDAGYLGKIFRQNGETVAVASTIAAMVEESQDVAKLADYTLKDVEPGNVDEEAVAAPVSTTTTTTKTPKPAGGKIRYGGSLDEAVAASGPGVMRIAARLDKAALEAITPTGRGGRFTKADFVGQPGFDYEKAAPAPKGSSSSFTNASRECCAENTNGAVGSSAVVKSFPVYNFKVSDTTLLQQLLNSMPTPKAKGAAVGK
Protein: Neurotrophin-4 (NT-4) (Neurotrophin-5) (NT-5) (Neutrophic factor 4) (P34131)
Organism: Rattus norvegicus (Rat)
Function: Could serve as a target-derived trophic factor for sensory and sympathetic neurons.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P34130}.
Interaction partners:
- NT-3 growth factor receptor
- High affinity nerve growth factor receptor
- BDNF/NT-3 growth factors receptor
- Tumor necrosis factor receptor superfamily member 16
- Neurotrophic factor BDNF precursor form
- Beta-nerve growth factor
- Glial cell line-derived neurotrophic factor
- Sortilin
- Neurotrophin-3
- Ciliary neurotrophic factor
Sequence:
MLPRHSCSLLLFLLLLPSVPMEPQPPSSTLPPFLAPEWDLLSPRVALSRGTPAGPPLLFLLEAGAYGEPAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKAESAGEGGPGVGGGGCRGVDRRHWLSECKAKQSYVRALTADSQGRVGWRWIRIDTACVCTLLSRTGRA
Protein: DNA packaging ATPase P9 (Protein P9) (P27381)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: Together with the packaging efficiency factor P6, forms the external part of the portal vertex that is embeded in the capsid and which plays critical roles in genome packaging and genome ejection. Both proteins multimerize as a single ring-shaped heterdodecamer arranged around a central channel.
Subcellular location: Virion. Note=Component of the capsid. Localizes at the unique vertex of the capsid, which extends to the internal membrane via two small integral membrane proteins, P20 and P22. {ECO:0000269|PubMed:25514469}.
Interaction partners:
Sequence:
MTIRMPNDRQRILVLGKTGTGKTCAAVWHLSQKDFKRKAWIVLNHKGDDLIDSIEGANHVDLNFRPKKPGLYIYHPIPDVDDAEVTQLLWDIHAMGDIGVYVDEGYMIPNRDPAFQALLTQGRSKKIPMIILSQRPVWLTRFAISESDFFQIFQLGDQRDRQTVQGFVPVDLEKLMQAPVNTVPALKKFHSIYYDVGANNCVIMTPVPTADAVLARFDLGKKRKQTL
Protein: CDC50-related protein CDC50.1 (S7WII9)
Organism: Toxoplasma gondii (strain ATCC 50853 / GT1)
Function: In tachyzoites, required for the cellular trafficking of guanylate cyclase GC and UGO to the cell membrane. May play a role in the folding of the GC P-type ATPase-like domain to sense vacuolar changes in phosphatidic acid and pH levels which trigger parasite egress.
Subcellular location: Membrane {ECO:0000305|PubMed:30742070}; Multi-pass membrane protein {ECO:0000255}. Note=In intracellular tachyzoites, localizes to the apical cap, to the cytoplasm in disperse foci and to the residual body. {ECO:0000269|PubMed:30742070}.
Interaction partners:
Sequence:
MGENSTTGLRGQADVSQFSDAAVEPTLSSPPTGQRQQSLPLFGEETCSISSAPSVGGGGGWPFQRQGSSRLTSRGTSLSSCSDAGSGLGALRQREDSFPEYHGVGLPLGGKYALDGTGLVLAPRVPFIFSHQLPSLTGLDEAGFSDTRKVPSTYQALAARFVHQVHQEAGNGMYPLWSAGVVLRLCLLGALFFVSVGAWLIFEDEQHVECKLNYAEKTLQEGSSRYLLKGISSAHCTREVNELKGEEISVYAEMGHFFQNDAQVLWSRNDRQLAGKIFTDPKDVRECEPLATAVVGNVTKVLHPCGALAWAVFTDKYQFLEGTPEGDNDQVPMKPIPLNQTQAVLLHSWPWQDMYKNPPAEDRAAVLDKVYFWMSPVDNDDGEDMYKTREEARAELLMDRLNYEEAGEMVENGHFIQWMQTAALGTFRKLYGSLEGPLKLPVSAHITVMYDVSSWKGKKAIVLVQKSRLGGRSLFIGIAYLSFGCLLTMLVFYMLWKKWQYRREGEEIRDLRWQTKTRGSKKTK
Protein: Carboxysome shell protein CcmK2 (Carbon dioxide-concentrating mechanism protein CcmK2) (Q03511)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:25117559, ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:31048338}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:25117559}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome assembly protein CcmM
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell protein CcmP
- Ribulose bisphosphate carboxylase small subunit
- Light-independent protochlorophyllide reductase subunit N
Sequence:
MPIAVGMIETLGFPAVVEAADAMVKAARVTLVGYEKIGSGRVTVIVRGDVSEVQASVSAGLDSAKRVAGGEVLSHHIIARPHENLEYVLPIRYTEAVEQFRM
Protein: Vacuolin-A (O15706)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endosome membrane; Peripheral membrane protein. Lysosome. Note=Post-lysosome.
Interaction partners:
Sequence:
MIEGSGSKTPKRNSDEISVKSLSIHEANTLSSEHEHESGNEELTLSQIVIRSDFANESSERQSKIILDRFNQGIGKNSAFTDSPALGRGLSRVDVSYFVMGHRNQVAELYDPRGQRFSTVLTPDPTVNIKYVGPVSKTAHYFGAYGKHVLNVPAGHYAKAFSKNRPVLYGEGPHVIIDPTFQFDENNGFVNQQEPFIEHSTINILRIPAGKIAKVWIGTQPHILESRRDPYVFVDAQFKLVSPDGAKKAQLFESSSCTFVEHGSIKRIIPHTGEVAITYNNGILTIIPTPKDGKPVIIDSPTHNFEGFISTSLQTCLFPSKETKQQALADNKSALADEINLKIFQTRDSLRVGVVLVVAFKIVDPELAITKLGKEGIINHIENVSFADMGKAIQLSTLQEIMYFNSIKPGQATNDDSVQTIQDRVKSHLARDLFDYGVELSRLQIETMKVLDTEIAKKLAGQSVTSAEFTTKQATLVKEYDIKTTEARLKAETDNIALEQRNKAIISESQAKLSSAQREAESLLITAEAQKKASELQGELYTKYPILAEIELARIKAEALKNATLYITPQDAGAFMNSPLVYFDKMMNANNTIQQKKN
Protein: Zinc finger CCCH domain-containing protein 12 (AtC3H12) (Q9LQM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Receptor-like protein 48
- LOW protein: zinc finger CCCH domain protein
- Zinc finger CCCH domain-containing protein 59
- Zinc finger CCCH domain-containing protein 46
- Zinc finger CCCH domain-containing protein 51
- Zinc finger CCCH domain-containing protein 55
- Zinc finger CCCH domain-containing protein 62
- Zinc finger CCCH domain-containing protein 56
- Zinc finger CCCH domain-containing protein 1
- Zinc finger CCCH domain-containing protein 54
Sequence:
MSHHRRDSGGDVVHVIPTNNPPPDNWFPNLGDSAVWATEDDYNRAWAMNPDNTSGDNNGPPNKKTRGSPSSSSATTTSAASNRTKAIGKMFFKTKLCCKFRAGTCPYITNCNFAHTVEELRRPPPNWQEIVAAHEEERSGGMGTPTVSVVEIPREEFQIPSLVSSTAESGRSFKGRHCKKFYTEEGCPYGESCTFLHDEASRNRESVAISLGPGGYGSGGGGGSGGGSVGGGGSSSNVVVLGGGGGSGSGSGIQILKPSNWKTRICNKWEITGYCPFGAKCHFAHGAAELHRFGGGLVEEEGKDGVSPNPDTKQTVQNPKGLSDTTTLLSPGVPHNADASYHTGVALQRASSAVTQKPGIRTHQKWKGPAKISRIYGDWIDDIE