wanglab/gogpt-training-data huggingface dataset:
Protein: Acetylcholine receptor subunit epsilon precursor (Cholinergic receptor, nicotinic, epsilon) (A2BG85)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Acetylcholine receptor subunit alpha
- Acetylcholinesterase collagenic tail peptide isoform X2 of asymmetric acetylcholinesterase)
- Docking protein 7.
- 43 kDa receptor-associated protein of the synapse
- Muscle, skeletal receptor tyrosine-protein kinase isoform 3 precursor
- Cholinergic receptor, nicotinic, alpha 4b
- Cholinergic receptor, nicotinic, alpha 2a
- Cholinergic receptor, nicotinic, alpha 7
- Cholinergic receptor, nicotinic, beta 1
- glutamine--fructose-6-phosphate transaminase
Sequence:
MAVAERFGRTCVVAIALLATVLQVTGNEESQLIADKFKNYSKNIRPARHADEKVKVQVKLTLTNLISLNEKEETLTTNVWIEIQWHDYRLAWNTSEYHDIEQIRVPYYTVWLPDIVLENNIDGKFDVAYYANVLISSDGSMYWLPPAIYRSTCAIEITYFPFDWQNCTLVFRSQTYSANEIDIVLAEDENGKPIEWVDIDPEAFTENGEWAIKHRPARKLTNQRYSPDDLEYQEVYYNIIIQRKPLFYVINIILPCSLISSLVVLAYFLPAKAGGQKLTVSISVLLAQTVFLILISQKIPETSLSVPLIGKYLIFVMSMTTLIVTNCIIVLNYSLRSPSTHNMSQSIKHIFLEVVPRYLGMAPFVDEGDQGGVYEMRERRRSSFGLMQRAEEYVLKQPRSEMMFDKQRERHGLMRTIVDEIDVSSTANLYKSLAKTAPEIKECVDACNFIAESTKQQNDTGSEMESWVLIGKMIDKVCFWAAISLFSIGTIAIFLMGHYNQAPEYPFAWENKKYVPE
Protein: E3 SUMO-protein ligase PIAS4-A (EC 2.3.2.27) (Protein inhibitor of activated STAT protein 4) (F1R4C4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase (By similarity). May play a role as a transcriptional coregulator in various cellular pathways (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (By similarity). Negatively regulates induction of interferon phi 1 (ifnphi1) mediated by mavs and ticam1/trif. Also inhibits ifnphi1-mediated activation of the interferon-stimulated genes (ISGs) pkz and cd40, and to a lesser extent rsad2 and isg15. May inhibit ticam1/trif-mediated activation of NF-kappa-B.
Subcellular location: Nucleus {ECO:0000269|PubMed:22345667}.
Interaction partners:
- SUMO-conjugating enzyme UBC9-A
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier
- E3 ubiquitin-protein ligase rnf168
- non-specific serine/threonine protein kinase
- Protein inhibitor of-activated STAT, 1b.
- SUMO-conjugating enzyme UBC9-B
- Ube2n protein
Sequence:
MAAELVEAMNMVKSFRVSDLQTLLASMGRSKSGLKQDLVGRALRLVQTEYSPELLKNVRQLYETRFPKASAWLAARRPETVAVNYPALNSSPRGTGQGTDYLNGIPKPAPPPAAEVKLVPLPFYHNLETLLPPTELVAQNSEKLQESQCVFDLTPNQVDQIRNSSELRPGMKSVQVVLRICYTDSIGVQEDQYPPNIAVKVNQSYCHVPGYYPSNKPGVEPRRPCRPVNITPWLHLSTVTNRVTITWGNFGKRYSVAVYLVRVFTSGELFNQLKHCSVENPDRCRERIQDKLRFDPESEIATTGLRVSLICPLVKMRLGVPCRVLTCAHLQCFDAVFFLQMNEKKPTWTCPVCDKPAPFELLTIDGLLSEILKETPEDVEEIEYLTDGSWRPIRDDKEKERERENSRTPDYPVVDICVPEANGHSPAHSGTNQTGKSGSGGASAGTGSTSGGSGGGTVVDLTLDDSSEEEGGGGAEDSEETDDSQDSPAPKRGRYDYDKDLVTAY
Protein: SH2 domain-containing protein 3A (Novel SH2-containing protein 1) (Q9BRG2)
Organism: Homo sapiens (Human)
Function: May play a role in JNK activation.
Interaction partners:
- Serine protease 57
- Nuclear pore complex protein Nup93
- Peptidyl-prolyl cis-trans isomerase H
- SH2 domain-containing protein 3C
- Peptidyl-prolyl cis-trans isomerase G
- Interferon regulatory factor 3
- Cytospin-B
- Nuclear RNA export factor 1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Peptidyl-prolyl cis-trans isomerase FKBP1A
Sequence:
MQVPQDGEDLAGQPWYHGLLSRQKAEALLQQNGDFLVRASGSRGGNPVISCRWRGSALHFEVFRVALRPRPGRPTALFQLEDEQFPSIPALVHSYMTGRRPLSQATGAVVSRPVTWQGPLRRSFSEDTLMDGPARIEPLRARKWSNSQPADLAHMGRSREDPAGMEASTMPISALPRTSSDPVLLKAPAPLGTVADSLRASDGQLQAKAPTKPPRTPSFELPDASERPPTYCELVPRVPSVQGTSPSQSCPEPEAPWWEAEEDEEEENRCFTRPQAEISFCPHDAPSCLLGPQNRPLEPQVLHTLRGLFLEHHPGSTALHLLLVDCQATGLLGVTRDQRGNMGVSSGLELLTLPHGHHLRLELLERHQTLALAGALAVLGCSGPLEERAAALRGLVELALALRPGAAGDLPGLAAVMGALLMPQVSRLEHTWRQLRRSHTEAALAFEQELKPLMRALDEGAGPCDPGEVALPHVAPMVRLLEGEEVAGPLDESCERLLRTLHGARHMVRDAPKFRKVAAQRLRGFRPNPELREALTTGFVRRLLWGSRGAGAPRAERFEKFQRVLGVLSQRLEPDR
Protein: TAR DNA-binding protein-43 homolog, isoform A (Q9W1I0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDFVQVSEEEGDEPIELPAEEDGTLLLSTLQAQFPGSCGLKYRNLDTKAVRGVRSNEGRLFPPSVESGWGEYAYFCVFPKENKRKSDDNLENSTAKTKRIETRLRCTDLIVLGLPWKTTEESLREYFETYGEVLMAQIKKDTKSGQSKGFGFVRFGSYDAQMRVLTNRHLIDGRWCEVKVPNSKGMGHQVPCKVFVGRCTEDINSDDLREYFSKFGEVTDVFIPRPFRAFSFVTFLDPDVAQSLCGEDHIIKGVSVHVSNAAPKAEQNRNQQVQSYNYNSANSFGMHSYHPQGNHMNPGRNGHHRGRQFSILDGSERGPQQCQQLWWTEGAE
Protein: Stardust, isoform L (EC 2.7.4.8) (M9NEZ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQANSSRSNLSAQSSGTPSASTISSSQGKQQVVELSGYVIILVENVEGKIKLYGSPPDRDNLEVGDEILEVNGLTLENISRTEVIRHIHDCIKSCTICLRVRKKNDSRLAWDIGNSVQDAFVIAVEEHARERLQRLAALNRVTPVDITQLSKKLQQTKSGTATSQRQDLSFLNESTPIYVTSFTSNQITCSSSTMTTATAGGPISAPSLATATTTVPTASSHTTTVVAQIEHGASALVSAAVAAATAADRNANSTTSAALKQTANCIGNSTSSLGTTSTTSSQSTSSATGHIYQTSQAQQQQLQQLQQQLAAAAAAGKPLQAKSLLASSLQHLAEEVDNEDLDDDDDVDGANYCGITYISYNNKHAQLPTTTLPATTALPAAAASLATTAAIYQQRQQQQHQQQQQQQQQPVHHHNHPPTASQLNRATAPAPLQLGGPVNPSFVDAQTSTSPLMAQQLHSQHADVDAAPPSSSSSSAVVVVERHVHGTTTPKTEYSTAISSGQLQQAFAELQLHSSNNNATQQQQQHLLLSNNNNSNNSMAAAQTTASLMKNCDLLISNNLYPPRRELLEDVIVHQASDVHSYSTSASAAAIASSSNRSQQQQQQQQQHQLLSAAYELQQQQQLQLQQQQQQQNSPTSSISIGRTELLLGDQSLRQDPRGNRRRSGSSIVVLDGDDLKPCLPDDYISGQHHLNHQQQLQLQQQLQQQHPLQQQHYRTHSGDIREIDQEMLTMLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPLFYLLEERLKPAKIKAQVKDTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (DNA polymerase alpha holoenzyme-associated protein P1) (P1-MCM3) (P25206)
Organism: Mus musculus (Mouse)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P25205}. Chromosome {ECO:0000250|UniProtKB:P25205}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P25205}.
Interaction partners:
- DNA replication complex GINS protein PSF2
- Cell division control protein 45 homolog
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM6
- DNA replication factor Cdt1
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM7
- Origin recognition complex subunit 2
Sequence:
MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQNKVRELISDNQYRLIVSVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYIGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKVKPGDRIQVVGTYRCLPGKKGCYTSGTFRTVLIACNVKQMSKDIQPAFSADDIAKIKKFSKTRSKDVFEQLARSLAPSIHGHDYVKKAILCLLLGGVERELENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHQYRAPGEQDGDALPLGSSVDILATDDPDFTQDDQQDTRIYEKHDSLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPTLTQESAAYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKASEDESDLEDEEEKSQEDTEQKRKRRKTHAKDGESYDPYDFSEAETQMPQVHTPKTDDSQEKTDDSQETQDSQKVELSEPRLKAFKAALLEVFQEAHEQSVGMLHLTESINRNREEPFSSEEIQACLSRMQDDNQVMVSEGIVFLI
Protein: Protein Mabiki (Q9VK13)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in inducing apoptosis and is involved in the repair of head patterning defects in the embryo caused by extra maternal copies of the homeotic gene bicoid.
Interaction partners:
- ADP-ribosylation factor-like protein 2
Sequence:
MEHHQIYRHKKFDMGRKIEKCDLQLKEELISRSGTPCTSRSPFDAANQSVSLGFSDQDADFPPLPKRRRLGSSSSSVSYQSASPIITEAIQDIFKYHVNMVRKFPKKERSPKDQERRNKNTIACRMSRRKKKFDDLQIEQQYKECSDEHLKIAEQSLRARVYLNHLKQLVKQEDHPLVSSRRVPEENTKSNFSIDYLIGGIKQEHA
Protein: Bactericidal permeability-increasing protein (BPI) (Q6AXU0)
Organism: Rattus norvegicus (Rat)
Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P17213}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000250|UniProtKB:P17213}.
Interaction partners:
- Myeloperoxidase
- Cathepsin G
- Granzyme-like protein 2
- Lipopolysaccharide-binding protein
- BPI fold-containing family A member 1
Sequence:
MAWGPDNVRKWSSLALLAIVGTALTAATDPGFVARISQKGLDFVCQESMVELQKELLAISIPDFSGDFKIKHLGKGTYEFYSMAVEGFHIPDPQIKLLPSDGLQLSITSASIKISGRWKYRKNILKASGNFQLSIQGVSIIADLILGNDPSGRITITCSTCDSHINSVRIKVSGSMLGWLIQLFHRKIETSLKKTIYKKICKIVRNSVSAKLQPYVKTLPVVAKVDDITSIDYSLLAPPMTTDKFLEGQLRGEFFWRGHHGPFPAVPPVMNILPNNNYMVCMGISDYFFNTAEFAYQESETLKITLRDQLLAKDARYHLNTDFLKTFLPEVAKKFPSMGLQLLISAPLFAHLNIQPSGLSLSPNLETRAFVVLPNSSLIPLFLLGMKTNASLEVNAMKNRLIGEMKLGRLLLELKQSNFGSFKVELLEDVINYLMSTMVLPKINEKLRRGFPLPLPAGIQLINSILYSSQNFLLLEADLHRT
Protein: Lipoprotein YafY (P77365)
Organism: Escherichia coli (strain K12)
Function: When overproduced strongly induces degP through the activation of the two-component envelope stress response system CpxA/CpxR.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:15252048}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:15252048}.
Interaction partners:
- Uncharacterized protein YkfB
Sequence:
MKRKTLPLLALVATTLFLIACDDRSDDLKAISKFKDLTPPRFSDVVSHQDDVSEEWSQVDYLSGPTLQVLRTRQSPDGCEDGSYYYLVDMQEKTVQPLMNALCIADNIKLEYQEVTDPYTKEKYFEYAHDGKLMGQLLIPSNPDNQE
Protein: Amino acid transporter ANT1 (Aromatic and neutral amino acid transporter 1) (Q9SF09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Translocates aromatic and neutral amino acids such as tyrosine, tryptophan, phenylalanine, histidine, proline, leucine, valine, glutamine, as well as arginine. Transports the auxins indole-3-acetic acid (IAA) and 2,4-dichlorophenoxyacetic acid (2,4-D).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27925655}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cationic amino acid transporter 6
- WAT1-related protein At1g25270
- WAT1-related protein At2g40900
- WAT1-related protein At4g01430
- Protein GLUTAMINE DUMPER 2
- Sugar transporter ERD6-like 15
- WAT1-related protein At1g09380
- WAT1-related protein At1g44800
- WAT1-related protein At1g01070
- ADP,ATP carrier protein ER-ANT1
Sequence:
MAIKDLTATTGDSSLPLIKSPPSETTGGDRTSALQTLGNIIVSIVGTGVLGLPYAFRIAGWLAGSLGVIIVGFATYYCMLLLIQCRDKLESEEGEEESKTYGDLGFKCMGTKGRYLTEFLIFTAQCGGSVAYLVFIGRNLSSIFSSYGLSMVSFILILVPIEVGLSWITSLSALSPFSIFADICNIIAMCFVVKENVEMVIEGDFSFSDRTAISSTIGGLPFAGGVAVFCFEGFAMTLALESSMREREAFPKLLAKVLAGITFVYVLFGFCGYMAYGDQTKDIITLNLPNNWSAIAVQIGLCVGLTFTFPIMVHPLNEIIEQKLKRIDWLQKHHNGYSNETGSVSKFAIFTTRTLLVVGLAAIASLVPGFGTFASLVGSTLCALISFVLPASYHLTLLGPSLNVWNKSIDVFIVICGLIFAVYGTYNTIVGV
Protein: Arabinan endo-1,5-alpha-L-arabinosidase C (EC 3.2.1.99) (Endo-1,5-alpha-L-arabinanase C) (ABN C) (Q5AUM3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Transaldolase
Sequence:
MKLALSLFLLSGSLAQYSNPGACSGDCWGHDPGFYQRVSDGRYYRFSTGGGIQIHASDNLEGPWEAVGEALPGGSVVDHAGSTNLWAPDIHYEASTNLYYMYYSVSTLGSRDSVIGVATSPNLQPNWTDHGALFRSQAGGNYNAIDANWASIGGSPILTFGSYWNGIHQLPLAGPLSLADGATPTQIAYNSSGNHAIEAGFVFYRRGWYYLTFSSGRAGSYDTNPPATGEEYRIVVCRSASGTGDFVDKSGRSCLTDNGGTTILASHGNVYGPGGQGVFEDRTRGWVLYYHYANPDIGLSTGQYQFGWNVLQWADGWPSV
Protein: Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (Mediator complex subunit 27) (A0A8I5ZWJ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADVLSVGVNLEAFSQAISAIQALRSSVSRVFDCLKDGMRNKETLEGREKAFIAHFQDNLHSVNRDLNELERLSNLVGKPSENHPLHNSGLLSLDPVQDKTPLYSQLLQAYKWSNKLQYHAGLASGLLNQQSLKRSANQMGVSAKRRPKAQPTTLVLPPQYVDDVISRIDRMFPEMSIHLSRPNGTSAVLLVTLGKVLKVIVVMRSLFIDRTIVKGYNESVYTEDGKLDIWSKSSYQVFQKVSVPLCLIQLSSIPEGKCSSLTYSGDMGKLQMPWL
Protein: Thiopurine S-methyltransferase (EC 2.1.1.67) (Thiopurine methyltransferase) (O55060)
Organism: Mus musculus (Mouse)
Function: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (also called mercaptopurine, 6-MP or its brand name Purinethol) using S-adenosyl-L-methionine as the methyl donor. TPMT activity modulates the cytotoxic effects of thiopurine prodrugs. A natural substrate for this enzyme has yet to be identified.
Subcellular location: Cytoplasm.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Xanthine dehydrogenase/oxidase
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP synthase
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Nucleotide triphosphate diphosphatase NUDT15
Sequence:
MSLDMKEHPDAEVQKNQVLTLEDWKEKWVTRHISFHQEQGHQLLKKHLDTFLKGQSGLRVFFPLCGKAIEMKWFADRGHTVVGVEISEIGIREFFAEQNLSYTEEPLAEIAGAKVFKSSSGSISLYCCSIFDLPRANIGKFDRIWDRGALVAINPGDHDRYADIILSLLRKEFQYLVAVLSYDPTKHAGPPFYVPSAELKRLFGTKCSMQCLEEVDALEERHKAWGLDYLFEKLYLLTEK
Protein: Calcineurin subunit B (Calcineurin regulatory subunit) (Protein phosphatase 2B regulatory subunit) (J9VL81)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Interaction partners:
Sequence:
MGAAESSMFNSLEKNSNFSGPELMRLKKRFMKLDKDGSGSIDKDEFLQIPQIANNPLAHRMIAIFDEDGSGTVDFQEFVGGLSAFSSKGGRDEKLRFAFKVYDMDRDGYISNGELYLVLKQMVGNNLKDQQLQQIVDKTIMEADKDGDGKLSFEEFTQMVASTDIVKQMTLEDLF
Protein: Receptor expression-enhancing protein 5 (GP106) (Polyposis locus protein 1 homolog) (Protein TB2 homolog) (Q60870)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24668814}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:32075961}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network (PubMed:24668814). In cardiomyocytes, localizes to the junctional sarcoplasmic reticulum membrane which is closely tethered to the cell membrane and contractile machinery (PubMed:32075961). {ECO:0000269|PubMed:24668814, ECO:0000269|PubMed:32075961}.
Interaction partners:
- Reticulon-4
- Reticulon-1
- Reticulon-3
- Atlastin-1
Sequence:
MRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISMKAIESPNKDDDTQWLTYWVVYGVFSIAEFFSDLFLSWLPFYYMLKCGFLLWCMAPSPANGAEMLYRRIIRPIFLRHESQVDSVVKDVKDKAKETADAISKEVKKATVNLLGDVKKST
Protein: AT15593p (Q5BHW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKNARRRPLMIDPQGQANKWIKNYEKNNKLCVIRLNQADYTRVMENAIQFGLPVLLENIGEELDPVLESVLQKTLFKQGGALCIKLGDSVIEYNHSFRFYMTTKLRNPHYLPEVAVKVTLLNFMITTQGLQDQLLGITVARERPDLEAEKNNLIVQGADNKRMLKETEDQILEVLSSAENILEDETAVQILSSAKALANDISEKQVITEATEKQIDIARLSYVPIAEHSTILFFTIVELANIDPMYQYSLVWFVNLYMSSIDNTEKVDDIAARLLDLRNHFTYSLYVNICRSLFERDKLLFSLILNINMMKHDNRIDNAEWMFLLTGGVGLENPYKNPTTWLGVQNWDELCRLTNLTNFKGLREDFNENSAQWKPFFDSKSPQDNKDIPKSWDNRVSVFQKLLLLRVFRPDKLVPAVLNFVSGELGERFVDPPQFDLMASFADSHCCVPLIFILTPGSDPTATLLKFAEDQGFGTNRLFSLSLGQGQGPIAMKMIDEGVKMGNWVVLQNCHLAASFMPLLEKICENLLPDATHPDFRLWLTSYPADHFPVVVLQNGIKMTNEPPKGLRSNILRSMISDPISDPEWYESCTQPRIFKQLIYSLCFFHAVIQERRYFGPIGWNIPYEFNETDLRISLMQLRMFLNQYETVNYDALRYLTGECNYGGRVTDDWDRRTLKTILDKFYCPAVIDLETPYYLDETGLYYVPVFKEVDLYLNFTRDLPQISAPAIFGFHANADIMKDQKETDMLLSHTLLTQDTSASSDDSGGSKALTPEEVVTNVATDILDKLPKLFDRDAALLKYPTLYHQSMNTVLVQEMVRFNVLLNTIRTSLITLRKGIKGLVVMSPAVEAVYKSVLIAKIPAMWAGKSYPSLKPLGSYVTDFLRRLEFLQHWFDHGAPSTFWLSGFFFTQAFLTGAQQNYARKYVISIDLLAFDYEVLTVEEPQRQGLSGPEDGVFVYGIFLEGARWDRTGKYLAESRPRELFDTMPLIWLKPLKRVDLPERHNYLCPMYKTAERRGVLSTTGHSTNFVVAMLLLCNPNTPVSHWIIRGTALLCQLSF
Protein: AP2/ERF domain-containing protein (A0A0Q3JRW7)
Organism: Brachypodium distachyon (Purple false brome) (Trachynia distachya)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTRGSQPAAQLMAFSEPKPIAASSGHQPNPSPPSSPSERPPAGGRGSRRRTQEPGRFLGVRRRPWGRYAAEIRDPTTKERHWLGTFDTAQEAALAYDRAALSMKGAQARTNFVYAAPASCYSNYPPFLAPFHSPAPGTTMANNAAPVMQQYMLPGHGHAPHHIGSGSGSSYASGGSECSMPMPMPMMVDVVRNGSGSGGGSRGHVQREDEDFFCFSGSALDDNSGYLSSVVPESCLRPASSRVEDTTRRYSVSDADAYGYGMMGREDVDDLAQMVAGFWGSDAAAAYGSGGGGGDGMVAASSSQGSDAGYSPFSFLSH
Protein: Guide RNA binding protein gBP25 (Q952G2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLRRIISQQTTLIRKPLGAALFATSALRLEAASSSDADGKEVGSSGEGNRATGGKWRRPSLAQQRARRAQLPPAFDVVHWNDEDISRGHLLRVLHRDTFVVLDYHRQARMLTEEGNKAERVVSVMLPAVYTARFLAVLEGRSEKVEVHSRYTNATFTPNPAAPYTFTLKCTSTRPAQQKQQVAGEEGDETFEWTVEFDVAESLMLQRFLTQALHYNTGFARTSV
Protein: MADS-box protein MADS7 (A2ID27)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEFPNLDPESSSQKKMGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYANNSVRATIERYKKACSDATTPGSVAEANIQFYQQEATKLRRQIRDVQNMNRHILGEALSSLTFKELKNLEGRLEKGICRIRSKKNELLFAEIGFMQKREVELQNDNMYLRAKIAENERAQQQSNQLMQAASSYNRNFLPVNLLEPSNNDYSNQDQTPLQLV
Protein: Protein lin-7 homolog C (Lin-7C) (mLin7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3) (O88952)
Organism: Mus musculus (Mouse)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules. This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
Subcellular location: Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction. Postsynaptic density membrane; Peripheral membrane protein. Cell junction, tight junction. Note=Mainly basolateral in renal epithelial cells.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- Disks large homolog 1
- Protein PALS1
- Disks large homolog 4
- InaD-like protein
- MAGUK p55 subfamily member 2
- Liprin-alpha-2
- MAGUK p55 subfamily member 7
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT
Protein: Intraflagellar transport 27 homolog (Chlamydomonas) (Intraflagellar transport protein 27 homolog (EC 3.6.5.2)) (Zgc:101893) (Q5PR92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Intraflagellar transport 81 homolog.
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport 74.
- Intraflagellar transport 52 homolog
- Intraflagellar transport protein 22 homolog
- Intraflagellar transport protein 70A
- Intraflagellar transport 88 homolog.
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 172 homolog
Sequence:
MVKLRARCVVVGDAAVGKSTLCQMFCSDGAVYQKNYTMNVGVELLEKTVPIPDTSDSVELFIYDSAGRELFSDACENVWSQPSVVCVVFDVTSEASFNNCSRWIDRVQTHSHGLHTPGVLVGNKCDLTSRREVDAAAAQAFAQTHTLQYHETSAKEIGHYEAPFLSLAAAFHSLYQEQKNSILSLI
Protein: Tapasin (Q3SAU9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MANISTIYKLSFLAFTYFIQVYGTSCPVLECWFVQEKPGRGGGFPAAMIQEKSLLYINTDPESEQTKSQQGPSADISHDRVYYITDPAAILCSSSLHPPEGSVHKPQCEINPFMPQPSTVQWAVPLTDSAHSPIYLQADWYSAALQGLDGQLALSSVMRAPTATKVPTVVLSVSSRTPLVRSRLGEPVVLDCGFWAETSSPLSGSGFAVEWRYQFRGDGRLVLAYDGKTDRFAETKEKGAGLDFTALHETGNASLILQEAEVRHTGTYICTVYLPYLLAQVAVELEIVEPPSLSIFPSPLPLSVPGQVVKVQCEASGFFPLSLEFYWELTGPDGKVRPLGQGSVTGHRQGPDNTYSQTTRLELDSAKLDLGRGGEVTCVAVHPGGTRRARVTLNVIGVNGPSIEDSMAMVAVALGLYGLIKIVSWTFSSGSDDTNSQEKKVK
Protein: PopN (Type III secretion outer membrane protein PopN) (YopN family type III secretion system gatekeeper subunit) (O30531)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MDILQSSSAAPLAPREAANAPAQQAGGSFQGERVHYVSVSQSLADAAEELTFAFSERAEKSLAKRRLSDAHARLSEVQAMLQEYWKRIPDLESQQKLEALIAHLGSGQLSSLAQLSAYLEGFSSEISQRFLALSRARDVLAGRPEARAMLALVDQALLRMADEQGLEIELGLRIEPLAAEASAAGVGDIQALRDTYRDAVLDYRGLSAAWQDIQARFAATPLERVVAFLQKALSADLDSQSSRLDPVKLERVMSDMHKLRVLGGLAEQVGALWQVLVTGERGHGIRAF
Protein: Protein Turandot E (Protein Victoria) (Q8INV7)
Organism: Drosophila melanogaster (Fruit fly)
Function: A humoral factor that may play a role in stress tolerance.
Subcellular location: Secreted {ECO:0000269|PubMed:11409894, ECO:0000305}.
Interaction partners:
Sequence:
MSNTRTVHSSTSISKMNSALQISCLLVVLGCLLGSGHCQSEAEFAAKSREIAQVFGNPSVDKYTKARNLPTLIAFYEKYSSRLRLTPQERISINNAMRQYKAQRNQQVDGVSAQGGWLSDIIKTAISIIVKAVE