wanglab/gogpt-training-data huggingface dataset:
Protein: NAD(+) kinase (EC 2.7.1.23) (Unknown transcript 1 protein) (P21373)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors.
Interaction partners:
- ATP-NADH kinase YEF1
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- NAD-dependent histone deacetylase HST3
- NAD-dependent histone deacetylase HST4
- NAD-dependent histone deacetylase SIR2
- NAD-dependent protein deacetylase HST1
- NAD-dependent protein deacetylase HST2
- NAD-capped RNA hydrolase NPY1
Sequence:
MKENDMNNGVDKWVNEEDGRNDHHNNNNNLMKKAMMNNEQIDRTQDIDNAKEMLRKISSESSSRRSSLLNKDSSLVNGNANSGGGTSINGTRGSSKSSNTHFQYASTAYGVRMLSKDISNTKVELDVENLMIVTKLNDVSLYFLTRELVEWVLVHFPRVTVYVDSELKNSKKFAAGELCEDSKCRESRIKYWTKDFIREHDVFFDLVVTLGGDGTVLFVSSIFQRHVPPVMSFSLGSLGFLTNFKFEHFREDLPRIMNHKIKTNLRLRLECTIYRRHRPEVDPNTGKKICVVEKLSTHHILNEVTIDRGPSPFLSMLELYGDGSLMTVAQADGLIAATPTGSTAYSLSAGGSLVCPTVNAIALTPICPHALSFRPIILPESINLKVKVSMKSRAPAWAAFDGKDRIELQKGDFITICASPYAFPTVEASPDEFINSISRQLNWNVREQQKSFTHILSQKNQEKYAHEANKVRNQAEPLEVIRDKYSLEADATKENNNGSDDESDDESVNCEACKLKPSSVPKPSQARFSV
Protein: Selenocysteine lyase (EC 4.4.1.16) (C9JNL5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIV
Protein: Synaptopodin (Q9Z327)
Organism: Rattus norvegicus (Rat)
Function: Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11595771, ECO:0000269|PubMed:9314539}. Cell junction, tight junction {ECO:0000269|PubMed:9314539}. Perikaryon. Cell projection, dendritic spine {ECO:0000269|PubMed:9314539}. Postsynaptic density {ECO:0000269|PubMed:9314539}. Synapse {ECO:0000269|PubMed:9314539}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N3V7}. Note=Localized at the tight junction of cells. In brain, localized to the postsynaptic densities and in the perikarya. Associated with dendritic spines of a subset of synapses (PubMed:9314539). {ECO:0000269|PubMed:9314539}.
Interaction partners:
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- CD2-associated protein
- Alpha-actinin-4
- Actin, cytoplasmic 1
- Nephrin
- Podocin
- Actin, cytoplasmic 2
- Podocalyxin
- Wilms tumor protein homolog
- Dendrin
Sequence:
MLGTHFPPPPLGPSEGRAAPCTFQIPDGSYRCLALEAEESSSEDGLQGEVRLVDLEEEGTSKSRVNHGTPPLSRAPAIIQPSSCCREARGGFQHSDKPSREWDVVQARKVMTASVSSSPVPRVAQKPALGRSTSFTEKDLKEAKERSQRIAAQLTTPPSSNSRGVQLFNRRRQRVNEFTLESRGQRSPKLSQEALQTGHPSSPIGHAPGLSVNPTSPSKPGSPKHSSSQSPSRGVPGHIMEGYSEEASLLRHLEKVASEEEEVPLVVYLKENAALLTANGLHLSQNRETQQSSPNPPETEEVPSPAADINQNPSSPNATLTTAASNSHHNQPTADVNQNPPATITPVQQNSSETQCSPNGTLDSKPNTPSADDGQRPVPAEEVRSSILLIDKVSAPPSAASPFSREATPLSSSGPPAADLMSSSLLIGMQPSTLVASAEQEVSGHAAVTTPTKVYSEVHLTLAKPASVVNRTARPFGMQSPGTTSQIEQSPMMGRRHFGEKAWAPPASSMADRSPQPQRHIMARSPMVERRLVGQRSPVVERRPLGNFTPPPTYAETLSTAPVASQVRSPPSYSTLYPSSDPKPPHLKGQVVPANKTGILEESMARRGSRKSMFTFVEKPKVTPNPDLLDLVQTADEKRRQRDQGEVGMEDEPFALGAEASNFQQEPIARDRSGPAAAEETVPEWASCLKSPRIQAKPKPKPNQNLSEASGKGAELYARRQSRMEKYVIESSGHAELARCPSPTMSLPSSWKYTTNAPGGFRVASLSPARTPPASLYHGYLPENGVLRPEPTKQQPHQMRPSLYALSPVKEPAKISSRATSSRASSRTVSPRAASPAKPSSLDLVPNLPRAGLPPSPALPRPSRSSPGLYNAPVQDSLQPTAVSPTYSSDISPVSPSRAWSPRAKQAPRPSFSTRNAGIEAQVWKPSFCFK
Protein: Dermorphin-1 [Cleaved into: Deltorphin (Dermenkephalin); Dermorphin] (P05422)
Organism: Phyllomedusa sauvagei (Sauvage's leaf frog)
Function: Dermorphin has a very potent opiate-like activity. It has high affinity and selectivity for mu-type opioid receptors.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MSFLKKSLLLILFLGLVSLSVCKEEKRETEEENENEENHEEGSEMKRYMFHLMDGEAKKRDSEENEIEENHEEGSEMKRYAFGYPSGEAKKIKRVSEEENENEENHEEGSEMKRYAFGYPSGEAKKIKRESEEEKEIEENHEEGSEMKRYAFGYPSGEAKKIKRESEEENENEENHEEGSEMKRYAFGYPSGEAKKM
Protein: UDP-glucose:Glycoprotein Glucosyltransferase (G5EF14)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Calnexin
- Calreticulin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3
- BPI2 domain-containing protein
Sequence:
MRLTHFLLFLANLKFCWNDNSINVRLNAKWRSSSILAEISEYIGKENPEAFWNFVNSVNQEIDETSNKNDSIRNKYDFGMSVANNILGPFEMKLLRFSLATRSISPRVQAHEQIGMEFKPEKCSFSFFVYGGQAGCQLSELNLNNYDDNNLKIFSFDHIYPVQSTAEKTILIYGELGTYELKNLLLEAQSLIEKHKNLRFVVRHFSRFSDQKPSLSGYGVELALKNTEYKAVDSSSTNKLDEPENLHGLNFKILKNRHLELQNELESLRENLEKQGEIVPLKQWQLKDLGFKTCQKLKSLTEIREMEILLQDFPTHARVTSHQNLNETLQRSIQKGQETLEAKGIESGTNILAINGRVIAKGDSFVDLFALMEKVEEEKKMVNEFVKGFGNSETEEFERINIPKMLTLVDLSSVKLSEHAFDYSIAEPVYLNDLESTRSPYKSLMLMLQPFPPGQIRPISRNIFNLIMFLDPFDSDDRVFDDVIRNFQTGIHIRFGFVPILDEAKYGKSIEEAVDSMIVPPTKKVFWKSKDSLINALKKGSRFVAEAGLTQLPLVLLNGYPLDVTSIERFESSLTQNIQKQTTRLQLALLHGLIEDSVQIDRWWFEKKTNPDIIQRLNQRITTAFNNKEFLNISRRSIQFLKNVHYFSEESDTVLANADVTTWIIADFENPSNRLFATKAIRSIASQKNNKIALIPNPSSSRSNDNPCSFNFENVGPNSDMTILSKIESFCMKNINLSPLDIGVNPGETVVVSNGLLIGPLAGRTELLKTDDFNYLDTFWKEKGATKAATFFNENTVYDVTISFYCSIAKKFKEDQQRMDFDEFMESGNGNTIIFPPIDSTNSTITVTWIANPVSREAQQIISVVKILQRITNSRIEIIFNPSADIQEMPIKRFYRFVANEKLLFNEDGSMENHSVVFSNLPQKQLLTMSLETNDAWMIEVKKAEYDLDNILLETASEDVEAVYSLEHILVEGTSRKMSGEASDGLEVELSSGGKNYDTIVMLNLGYFQLKAEPGVWNLHLRNGHSADEHKIVTIDSIPVENDIQIVVDSFSGKWVELSVEELTEPKESDDELSIESLLNSAKNYFASPEPSEVINVFSLASGHLYERFMRIMMTSVLNNTKTQKVKFWLLKNYLSPKFKETIPKLAEFYKFEFELVEYKWPKWLHKQTEKQRVMWGYKILFLDVLFPLNVDKIIFVDADQVVRADLQELMDFNLNGAPYGYVPFCESRTEMDGFRFWKSGYWKNHLMGRKYHISALYVVDLKAFREFSAGDRLRGRYDSLSADPNSLSNLDQDLPNNMLHEVPIKSLPQEWLWCETWCDDGSKEKAKTIDLCNNPLTKEPKLNSAKRIIKEWTEYDSEISKVLNSADINTPSPSVDRDEL
Protein: At2g17880 (Chaperone DnaJ-domain superfamily protein) (Putative DnaJ protein) (O48828)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Chaperone DnaJ-domain superfamily protein
- NAD
- Heat shock 70 kDa protein 17
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- DnaJ domain protein
- Chaperone protein dnaJ C76, chloroplastic
- Chaperone DnaJ-domain superfamily protein
- Chaperone DnaJ-domain superfamily protein
- AT5g19120/T24G5_20
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
Sequence:
MLSSSPTFFATPFLSSSSSSSPSFSSTSPPSRISRISPSLSTTTASYTCAEDLPRLRQIPQRFSATASLYEILEIPVGSTSQEIKSAYRRLARICHPDVARNSRDNSSADDFMKIHAAYCTLSDPEKRAVYDRRTLLRSRPLTAGYGSYGGRNWETDQCW
Protein: Metallophosphoesterase MPPED2 (EC 3.1.-.-) (Fetal brain protein 239) (239FB) (Metallophosphoesterase domain-containing protein 2) (Q15777)
Organism: Homo sapiens (Human)
Function: Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system.
Interaction partners:
- Doublecortin domain-containing protein 1
- DnaJ homolog subfamily C member 24
- Mitochondrial inner membrane protease subunit 1
- Elongator complex protein 4
- Nuclear receptor subfamily 2 group F member 6
- Follitropin subunit beta
Sequence:
MAHGIPSQGKVTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDKEFMADLVKQDYYRFPSVSKLKPEDFDNVQSLLTNSIYLQDSEVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGIDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGIMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS
Protein: Splicing factor 3B subunit 5 (Pre-mRNA-splicing factor SF3b 10 kDa subunit) (Q9VHI4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in pre-mRNA splicing as component of spliceosome. As part of the spliceosome complex, plays a role in the regulation of spermatogonial differentiation. When associated with the SAGA transcription regulatory histone acetylation (HAT) complex, might be involved in the transcriptional activation of a subset of SAGA-regulated genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:18981222, ECO:0000269|PubMed:27185460}.
Interaction partners:
- Splicing factor 3B subunit 4
- LD45152p
- Splicing factor 3B subunit 1
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 1
- Probable ATP-dependent RNA helicase DDX46
- Probable small nuclear ribonucleoprotein Sm D2
Sequence:
MGERYNIHSQLEHLQSKYIGTGHADTTKFEWLTNQHRDSLASYMGHYDILNYFAIAENESKARVRFNLMERMLQPCGPPPEKLED
Protein: CUGBP Elav-like family member 2 (Q5VZZ6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGTINTPRSKRLLLPKDNNGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: Probable transmembrane protein (P94983)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Adenylate cyclase
- Possible conserved membrane protein
- Uncharacterized protein Rv0493c
- Uncharacterized membrane protein Rv3835
Sequence:
MIYRVACLLARIRFTVGYVAALASVSTTILMHGPQVHAQVIRHASTNLHNLAHGHLGTLWNSAFVIDEGPLYFWLPCLACLLAVAELQLRSLRLTVAFVVGHIGATLLVAAVLAGAIEIGWLPWSISRVSDVGMSYGALAALGALTAAIPGRWRPAWIGWWVSLGLATATIGGGFTDAGHTVALLLGMLVTACFTRPARWTLGRCALLAVASGFCLVLLAHSWWSLVSGSALGLLGALGAAGFARWTRARATSLPPGALAIPQPALSR
Protein: Phosphomethylpyrimidine synthase (EC 4.1.99.17) (Hydroxymethylpyrimidine phosphate synthase) (HMP-P synthase) (HMP-phosphate synthase) (HMPP synthase) (Thiamine biosynthesis protein ThiC) (Q9A6Q5)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Interaction partners:
- hydroxymethylpyrimidine kinase
- Thiazole synthase
- Thiamine biosynthesis protein ThiS
- Thiamine-phosphate synthase
- Molybdopterin-synthase adenylyltransferase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Thiamine phosphate synthase/TenI domain-containing protein
- N5-carboxyaminoimidazole ribonucleotide synthase
- 7-carboxy-7-deazaguanine synthase
- Triosephosphate isomerase
Sequence:
MNIQSTIKAVAETISTGPIPGSRKVYQAGELFPELRVPFREVAVHPSANEPPVTIYDPSGPYSDPAIQIDIEKGLPRTREALVVARGDVEEVADPRQVKPEDNGFAQGKHLAPEFPDTGRKIYRAKPGKLVTQLEYARAGIITAEMEYVAIRENLRREQDRPCVRDGEDFGASIPDFVTPEFVRQEIARGRAIIPANINHGELEPMAIGRNFLVKINANIGNSAVLSTVADEVDKLVWATRWGADTVMDLSTGRNIHNIRDWIIRNSSVPIGTVPIYQALEKVNGVAEDLNWEVFRDTLIEQCEQGVDYFTIHAGVRLPFIPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYERFDEICEIMRAYDVSFSLGDGLRPGSTADANDEAQFSELRTLGELTKVAWKHGVQVMIEGPGHVAMHKIKANMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPDRDDVKTGVITYKLAAHAADLAKGHPGAAMWDDAISRARFEFRWEDQFNLGLDPETARKFHDETLPKEAHKTAHFCSMCGPKFCSMKISQEVRDFAAGKAPNSAELGMAEMSEKFREQGSEIYLKTE
Protein: Myomesin-2 (Q3UQS9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSLVAVPFYQKRHKHFDQSYRNIQTRYLLDQYALKKQATTQSSSQRSLTERSSSKRASSQSSAGAMTCRLCAKRVSASEEEEVENENRYRSQAASYGEAKRQRFLSELAQLEENVHLARSQARDKLDKYFMEQTVEDNLAWERHSFEYRMSRAPEILVRLRSHTIWERMSVRLCFTVQGFPTPVVQWYKDGSLICQAGEPGKYRIESRYGVHTLEINRANFEDTATYSAVATNSHGQVSTNAAVVVRRYRGEEEPFHSVGLPIGLPLSSVIPYTHFDVQFLEKFGVTFRREGETVTLKCTLLVTPDLKRVQPRAEWYRDDVLLKESKWTKMFFGEGQASLSFSHLNKDDEGLYTLRIVSRGGVSDHSAFMFVRDADPLVTGAPGAPMDLQCHDANRDYVIVTWKPPNTTTESPVIGYFIDKCEVGTNNWVQCNDAPVKICKYPVTGLFEGRSYVFRVRAVNNAGISRPSRISDAVAALDPVDLRRLQAIHLEGEKEIVIYQDDLEGDVQIPGPPTNVQASEVSRNYVVLSWDPPSPRGKDPLMYFIEKSAVGSGSWQRVNAQTAVRSPRYAVFDLAEGKSYVFRVLSANKHGLSDPSEITPPIQAQDMIVVPSAPGRVLASRNTKTSVVVQWDRPKHEEDLLGYYVDCCVAGTNMWEPCNHKPIGYNRFVVHGLTTGEQYIFRVKAVNAVGTSENSQESEVIKVQAALTVPSHPYGITLLNCDGHSMTLGWKVPKFSGGSAIIGYYLDKREVHHKNWHEVNSSPVKERILTVEGLTEGSLYEFKIAATNLAGIGQPSDPSEHFKCEAWTDPEPGPAYDLTFCEVRDTSLVILWKAPVYSGSSPVSGYFVDFKEEDSGEWKTTSEAATPNRYLKVCDLQQGKTYVFRIRAVNASGPGKPSDTSEPVLVEARPGTKEISAGVDEEGNIYLGFDCQEMTDASQFTWCKAYEEIADEERFEVHTEGDHSKLYFKNPDKEDLGTYSVSVSDTDGVSSSFVLDEEELERLMALSNEIKNPTIPLKSELAYEIFDKGQVRFWLQAEHLSPDASFRFIINDREVSDSDTHRIKCDRSTGMIEMVMDRFTIENEGTYTVQIQDGKAKNQSSLVLIGDAFKAVLEEAEFQRKEFLRKQGPHFAEYLHWDVTEECEVRLVCKVANTKRETVFKWLKDDVLYETETPPDLEKGVCELLIPKLSKKDHGEYKATLKDDRGQDVSVLEVGGKVYEDMILAMSRVCGASASPLKVLCTPEGIRLQCFMKYFTEEMKVSWYHKEAKISSSEHMRIGGSEEMAWLQICEPTEKDKGKYTFEIFDGKDSHQRSLDLSGQAFDEAYAEFQQLKAAAFAEKNRGKVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVVWFKNDKDIELSEHFLVKMEQSKYVSLTIQGVTAEDSGKYSINVKNKYGGEKIDVTVSVYKHGEKIPDISPPQQAKPKLIPASTSSD
Protein: Nucleoprotein (Nucleocapsid protein) (NP) (Protein N) (Q07097)
Organism: Sendai virus (strain Fushimi) (SeV)
Function: Encapsidates the genome in a ratio of one N per six ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with 13.07 N per turn. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Replication is dependent on intracellular concentration of newly synthesized N, termed N(0), which corresponds to the protein not associated with RNA. In contrast, when associated with RNA, it is termed N. During replication, encapsidation by N(0) is coupled to RNA synthesis and all replicative products are resistant to nucleases.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm.
Interaction partners:
Sequence:
MAGLLSTFDTFSSRRSESINKSGGGAVIPGQRSTVSVFVLGPSVTDDADKLFIATTFLAHSLDTDKQHSQRGGFLVSLLAMAYSSPELYLTTNGVNADVKYVIYNIEKDPKRTKTDGFIVKTRDMEYERTTEWLFGPMVNKSPLFQGQRVAADPDTLLQTYGYPACLGAIIVQVWIVLVKAITSSAGLRKGFFNRLEAFRQDGTVKGALVFTGETVEGIGSVMRSQQSLVSLMVETLVTMNTARSDLTTLEKNIQIVGNYIRDAGLASFMNTIKYGVETKMAALTLSNLRPDINKLRSLIDTYLSKGPRAPFICILKDPVHGEFAPGNYPALWSYAMGVAVVQNKAMQQYVTGGTYLDMEMFLLGQAVAKDAESKISSALEDELGVTDTAKERLRHHLANLSGGDGAYHEPTGGGAIEVALDNADIDLETEAHADQDARGWGGESGERWARQVSGGHFVTLHGAERLEEETNDEDVSDIERRIAMRLAERRQEDSATHGDEGRNNGVDHDEDDDAAAVAGIGGI
Protein: Neuroligin 1 (E9QK34)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKLDDVDPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTGEHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVMLPVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDDIRDSGGPKPVMVYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRITVFGSGAGGSCVNLLTLSHYSEGLFQRAIAQSGTALSSWAVSFQPAKYARILATKVGCNVSDTVELVECLQKKPYKELVDQDVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEVPYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYSQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHNLNDISQYTSTTTKVPSTDITLRPTRKNSTPVTSAFPTAKQDDPKQQPSPFSVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHDVHRRCSPQRTTTNDLTHAPEEEIMSLQMKHTDLDHECESIHPHEVVLRTACPPDYTLAMRRSPDDIPLMTPNTITMIPNTIPGIQPLHTFNTFTGGQNNTLPHPHPHPHSHSTTRV
Protein: Elongin-C (EloC) (Elongin 15 kDa subunit) (RNA polymerase II transcription factor SIII subunit C) (SIII p15) (Stromal membrane-associated protein SMAP1B homolog) (Transcription elongation factor B polypeptide 1) (P83941)
Organism: Rattus norvegicus (Rat)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15369}.
Interaction partners:
- von Hippel-Lindau disease tumor suppressor
- Elongin-B
- Cullin 2
- E3 ubiquitin-protein ligase RBX1
- Elongin-B
- Cullin-5
- Hypoxia-inducible factor 1-alpha
- RING-box protein 2
- Endothelial PAS domain-containing protein 1
- Elongin-A
Sequence:
MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Protein: Protein sel-1 homolog 1 (Suppressor of lin-12-like protein 1) (Sel-1L) (Q9UBV2)
Organism: Homo sapiens (Human)
Function: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16186509}; Single-pass type I membrane protein {ECO:0000269|PubMed:16186509}.
Interaction partners:
- Derlin-2
- E3 ubiquitin-protein ligase synoviolin
- Protein OS-9
- Derlin-1
- Endoplasmic reticulum lectin 1
- Lipid droplet-regulating VLDL assembly factor AUP1
- Ubiquitin-conjugating enzyme E2 J1
- Transitional endoplasmic reticulum ATPase
- FAS-associated factor 2
- ER degradation-enhancing alpha-mannosidase-like protein 1
Sequence:
MRVRIGLTLLLCAVLLSLASASSDEEGSQDESLDSKTTLTSDESVKDHTTAGRVVAGQIFLDSEESELESSIQEEEDSLKSQEGESVTEDISFLESPNPENKDYEEPKKVRKPALTAIEGTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYKADEKWGFCETEEEAAKRRQMQEAEMMYQTGMKILNGSNKKSQKREAYRYLQKAASMNHTKALERVSYALLFGDYLPQNIQAAREMFEKLTEEGSPKGQTALGFLYASGLGVNSSQAKALVYYTFGALGGNLIAHMVLGYRYWAGIGVLQSCESALTHYRLVANHVASDISLTGGSVVQRIRLPDEVENPGMNSGMLEEDLIQYYQFLAEKGDVQAQVGLGQLHLHGGRGVEQNHQRAFDYFNLAANAGNSHAMAFLGKMYSEGSDIVPQSNETALHYFKKAADMGNPVGQSGLGMAYLYGRGVQVNYDLALKYFQKAAEQGWVDGQLQLGSMYYNGIGVKRDYKQALKYFNLASQGGHILAFYNLAQMHASGTGVMRSCHTAVELFKNVCERGRWSERLMTAYNSYKDGDYNAAVIQYLLLAEQGYEVAQSNAAFILDQREASIVGENETYPRALLHWNRAASQGYTVARIKLGDYHFYGFGTDVDYETAFIHYRLASEQQHSAQAMFNLGYMHEKGLGIKQDIHLAKRFYDMAAEASPDAQVPVFLALCKLGVVYFLQYIRETNIRDMFTQLDMDQLLGPEWDLYLMTIIALLLGTVIAYRQRQHQDMPAPRPPGPRPAPPQQEGPPEQQPPQ
Protein: Clusterin (Q6PBL3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR002368}.
Interaction partners:
Sequence:
MKVLWSLLGLFLLYLSTECLLPPSKEELNQMSQVGEKYLDRQIENAISGVKEMKTVMERSEEEHKRMLSEMEKTQKEKENALKTAQEMKEKLSEEQSVCNETMEALWEECKPCLRKTCVKFYSRTCRSGSGLVGRQLEEILNRTSPISIFINGQSIETLLSEDQQQTRHFQDLEESYTEVSDGVENMFTDSMKVFDHMQMFHHPGFFPSRFQFPSMFGGHEGSTHAGRIYRSPMHDSLFHSLQSLFRPMERSMSMFGKNEERNFTSEGWKLNEKVTTDDKMTCKEIRRNSFGCVKLKDECEKCQQIQHIDCSGKRPLEGPLKEELERALGKAEEFTQEFNNLLNIFQEQMFNTSSLLDLFNKQFGWVSSLANHTQNEDGFFQIQAVMSKGSDNAENPADTRVSVKLFDGPDMIYTVPGDIPWSDPKFSEVVAQEALDRYKQNAVITKL
Protein: Platelet-derived growth factor receptor-like protein (F1QHI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Paraoxonase
Sequence:
MKFWLFFTLALLWLEVQNGVCQQVKRKKEAGENRIKPGRKRAKVRYPKVKEKDTGSKGQSILTQVLDKGRFLRLGESLSLNPGKTLELRCKGTKIGWAYPSYLDTFNDNRLSIKQHERYGQLILTSPSAADTGEYSCWVLLCDGQECEKDVDTISATYIYFTDKDELFVPSAIHFEIIYLRPDKPATIPCRVTNPKIKVSLHREVPAEEIAVDGTQISYNPTKGFIIQNPSPEHKGAYYCKANSTSKTTPQISTKYQLLYVEVPSGPPFATIEASSNSVSGGDVFNVTCTVLGEPEMNVSFSWRYPGQDQRPVNIQDSWRLINRGVGHTTRISHSVMIVDDVETIDYGKYICTAKNKNGETLVATSVKSRD
Protein: Fibrinogen like 1B precursor (Si:ch211-287a12.9) (F1QG23)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPQLVFILICHALTLLQASAGEECQSYEMSKLKEEIRMLNNKLLIGEWKVMHLRTHRKFRLVPNLELQENKPSENNTEPSPTLPSTGGSLLVHDKDCSELYDRLKPVSGFYRIKPKPLLEPFLVYCDMDDGGAWTVIQKRINGKVDFDRKWEDYKNGFGNFQSSKDEFWLGNDHIHVLLSDGDSVMKIDLTDWKGGKSYAMYDNFKVSDEKDKYRLYYGMYSGQAGDALSGGANMVEQWSASHNGMQFSTRDQDHDRYLQGSCAAENKGGWWYNRCHAANLNGRFYRGGEYKAKYDNGIVWSTWKGLWYSLRHTVMKVRPSSHMDSVGSGGGPTE
Protein: Adenylyl-sulfate kinase 2, chloroplastic (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 2) (Adenosine-5'-phosphosulfate kinase 2) (APS kinase 2) (O49196)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19304933}.
Interaction partners:
- ATP sulfurylase 1, chloroplastic
- ATP sulfurylase 2
- ATP-sulfurylase 3, chloroplastic
- ATP sulfurylase 4, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- Assimilatory sulfite reductase
- Adenylyl-sulfate kinase 1, chloroplastic
- 3'
Sequence:
MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG
Protein: Troponin I, fast skeletal muscle (Troponin I, fast-twitch isoform) (P27768)
Organism: Rattus norvegicus (Rat)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin C, skeletal muscle
- Troponin T, fast skeletal muscle
- Troponin T, slow skeletal muscle
- Troponin T, cardiac muscle
- Calcium-transporting ATPase
- Troponin C, slow skeletal and cardiac muscles
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-4
- Tropomyosin beta chain
- Troponin I, slow skeletal muscle
Sequence:
MGDEEKRNRAITARRQHLKSVMLQIAATELEKEESRRESEKQNYLSEHCPPLHIPGSMSEVQELCKQLHAKIDAAEEEKYDMEVKVQKSSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSKHKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFESES
Protein: ADP-ribosylation factor 6 (Q9U2S4)
Organism: Caenorhabditis elegans
Interaction partners:
- Exchange factor for Arf-6
- Exocyst complex component 5
- Ras-related protein Rab-35
- Kinesin-like protein
- JNK-interacting protein
- Mss4 protein
- GTP exchange factor for ARFs 1
- Dynamin-type G domain-containing protein
- Fungus-Induced Protein
- Actin
Sequence:
MGKFLSKIFGKKELRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNIKFNVWDVGGQDKIRPLWRHYYTGTQALIFVMDAADRDRVDEARMELHRIINDREMKEAIILVFANKQDLADAMKPHEIQDKLGLTRIRDRNWYVQPSCASTGDGLHEGLTWLSQNCKP
Protein: Paired box protein Pax-2-B (xPax-2b) (O57682)
Organism: Xenopus laevis (African clawed frog)
Function: Probable transcription factor. Involved in kidney development, acting synergistically with lhx1/lim-1 in pronephric morphogenesis during the tailbud stages.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q02962, ECO:0000255|PROSITE-ProRule:PRU00381}.
Interaction partners:
Sequence:
MDMHCKADPFSAMHRHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIADYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGTPVSTPGHTLVPSTASPPVSSASNDPVGSYSINGILGIPRSNGEKRKRDEDGSDGSGPNGDSQSSVESLRKHLRADNFTQQQLEALDRVFERPSYPDVFQSAEHIKSEQASEYSLPALTPGLDEVKSSLSASGNADLGSNVSGPQSYPVVTESFASHLYLKQEPHEASLTPFTPSSLASSGLADIQPFQMALTVDASTPTYSSFTHHGPPYGQFGSQPLIAGRDMSSTTLPGYPPHVPPTGQGSYPTSTLAGMVPGTNVSVHHSVQPVECCSCLSSSKPCLFHCRTGSGSEFSGNPYSHPQYTTYNEAWRFSNPALLSSPYYYSATSRGSAPPTAATAYDRH