wanglab/gogpt-training-data huggingface dataset:
Protein: Merozoite surface protein 9 (101 kDa malaria antigen) (Acidic basic repeat antigen) (p101 protein) (Q8I5D2)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, involved in the sialic acid-independent (SAID) merozoite invasion of host erythrocytes by binding to host SLC4A1/Band 3 protein on the surface of the host erythrocyte.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:W7F8N2}; Peripheral membrane protein {ECO:0000250|UniProtKB:W7F8N2}; Extracellular side {ECO:0000250|UniProtKB:W7F8N2}. Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:W7F8N2}. Secreted {ECO:0000269|PubMed:14630931, ECO:0000269|PubMed:29511044}. Note=Localizes to the merozoite surface at the time of schizont rupture. {ECO:0000250|UniProtKB:W7F8N2}.
Interaction partners:
- Nucleoporin NUP221, putative
- Serine-repeat antigen protein 5
- Merozoite surface protein 1
- Merozoite surface protein P92
- Calcium-dependent protein kinase 1
- cAMP-dependent protein kinase catalytic subunit
Sequence:
MMNMKIVLFSLLLFVIRWNIISCNKNDKNQGVDMNVLNNYENLFKFVKCEYCNEHTYVKGKKAPSDPQCADIKEECKELLKEKQYTDSVTYLMDGFKSANNSANNGKKNNAEEMKNLVNFLQSHKKLIKALKKNIESIQNKKHLIYKNKSYNPLLLSCVKKMNMLKENVDYIQKNQNLFKELMNQKATYSFVNTKKKIISLKSQGHKKETSQNQNENNDNQKYQEVNDEDDVNDEEDTNDDEDTNDEEDTNDDEDTNDDEDTNDEEDTNDEEDHENNNATAYELGIVPVNDVLNVNMKNMITGNNFMDVVKNTLAQSGGLGSNDLINFLNQGKEIGENLLNITKMNLGDKNNLESFPLDELNMLKDNLINYEFILDNLKTSVLNKLKDLLLRLLYKAYVSYKKRKAQEKGLPEPTVTNEEYVEELKKGILDMGIKLLFSKVKSLLKKLKNKIFPKKKEDNQAVDTKSMEEPKVKAQPALRGVEPTEDSNIMNSINNVMDEIDFFEKELIENNNTPNVVPPTQSKKKNKNETVSGMDENFDNHPENYFKEEYYYDENDDMEVKVKKIGVTLKKFEPLKNGNVSETIKLIHLGNKDKKHIEAINNDIQIIKQELQAIYNELMNYTNGNKNIQQIFQQNILENDVLNQETEEEMEKQVEAITKQIEAEVDALAPKNKEEEEKEKEKEEKEKEEKEKEKEEKEKEEKEKEEKEKEEKEEEKKEKEEEQEEEEEEEIVPENLTTEESK
Protein: Lecithin retinol acyltransferase (EC 2.3.1.135) (Phosphatidylcholine--retinol O-acyltransferase) (Q9JI61)
Organism: Rattus norvegicus (Rat)
Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A (By similarity). LRAT plays a critical role in vision (By similarity). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000269|PubMed:18544127}. Endosome, multivesicular body {ECO:0000269|PubMed:18544127}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18544127}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells.
Interaction partners:
- Retinoid isomerohydrolase
- Retinol dehydrogenase 5
- Cytochrome P450 26A1
- NADP-retinol dehydrogenase
- Retinol dehydrogenase 10
- Dehydrogenase/reductase SDR family member 9
- All-trans-retinol 13,14-reductase
- Retinol dehydrogenase
- Retinol-binding protein 1
- Retinol dehydrogenase 16
Sequence:
MKNSMLEAASLLLEKLLLISNFKIFSVCAPGGGTGKKHPYEINSFLRGDVLEVSRTHFTHYGIYLGDNRVAHLMPDILLALTSDKERTQKVVSNKRLLPGVICKVASIRVDTVEDFAYGADILVNHLDETLKKKSLLNEEVARRAEQQLGLTPYSLLWNNCEHFVTYCRYGSPISPQAEKFHETVKILIRDQRSCLASAVLGLVSIIYTGLASYMTLPAVCIPFCLWMMSG
Protein: Ribonuclease alpha-sarcin (EC 4.6.1.23) (rRNA endonuclease) (P00655)
Organism: Aspergillus giganteus
Function: Alpha-sarcin is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes (By similarity). Inhibits both the EFl (elongation factor 1)-dependent binding of aminoacyl-tRNA and the GTP-dependent binding of EF2 (elongation factor 2) to ribosomes.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MVAIKNLVLVALTAVTALAVPSPLEARAVTWTCLNDQKNPKTNKYETKRLLYNQNKAESNSHHAPLSDGKTGSSYPHWFTNGYDGDGKLPKGRTPIKFGKSDCDRPPKHSKDGNGKTDHYLLEFPTFPDGHDYKFDSKKPKENPGPARVIYTYPNKVFCGIIAHTKENQGELKLCSH
Protein: BZIP transcription factor family protein (Basic-leucine zipper (BZIP) transcription factor family protein) (Q9SKG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Sequence-specific DNA binding transcription factor
- Basic leucine-zipper 58
- At5g04840
Sequence:
MNGSDNITTPSGSRSMTQPSLASSSLPPLSPSSSTFRRNSLPSMSFSPSAPVESRDSSIKVNKNPSLPPLVDGEEDASWLEFGSSDYTDDELNKIAKSTKLQDIAKSTKLQEIVSDPKKVRRILKNRELAASSKQRKLKYMIDLEHRIKFLENKNALIFEKIKLLEKDKTILMNEKKEITIQIESLEQQAQLRDALTEKLHVEIERLKVITISNEKGSVELQRLKMETCEVLQYRREFDRSNMQGMDPNMFTWSQPNLGFYGQI
Protein: Histamine oxidase (EC 1.4.3.22) (Copper amine oxidase) (Q59118)
Organism: Arthrobacter globiformis
Function: Oxidizes histamine. Other amines including phenethylamine, tyramine, tryptamine, putrescine, and benzylamine also serve as substrate.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MTLQTTPSTPLVQDPPVPATLVHAAAQHPLEQLSAEEIHEARRILAEAGLVGESTRFAYLGLIEPPKTTRQGDVTGAARLVRAMLWDAAQSRSLDVRLSLATGLVVDRRELNPEADGQLPVLLEEFGIIEDILSEDPQWNAALTARGLTPAQVRVAPLSAGVFEYGNEEGKRLLRGLGFRQDHPADHPWAHPIDGLVAFVDVENRRVNHLIDDGPVPVPEVNGNYTDPAIRGELRTDLLPIEIMQPEGPSFTLEGNHLSWAGWDLRVGFDAREGLVLHQLHHSHKGRRRPVIHRASISEMVVPYGDPSPYRSWQNYFDSGEYLVGRDANSLRLGCDCLGDITYMSPVVADDFGNPRTIENGICIHEEDAGILWKHTDEWAGSDEVRRNRRLVVSFFTTVGNYDYGFYWYLYLDGTIEFEAKATGIVFTAALPDKDYAYASEIAPGLGAPYHQHLFSARLDMMIDGDANRVEELDLVRLPKGPGNPHGNAFTQKRTLLARESEAVRDADGAKGRVWHISNPDSLNHLGHPVGYTLYPEGNPTLAMADDSSIASRAAFARHHLWVTRHAEEELYAAGDFVNQHPGGAVLPAYVAQDRDIDGQDLVVWHSFGLTHFPRPEDWPIMPVDTTGFTLKPHGFFDENPTLNVPSSAAGHCGTGSEREHAAPGGTAVGHSGPDTGGQGHCGH
Protein: Autophagy-related protein 9 (Q961S5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}.
Interaction partners:
Sequence:
MTAILAHVHYLPSEWRQQAHTTKVRQEFSNFFQFKAGYLLSEIFSPFVTPFVLIFVFRPKAIELVRFFRTFTVSVRGVGNVCSFAQMDVRKHGNPDWQLTSELEEMTRATAQQPQQEPQQQSLAGGKTEMSLLRFTLNNPEWQMPKEAKQFLRGVREHAVGELVQAKTSMVQENPLTNSLISFGTMGADYCSIANSVLTAQVTPQQLEISQSLRPGLGPVSGGFPVAASDFRQMLQQNLSASVGPLDSMRRLRLSRAEGRLEGPTDTLLYGLCGVDPRVGSTPLNVGVADMCLSALYLHELNQQKRQARQSRIDEAEDERPGTSHWPPRPPAAPSADTGFGSRHTVITSKAAESTPLLGSIRS
Protein: Suppressor of activated egl-4 protein 1 (A8WHS5)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRNGSGLFCQIVKSANSSLPVAEQSPDAPSCSTNGVDGDMKHLMNGKKRSEDGDGPSRKNGFFYMAQQMNQTNFANELEALRKESWASTSSADEKMQTERKESLESIRKASCMSDSYYEIEEGPKISDPNPHINLGKNYQARVKKWCDRQVSTSERDAIEDRDEIVFSSEILQDIDPEQITAFELLACSQACPRAGRNKELALHLLMENKGNIEAAVEDLLRSDTLDWEHYSSVFGYMYNDSVLWTPDEIYQFQDAIYQSEKDFDKVAVELPGKSVKECVQFYYTWKKDCPDDYRKLRNLRRKRQLLDINLQKNQSEEPVVPAKKISIIESGDSDNESNATDSSFIGNGHMEFRDRAFTSPMMSSPREEPIIGLSPSSKDLFGIQKNYQPTAPRAHHTPSASASKKGAQPSADGFFHCRLCDKCFEKVKSLNAHMKSHAMKARAEQEAKAHDAQVAAAAAAQLTSAVGNVVGNPVATSPLNSFANGHLGISIPSTIGNLTPQQLTPQQLNLNQQLQTQLNSLSNQMSLNSPLTPQQQLQQFTQQHLMARAMQQNLFQPVTSTPLVQPTHPLIQAGLHSIN
Protein: Outer capsid glycoprotein VP7 (P12476)
Organism: Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A)
Function: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960, ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:2832610}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:15596814, ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:2832610}.
Interaction partners:
Sequence:
MYGIEYTTVLTFLISLILLNYILKSLTRMMDFIIYRFLFIVVILSPLLKAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTDIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTATFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDVLDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVNQIIQAMSKRSRSLNSAAFYYRI
Protein: Cysteine-rich protein 2 (CRP-2) (Heart LIM protein) (Q9DCT8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Alpha-defensin 20
- Serum response factor
Sequence:
MASKCPKCDKTVYFAEKVSSLGKDWHKFCLKCERCNKTLTPGGHAEHDGKPFCHKPCYATLFGPKGVNIGGAGSYIYEKPQTEAPQVTGPIEVPVVRTEERKTSGPPKGPSKASSVTTFTGEPNMCPRCNKRVYFAEKVTSLGKDWHRPCLRCERCSKTLTPGGHAEHDGQPYCHKPCYGILFGPKGVNTGAVGSYIYDKDPEGTVQP
Protein: Os06g0570900 protein (Q5Z610)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MDAIFALPPDARARAMGRAAARLPGCLYLCLWAPAAAIAGGVQPNHLFCLDAWIGGGGGVGAGGGGGDRALELFEAYRGALCAAVSGCVPGWAYKEGAACMELTEHDLAASASLQVQQQFYHETGTKMAVFMGCDSGEIEVGLSAASATATAAVVGEMQQSILEELLQMPPPPPSPSSSSLLSLSVGSPEYSSLVRSMATSVGASAAADPSPVHGGLLAPVYGEFPGSDDDAAMAQAMLAVISTPAPPPPLWRPPRRRARSSSSPRRATAFKAYNAALSPRARPRPGAPGQRMIKTGISLLASVHMQTRSRELAAARQRDTHAAPPPPPPPPPPSSSQLHHMISERRRRERINDSFQTLRALLPLPPDSKKDKAAILASTTEYMDKLISQVSELGEKNRQLEAQLAARSGEAQWPAASGGGGGESSSERVQVDVVIAGSSASTDQPREVSIRVTVRAECDVSELVVAVLARLREMGRFAVVSVDAGRRSSSFAQASLTFRVMAGDVCDETSLKEAVAKAVDGAVTAPPPPVAPPPPTSP
Protein: Early endosome antigen 1 (Endosome-associated protein p162) (Zinc finger FYVE domain-containing protein 2) (Q15075)
Organism: Homo sapiens (Human)
Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
Subcellular location: Cytoplasm. Early endosome membrane; Peripheral membrane protein.
Interaction partners:
- Ras-related protein Rab-5A
- Ras-related protein Rab-5C
- Rab5 GDP/GTP exchange factor
- Rab GTPase-binding effector protein 1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Syntaxin-6
- Ras-related protein Rab-5B
- Lysosome-associated membrane glycoprotein 1
- Transferrin receptor protein 1
- Ras-related protein Rab-11A
Sequence:
MLRRILQRTPGRVGSQGSDLDSSATPINTVDVNNESSSEGFICPQCMKSLGSADELFKHYEAVHDAGNDSGHGGESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDLQG
Protein: Pumilio homolog 1 (APUM-1) (AtPUM1) (Q9ZW07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Pumilio homolog 24
- Pumilio homolog 23
- S-protein homolog 17
- Putative pumilio homolog 22
- Pumilio homolog 26
- Protein EXPORTIN 1B
- Gamma-aminobutyrate transaminase POP2, mitochondrial
- Protein EXPORTIN 1A
Sequence:
MIPELGRRPMHRGNEDSSFGDDYEKEIGVLLGEQQRRQVEADELERELNLFRSGSAPPTVDGSVSAAGGLFSGGGGAPFLEFGGVNKGNGFGGDDEEFRKDPAYLSYYYANMKLNPRLPPPLMSREDLRVAQRLKGSNNVLGGVGDRRKVNDNRSLFSMPPGFEGEKTGASASEWDANGLIGLPGLGLGGKQKSFADIFQADMGHGHPVAQQPSRPASRNTFDENVDSNNNLSPSASQGIGAPSPYSYAAVLGSSLSRNGTPDPQAIARVPSPCLTPIGSGRMSSNDKRNTSNQSPFNGVTSGLNESSDLVNALSGLNLSCSVGLDDRSQAEQDVEKVRNYMFGLQGGHNEVNQHEFPNKSDQAHKATGSLRNSQLRGPHGSAYNGGVGLANPYQQLDSPNYCLNNYALNPAVASMMANQLGNNNFAPMYDNVSALGFSGMDSRHHGRGFVSSGQNLSESRNLGRFSNRMMGGGAGLQSHMVDPMYNQYADSLDLLNDPSMDRNFMGGSSYMDMLELQRAYLGAQKSQYGVPYKSGSPNSHSYYGSPTFGSNMSYPGSPLAHHGMPNSLMSPYSPMRRDEVNMRFPSATRNYSGGLMGSWHMDASFDEGFGSSMLEEFKSNKTRGFELSEIAGHVVEFSSDQYGSRFIQQKLETATTDEKNMVYEEIMPQALVLMTDVFGNYVIQKFFEHGLPPQRRELAEKLFDHVLPLSLQMYGCRVIQKAIEVVDLDQKIKMVKELDGHVMRCVRDQNGNHVVQKCIECVPEENIEFIISTFFGHVVTLSTHPYGCRVIQRVLEHCHDPDTQSKVMEEILSTVSMLAQDQYGNYVVQHVLEHGKPDERTVIIKELAGKIVQMSQQKFASNVVEKCLTFGGPEERELLVNEMLGTTDENEPLQAMMKDQFANYVVQKVLETCDDQQRELILTRIKVHLTALKKYTYGKHVVARIEKLVAAGERRMALQSLTQPQMA
Protein: Histamine H3 receptor (H3R) (HH3R) (Q9QYN8)
Organism: Rattus norvegicus (Rat)
Function: The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system. Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Histidine decarboxylase
- Histamine N-methyltransferase
Sequence:
MERAPPDGLMNASGTLAGEAAAAGGARGFSAAWTAVLAALMALLIVATVLGNALVMLAFVADSSLRTQNNFFLLNLAISDFLVGAFCIPLYVPYVLTGRWTFGRGLCKLWLVVDYLLCASSVFNIVLISYDRFLSVTRAVSYRAQQGDTRRAVRKMALVWVLAFLLYGPAILSWEYLSGGSSIPEGHCYAEFFYNWYFLITASTLEFFTPFLSVTFFNLSIYLNIQRRTRLRLDGGREAGPEPPPDAQPSPPPAPPSCWGCWPKGHGEAMPLHRYGVGEAGPGVEAGEAALGGGSGGGAAASPTSSSGSSSRGTERPRSLKRGSKPSASSASLEKRMKMVSQSITQRFRLSRDKKVAKSLAIIVSIFGLCWAPYTLLMIIRAACHGRCIPDYWYETSFWLLWANSAVNPVLYPLCHYSFRRAFTKLLCPQKLKVQPHGSLEQCWK
Protein: Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Nucleoporin Nup62) (P37198)
Organism: Homo sapiens (Human)
Function: Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:1915414}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:24107630}. Nucleus envelope {ECO:0000269|PubMed:24107630}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24107630}. Note=Central region of the nuclear pore, within the transporter (PubMed:1915414). During mitotic cell division, it associates with the poles of the mitotic spindle (PubMed:24107630). {ECO:0000269|PubMed:1915414, ECO:0000269|PubMed:24107630}.
Interaction partners:
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup88
- Nucleoporin p54
- Nucleoporin p58/p45
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup155
- Nuclear transport factor 2
- Nuclear pore complex protein Nup107
Sequence:
MSGFNFGGTGAPTGGFTFGTAKTATTTPATGFSFSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQTTGFTFGTATLASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTGLSLCTPVTTAGAPTAGTQGFSLKAPGAASGTSTTTSTAATATATTTSSSSTTGFALNLKPLAPAGIPSNTAAAVTAPPGPGAAAGAAASSAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEELVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNTSGAPADTSDPLQQICKILNAHMDSLQWIDQNSALLQRKVEEVTKVCEGRRKEQERSFRITFD
Protein: Plexin domain containing 1 (D3ZEE4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRAQLWLLQLLLLCGTARALSPATPAGHDERQGSAWTAKRTRQGWNRRVRESPGQVLKPGKTQLSQDLGGDSLAIDTLPDNRTRVVVLSLSLQEDNHNYYVSRVYGPGEQRTRDLWVDLSVANRNHVKVHRILSSSHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVLHRMLTATQYVAPLMANFNPGYSDNSTVAYFDNGTVFVVQWDHVYLQGREDRGSFTFQAALHQDGRIVFGYKEIPMAVLDISSAQHPVKAGLSDAFMILNSSPEVPESRRRTIFEYHRVELDSSKITTTSAVEFTPLPTCLQHQSCDACMSSNLTFNCSWCYVLQRCSSGFDRYRQEWLTYGCAQEAEGKTCEHFQDEGHYSASPDSSFSPSDGGSTTSSSLFIDSLTTEDDTKLNPYAEGDGLPDNSSPKTKGPPVHLGTIVGIVLAVLLVAAIILAGIYISGHPNSNAALFFIERRPHHWPAMKFHNHPNHSTYTEVEPSGHEKEGFVEAEQC
Protein: Iron-binding protein YfeA (Periplasmic chelated iron-binding protein YfeA) (Q56952)
Organism: Yersinia pestis
Function: Part of an ATP-driven transport system YfeABCD for chelated iron.
Subcellular location: Periplasm {ECO:0000269|PubMed:31478906}.
Interaction partners:
- Chelated iron transport system membrane protein YfeC
- Chelated iron transport system membrane protein YfeB
- Chelated iron transport system membrane protein YfeD
- Similar to Escherichia coli high-affinity zinc uptake system membrane protein ZnuB SW:ZNUB_ECOLI
- Zinc import ATP-binding protein ZnuC
- Putative cobalamin synthesis protein
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein bL28
- Divalent metal cation transporter MntH
- High-affinity zinc uptake system protein ZnuA
Sequence:
MIERLNSPFLRAAALFTIVAFSSLISTAALAENNPSDTAKKFKVVTTFTIIQDIAQNIAGDVAVVESITKPGAEIHDYQPTPRDIVKAQSADLILWNGMNLERWFEKFFESIKDVPSAVVTAGITPLPIREGPYSGIANPHAWMSPSNALIYIENIRKALVEHDPAHAETYNRNAQAYAEKIKALDAPLRERLSRIPAEQRWLVTSEGAFSYLAKDYGFKEVYLWPINAEQQGIPQQVRHVIDIIRENKIPVVFSESTISDKPAKQVSKETGAQYGGVLYVDSLSGEKGPVPTYISLINMTVDTIAKGFGQ
Protein: GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) (Glutamine amidotransferase) (Q8WSN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSNIFLGTAENGLRHDKIVILDAGAQYGKVIDRKVRELFVETDILPLDTPAATIRNNGYRGIIISGGPNSVYAEDAPSYDPDLFKLKIPMLGICYGMQLINKEFGGTVLKKDVREDGQQNIEIETSCPLFSRLSRTQSVLLTHGDSVERVGENLKIGGWSTNRIVTAIYNEVLRIYGVQFHPEVDLTINGKQMLSNFLYEICELTPNFTMGSRKEECIRYIREKVGNNKVLLLVSGGVDSSVCAALLRRALYPHQIIAVHVDNGFMRKKESEKVERSLRDIGIDLIVRKEGYTFLKGTTQVKRPGQYSVVETPMLCQTYNPEEKRKIIGDIFVKVTNDVVAELKLKPEEVMLAQGTLRPDLIESASSMVSTNAETIKTHHNDTDLIRELRNAGRVVEPLCDFHKDEVRDLGNDLGLPQELVERQPFPGPGLAIRVLCAEEAYMEKDYSETQVIIRVIVDYKNKLQKNHALINRVTAATSEAEQKDLMRISSNSQIQATLLPIRSVGVQGDKRSYSYVVGLSTSQEPNWQDLLFLAKIIPRILHNVNRVCYIFGEPVQYLVTDITHTTLNTVVLSQLRQADDIANEVSGFVIEINKMYYIITVLDHNASWTIRKISQMPVVLIPVHFDRDPINRTPSCRRSVVLRPFITNDFMTGVPAEPGSGQMPLQVSQFSIFLKNVYLIFSCSKVLNQIVRDISKLDGISRVLYDLTAKPPGTTEWE
Protein: LD08622p (Nuclear fallout, isoform B) (Q8T0E0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MYSDISLENRHDYDYRLELLQRKVDDLSDTQNIAEDRTTRTKTEYAVLQARYHMLEEQYRESELRAEERLAEEQKRHREILARVEREASLQNENCQMKIRATEIEATALREEAARLRVLCDKQANDLHRTEEQLELARDQIGVLQQEHEEQAQALRRHEQEKKSTEELMLELGRELQRAREESGARAMPTTSPESIRLEELHQELEEMRQKNRTLEEQNEELQATMLTNQATMLTNGVEQGRHLLNGTLNSLAQELEEMSQAQLQQAFQEKEDENVRLKHYIDTILLNIVENYPQLLEVKPMERK
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q38F27)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- MRH domain-containing protein
- Protein OS9-like domain-containing protein
- Katanin p60 ATPase-containing subunit A-like 2
- Derlin
- Derlin
- UBX domain-containing protein
Sequence:
MLSLYAYIFLSLVVTIGFVVDYATVYTDFFSLVVALTDSPIFRLLCVNSFIALSWVLWLVARFTFFGTLSRTESDAVRSVTPVYAMEFIVCPLYFGISTLSSAGVVSLVTVVVAVLHRLAQERVSTLQVMEDRVLRTPMLVRLLIFLYLFSMIDLYVVFDMIGNTAESYGDQLSMQYCIALLYVQFLISILKSFTQLFFTVATKESTYNSLAFYMEMFFSLSNNVVFFISFLYICTSSYVPFPLMRMFLQNMIMCGKNVRLVARYRKLTALLREIPNATEEILSRDPHCAICYDDMSPDQTCKQLPCGHCYHEACLLHWFEKMSTCPYCRSDIAQRTSAMAAYAKRVRVPADATTTPSEQTGSDASATPSPEDDTTSMPMPSEEEMRRSYERYLAEMASRQRAQGAAISAEADASRLGEEVSAASTDRFSVVEEINKSLTQSNAVRSVDVPAVSTKEAQRLAAYEEHAAAVRAAQEKLQQRLKSIDAS
Protein: Mannose-specific lectin (ASAL) (ASARI) (Allimin) (Leaf agglutinin) (Root agglutinin) (P83886)
Organism: Allium sativum (Garlic)
Function: Mannose-specific lectin. Shows agglutinating activity towards rabbit erythrocytes. However, it does not show agglutinating activity towards human erythrocytes. Has insecticidal activity against the cotton leafworm S.littoralis and the peach potato aphid M.persicae. Also displays antiviral activity and therefore may contribute to defense against infections.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P49329}.
Interaction partners:
Sequence:
MGRTTSSPKAMMRIATVAAILTILASTCMARNVLTNGEGLYAGQSLDVEQYKFIMQDDCNLVLYEYSTPIWASNTGVTGKNGCRAVMQRDGNFVVYDVNGRPVWASNSVRGNGNYILVLQKDRNVVIYGSDIWSTGTYRRSVGGAVVMAMNGTVDGGSVIGPVVVNQNVTAAIRKVGTGAA
Protein: Periplasmic trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (Q9I165)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_01060}.
Interaction partners:
- Malto-oligosyltrehalose trehalohydrolase
- maltose alpha-D-glucosyltransferase
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- 1,4-alpha-glucan branching enzyme GlgB
- Catalase HPII
Sequence:
MPDRTALPRAMLAAWVLLLLAACSQGPAPTPPASWGWQDASGERAIAPDEAYPELFQAVQENRLFSDQKHFVDALPLREPARIRADYLRERERPGFDLRAFVGRNFEESGSVETAPPEAGADLASHISDLWPALTRHYEQVPAHSSLLPLPKPYVVPGGRFREVYYWDSYFTMLGLAESGQHQRVRDMLDNFAYLIDTYGHIPNGNRSYYLSRSQPPFFAYMVDLQARREGDAAYRRYLPQLQKEYAYWMEGSAGLRPNEARLHVVKLADGSLLNRYWDNRDTPRQESFLEDRATAARAPQRPAGEVYRDLRAGAESGWDFSSRWLDDGRELASIRTTAIVPVDLNALLYHLERIIAKACASSALKACEQGYGARAEKRRQAIEDHLWHPAGYYADYDWQRRRPIERINAASLFPLFTGLASAERAGRTADSVAAQLLRPGGLATTTRASGQQWDEPNGWAPLQWVAVQGLRAYGRDALAEDIGRRFLAQVQQVYDREGKLVEKYDISGNQGGGGGGEYPLQDGFGWSNGVTLQLLRLYGPGAGR