wanglab/gogpt-training-data huggingface dataset:
Protein: Drainin (TBC1 domain family member 12 homolog) (O96904)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a GTPase-activating protein for Rab family protein(s) (By similarity). Required for osmotic regulation by the contractile vacuole in hypo-osmotic environments. Essential for periodic fusion of the contractile vacuole with the plasma membrane and consequent expulsion of water from the cell body.
Subcellular location: Contractile vacuole membrane. Cytoplasm.
Interaction partners:
- BEACH domain-containing protein lvsA
- Ras-related protein Rab-11A
- Ras-related protein Rab-8A
Sequence:
MICFDNSTAHTDSNNNNNQCDLPENYKELVTTGKVEKLILSPSSSLDRPKTLPPKSQEEVLKHQREYEEIQRKAKKTLEREAKEKEKLDAIRKEKERSLIDARKVWEEDIIPVWEKNSKKRDIKKIKDLSWRGLPPAVRGKIWRLCIGNDLRVTDELFNIFLGHANNAYNKTTSPPLKSSLSSSSKSPNINIDLRQANNSIHHSRSPMNTSTDGEDDVLDLETTNMALILQDIQDTFPSLMIFQKGGPLHSDLIDVLGAYICYRPDIGYVPGMTFLAAMFLLNMEKCDAFLSLSNHINSVCFLPFFRQDQSGIPKYLAAMDSTVEALTPPLHKHFKEIGISAKNYLVDWITTLFSKALPLDVATRIWDLVFIEGEIFIYRTALSILRYFISDLIQATYDECIDLFNKLPQRKISEDKLFEEIQSIVLDQRKFDKLLEK
Protein: Group 2 truncated hemoglobin GlbO (Hemoglobin-like protein HbO) (Truncated hemoglobin) (trHbO) (P9WN23)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: When expressed in E.coli and M.smegmatis, HbO increases oxygen uptake. Membrane vesicles of E.coli carrying HbO show a respiration activity about twice that of membranes without HbO. HbO seems to interact with a terminal oxidase. Therefore, HbO could participate in oxygen/electron-transfer process, suggesting a function related to the facilitation of oxygen transfer during aerobic metabolism of M.tuberculosis.
Subcellular location: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Group 1 truncated hemoglobin GlbN
- Probable alpha-glucosidase AglA
- HNH nuclease domain-containing protein
Sequence:
MPKSFYDAVGGAKTFDAIVSRFYAQVAEDEVLRRVYPEDDLAGAEERLRMFLEQYWGGPRTYSEQRGHPRLRMRHAPFRISLIERDAWLRCMHTAVASIDSETLDDEHRRELLDYLEMAAHSLVNSPF
Protein: GDP-mannose 3,5-epimerase (GDP-Man 3,5-epimerase) (EC 5.1.3.18) (Q93VR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a reversible epimerization of GDP-D-mannose that precedes the committed step in the biosynthesis of vitamin C (L-ascorbate), resulting in the hydrolysis of the highly energetic glycosyl-pyrophosphoryl linkage. Able to catalyze 2 distinct epimerization reactions and can release both GDP-L-galactose and GDP-L-gulose from GDP-mannose.
Interaction partners:
- GDP-L-galactose phosphorylase 1
- GDP-L-galactose phosphorylase 2
- Mannose-1-phosphate guanylyltransferase 1
- GDP-mannose 4,6 dehydratase 2
- ADP-glucose pyrophosphorylase family protein
- GDP-mannose 4,6 dehydratase 1
- ADP-glucose pyrophosphorylase family protein
- Probable mannose-1-phosphate guanylyltransferase 2
- Probable mannose-1-phosphate guanylyltransferase 3
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
Sequence:
MGTTNGTDYGAYTYKELEREQYWPSENLKISITGAGGFIASHIARRLKHEGHYVIASDWKKNEHMTEDMFCDEFHLVDLRVMENCLKVTEGVDHVFNLAADMGGMGFIQSNHSVIMYNNTMISFNMIEAARINGIKRFFYASSACIYPEFKQLETTNVSLKESDAWPAEPQDAYGLEKLATEELCKHYNKDFGIECRIGRFHNIYGPFGTWKGGREKAPAAFCRKAQTSTDRFEMWGDGLQTRSFTFIDECVEGVLRLTKSDFREPVNIGSDEMVSMNEMAEMVLSFEEKKLPIHHIPGPEGVRGRNSDNNLIKEKLGWAPNMRLKEGLRITYFWIKEQIEKEKAKGSDVSLYGSSKVVGTQAPVQLGSLRAADGKE
Protein: Receptor L-domain domain-containing protein (G8B6F2)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKFNFVTLLAILASGVFAADETNTTTTARSTTTTTGSNSKSTSTSSTDTCSFSRTTITNATALQQLTSCETLDGEITISGNEFASIDLPQLREIAGDVTVINSKSIVAINLNQLRSIDGKLTVTNMTQLNTIDLSSLRNSQDLELVSLPSFANLVLNRELERAGKVILSDTALTNLNGLTSFNNIQYMNINNNKNITQIQFPNLRSVTDALILSFNNDDAVVELNDLEWAANLTVQSVGQLSASELRAVNGTLQVSYNLFESLNLSTLTYVGSSLQVFAHDELTSIDFKSLREIGGELSLFNNSELHDLQNAFPSLEVVEGAVAISGDIANLSMNSLEKVKGDFQLNSTSEDFDCSDFDQLHDDGDIEGNNYICSTAVAESELQSAATGTTTRSGSTSTNTGSSSEETGSPNKSNGANKLFISSLVMPLGLILAVALL
Protein: Protocadherin beta 22 (Q91XZ8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MKIGREHRKRQVLLIFLLLGVVGAGSEPRRYFVMEETPSGTVLADLVQDLGLGVAELAARGAQVVSEEKESRLQLDLQTGKLILNEKLDREELCGSTEPCVTHFQVLLKKPLEIFQAELRVGDINDHSPEFPEREMAVKIIENSPVGTAFLLKTAQDLDVGNNSVQNYKIGTNSHFHVSIRNRGDGRKYPELVLDKELDREVQAAFRLTLTALDGGSPPRTGTSQIRIVVLDVNDNAPEFAQAFYRVQIPENSPSGSMVAKVSAKDLDTGTNGEVSYSLFHSSQEMSKTFELNALSGEVRLIKTLDFETTPSYELDIEATDGGGLSGKCSVSIQVVDVNDNYPELIISSLTNPIPENSPETEVALFRIRDRDSGENGRTICSIQDGVPFTLEPSVENFYRLVTDGALDREIRAEYNITISVTDLGIPKLTTQHTITVQVSDINDNAPAFTQVSYTMLVHENNSPALHIGTISATDSDSGSNAHITYSLLPAQEPQLALNSLISINADNGQLFALRALDYEALQAFEFHVSATDRGSPALSSQALVRIVVLDDNDNAPFVLYPMQNASAPCTELLPRAAEPGYLVTKVVAVDRDSGQNAWLSFQLLKATEPGLFSVWAHNGEVRTTRLLSERDVPKHRLLLVVKDNGEPPRSASVTLQVLMVDGFSQPYLPLPEVVRDPSHQEGDVLTLYLVIALASVSSLFLLSVLLFVGVRLCRRAREVSLGGCSVPEGHFPGHLVDVSGAGTLSQSYQYEVCLTGDSQSNEFKFLKPVFSGIVDQNYGRQPDDQSFSSVLGM
Protein: MIOREX complex component 9 (Mitochondrial organization of gene expression protein 9) (Q07349)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}. Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutaredoxin-like protein YDR286C
- Mitochondrial peculiar membrane protein 1
Sequence:
MFKVPVGLASRTRELMNSVTLNSLNNGKGFNMYLPGILRAFPKPVPSAITSPAIPKYRGESFQFRKLSCISSNYCSTTHQFLSSLKSSTSRLVGKRAFHSSRRAEIKFIFSSKSPKNGNKPFVKVYKVSPFFIIFATASIFTFILTSTIVVIPLIFHFFFPLLIMFFFFKQFKKWQKNIFYKDVLTSLPKTKLKITLPTMRSLQLQPMVQSWKEISSRMGIPNEFAKGLNVDLVKQEETRKQFLSFLQKRVLESFTKNELGIRSYFLGDSVEKWIKESYDLELDIDNCRSELRKFQTFIFSSVRYKLYLDSMKNLPLNPSKKLEGKKHIADVYVIILDESFPAIMFNGGAYSKADFFKILQESETSNSSKTLNTIIAIKSVNTLLSKHFVITTNGDSGEFFSKYNISKINDKNTEYTLKE
Protein: Presenilin sel-12 (Suppressor/enhancer of lin-12 protein 12) (P52166)
Organism: Caenorhabditis elegans
Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Provides the major presenilin function compared to hop-1 and spe-4. Required cell-autonomously for correct neurite connectivity of the AIY cholinergic interneurons and their correct functioning in thermotaxis. Required for mesodermal patterning of muscle function. Promotes basement membrane gap formation during tissue remodeling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gamma-secretase subunit pen-2
- Nicastrin
- Gamma-secretase subunit aph-1
- Protein lin-12
- Beta-catenin-like protein hmp-2
- Beta-catenin/armadillo-related protein 1
- cAMP-dependent protein kinase catalytic subunit
- Presenilin spe-4
- Presenilin hop-1
- Armadillo repeat-containing protein wrm-1
Sequence:
MPSTRRQQEGGGADAETHTVYGTNLITNRNSQEDENVVEEAELKYGASHVIHLFVPVSLCMALVVFTMNTITFYSQNNGRHLLYTPFVRETDSIVEKGLMSLGNALVMLCVVVLMTVLLIVFYKYKFYKLIHGWLIVSSFLLLFLFTTIYVQEVLKSFDVSPSALLVLFGLGNYGVLGMMCIHWKGPLRLQQFYLITMSALMALVFIKYLPEWTVWFVLFVISVWDLVAVLTPKGPLRYLVETAQERNEPIFPALIYSSGVIYPYVLVTAVENTTDPREPTSSDSNTSTAFPGEASCSSETPKRPKVKRIPQKVQIESNTTASTTQNSGVRVERELAAERPTVQDANFHRHEEEERGVKLGLGDFIFYSVLLGKASSYFDWNTTIACYVAILIGLCFTLVLLAVFKRALPALPISIFSGLIFYFCTRWIITPFVTQVSQKCLLY
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2 (EC 2.1.1.14) (Cobalamin-independent methionine synthase 2) (AtMS2) (Q9SRV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15024005}.
Interaction partners:
- Adenosylhomocysteinase 2
- Adenosylhomocysteinase 1
- Cystathionine beta-lyase, chloroplastic
- Homocysteine S-methyltransferase 1
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 3
- S-adenosylmethionine synthase 3
- S-adenosylmethionine synthase 2
- Cystathionine gamma-synthase 1, chloroplastic
- S-adenosylmethionine synthase 1
Sequence:
MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLLLSKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGKDKLVVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFTANADALSSRRSSPRVTNESVQKAAAALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQLGSAK
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (Q6FXZ0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein eS25
- RP28
- L17A
- Large ribosomal subunit protein uL30
- Candida glabrata strain CBS138 chromosome M complete sequence
- Small ribosomal subunit protein uS14
- 40S ribosomal protein S7
- L33
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
Sequence:
MAPIKTQESINQKLALVVKSGKFTLGYKSTIKSLRQGKSKLIIIAANTPVLRKSELEYYAMLSKTKVYYFQGGNNELGTAVGKLFRVGVVSVLDAGDSDILTALA
Protein: Methionine aminopeptidase 1 (MAP 1) (MetAP 1) (EC 3.4.11.18) (Peptidase M 1) (O59730)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Methionine aminopeptidase 2
- ER-derived vesicles protein erv14
- Zinc-regulated GTPase metalloprotein activator 1
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Guanine nucleotide-binding protein alpha-1 subunit
- Small ribosomal subunit protein uS3
Sequence:
MATEIAKHICCGIDCNNEADRLQCPKCLNDGVKSYFCGQECFRNSWNIHKHLHRPPNVEKREDGTYNPFPKFHFAGSLKPVYPLSPIRKVPPHIKRPDYAKTGVSRSEQIEGRSFKLKRLTPKEQEGMRKVCRLGREVLDAAAAAVRPGTTTDELDSIVHNACIERDCFPSTLNYYAFPKSVCTSVNEIICHGIPDQRPLEDGDIVNIDVSLYHNGFHGDLNETYYVGDKAKANPDLVCLVENTRIALDKAIAAVKPGVLFQEFGNIIEKHTNSITEKQISVVRTYCGHGINQLFHCSPSIPHYSHNKAPGIARPGMTFTIEPMLTLGPARDITWPDDWTSSTASGRCSAQFEHTLLVTETGCEVLTARLPNSPGGPLK
Protein: Ganglioside-induced differentiation-associated protein 2 (Q9DBL2)
Organism: Mus musculus (Mouse)
Interaction partners:
- Core histone macro-H2A.2
- WD repeat-containing protein 3
Sequence:
MDPLGAPSQFVDVDTLLSWGDSYEDEVDCADSTAEAFQEDASRSPFVYSRDVNGKVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYKSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGENIEKVVFAVSELEEATYQKLLPLYFPRSLKEEIRSLPYLPADIGNAEGEPVVPERQIRISEKPGASEDNEEEDEDEGLGVDLSFIGSHAFARMEGDIDKQRKLILQGQLSEAALQKQHQRNYNRWLCQARSEDLSDIASLKALYQTGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAVKEYVLVYFHTLTSDYNHLDSDFLKKLYDVVDIKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFPPFVLEYDARENGPYFASYPPSPDL
Protein: Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) (Q61625)
Organism: Mus musculus (Mouse)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex.
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:24357660}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cerebellin-1
- Neurexin-1
- Neurexin-3
- Delphilin
- Neurexin-2
- Glutamate receptor 1
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor 4
Sequence:
MEVFPLLLFLSFCWSRTWDLATADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI
Protein: Kelch repeat and BTB (POZ) domain containing 2 (Q8R1W9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSPDGTEEFELDGEMVALPPV
Protein: Nestin (P48681)
Organism: Homo sapiens (Human)
Function: Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity).
Interaction partners:
- Synemin
- RNA binding protein fox-1 homolog 3
- Cyclin-dependent kinase 5
- Transcription factor SOX-2
- CD44 antigen
- Glial fibrillary acidic protein
- Neuronal migration protein doublecortin
- Vimentin
- Paired box protein Pax-6
- Neurofilament medium polypeptide
Sequence:
MEGCMGEESFQMWELNRRLEAYLARVKALEEQNELLSAELGGLRAQSADTSWRAHADDELAALRALVDQRWREKHAAEVARDNLAEELEGVAGRCQQLRLARERTTEEVARNRRAVEAEKCARAWLSSQVAELERELEALRVAHEEERVGLNAQAACAPRCPAPPRGPPAPAPEVEELARRLGEAWRGAVRGYQERVAHMETSLGQARERLGRAVQGAREGRLELQQLQAERGGLLERRAALEQRLEGRWQERLRATEKFQLAVEALEQEKQGLQSQIAQVLEGRQQLAHLKMSLSLEVATYRTLLEAENSRLQTPGGGSKTSLSFQDPKLELQFPRTPEGRRLGSLLPVLSPTSLPSPLPATLETPVPAFLKNQEFLQARTPTLASTPIPPTPQAPSPAVDAEIRAQDAPLSLLQTQGGRKQAPEPLRAEARVAIPASVLPGPEEPGGQRQEASTGQSPEDHASLAPPLSPDHSSLEAKDGESGGSRVFSICRGEGEGQIWGLVEKETAIEGKVVSSLQQEIWEEEDLNRKEIQDSQVPLEKETLKSLGEEIQESLKTLENQSHETLERENQECPRSLEEDLETLKSLEKENKELLKDVEVVRPLEKEAVGQLKPTGKEDTQTLQSLQKENQELMKSLEGNLETFLFPGTENQELVSSLQENLESLTALEKENQEPLRSPEVGDEEALRPLTKENQEPLRSLEDENKEAFRSLEKENQEPLKTLEEEDQSIVRPLETENHKSLRSLEEQDQETLRTLEKETQQRRRSLGEQDQMTLRPPEKVDLEPLKSLDQEIARPLENENQEFLKSLKEESVEAVKSLETEILESLKSAGQENLETLKSPETQAPLWTPEEINQGAMNPLEKEIQEPLESVEVNQETFRLLEEENQESLRSLGAWNLENLRSPEEVDKESQRNLEEEENLGKGEYQESLRSLEEEGQELPQSADVQRWEDTVEKDQELAQESPPGMAGVENEDEAELNLREQDGFTGKEEVVEQGELNATEEVWIPGEGHPESPEPKEQRGLVEGASVKGGAEGLQDPEGQSQQVGAPGLQAPQGLPEAIEPLVEDDVAPGGDQASPEVMLGSEPAMGESAAGAEPGPGQGVGGLGDPGHLTREEVMEPPLEEESLEAKRVQGLEGPRKDLEEAGGLGTEFSELPGKSRDPWEPPREGREESEAEAPRGAEEAFPAETLGHTGSDAPSPWPLGSEEAEEDVPPVLVSPSPTYTPILEDAPGPQPQAEGSQEASWGVQGRAEALGKVESEQEELGSGEIPEGPQEEGEESREESEEDELGETLPDSTPLGFYLRSPTSPRWDPTGEQRPPPQGETGKEGWDPAVLASEGLEAPPSEKEEGEEGEEECGRDSDLSEEFEDLGTEAPFLPGVPGEVAEPLGQVPQLLLDPAAWDRDGESDGFADEEESGEEGEEDQEEGREPGAGRWGPGSSVGSLQALSSSQRGEFLESDSVSVSVPWDDSLRGAVAGAPKTALETESQDSAEPSGSEEESDPVSLEREDKVPGPLEIPSGMEDAGPGADIIGVNGQGPNLEGKSQHVNGGVMNGLEQSEEVGQGMPLVSEGDRGSPFQEEEGSALKTSWAGAPVHLGQGQFLKFTQREGDRESWSSGED
Protein: F-box/WD repeat-containing protein 4 (Dactylin) (F-box and WD-40 domain-containing protein 4) (P57775)
Organism: Homo sapiens (Human)
Function: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling.
Interaction partners:
- S-phase kinase-associated protein 1
- DNA polymerase lambda
- Cullin-1
- Transcription factor LBX1
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit eta
- Thioredoxin domain-containing protein 9
Sequence:
MAAAAGEEEEEEEAARESAARPAAGPALWRLPEELLLLICSYLDMRALGRLAQVCRWLRRFTSCDLLWRRIARASLNSGFTRLGTDLMTSVPVKERVKVSQNWRLGRCREGILLKWRCSQMPWMQLEDDSLYISQANFILAYQFRPDGASLNRRPLGVFAGHDEDVCHFVLANSHIVSAGGDGKIGIHKIHSTFTVKYSAHEQEVNCVDCKGGIIVSGSRDRTAKVWPLASGRLGQCLHTIQTEDRVWSIAISPLLSSFVTGTACCGHFSPLRIWDLNSGQLMTHLGSDFPPGAGVLDVMYESPFTLLSCGYDTYVRYWDLRTSVRKCVMEWEEPHDSTLYCLQTDGNHLLATGSSYYGVVRLWDRRQRACLHAFPLTSTPLSSPVYCLRLTTKHLYAALSYNLHVLDFQNP
Protein: Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (B6DTP5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MSSYSSDRDRGRDRGFGAPRFGGSRTGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVDTYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSDVANMHNGMNQQAYAYPATAAAAPMIGYPMPTGYS
Protein: Type II secretion system protein H (General secretion pathway protein H) (E0SLG0)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004377}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004377}.
Interaction partners:
- Type II secretion system protein J
- Type II secretion system protein L
- Type II secretion system core protein G
- Type II secretion system protein M
- Type II secretion system protein K
- Type II secretion system protein C
- Type II secretion system protein I
- Secretin OutD
- Type II secretion system protein F
- Type II secretion system protein E
Sequence:
MRQRGFTLLEIMLVVLLAGVAATLVMMAIPAPKQQDSGWQIARFKAQLQYAVEDSQMNDHILGIYIQPRRWQYALLQRQVVENSPDDQQRLRYVWVPWQPYRMSSPSELPDGFQIELSTQVGAAGDGAGFSPGNGDPHILILPGGEVTPFRLTLRNGNDSAWLQVDTNGRVQTSPEAEQ
Protein: Helix-loop-helix DNA-binding domain containing protein (Q2R0R9)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDARCANIWSSADARSEESEMIDQLKSMFWSSTDAEINFYSPDSSVNSCVTTSTMPSSLFLPLMDDEGFGTVQLMHQVITGNKRMFPMDEHFEQQQKKPKKKTRTSRSVSSSSTITDYETSSELVNPSCSSGSSVGEDSIAATDGSVVLKQSDNSRGHKQCSKDTQSLYAKRRRERINERLRILQQLVPNGTKVDISTMLEEAVQYVKFLQLQIKLLSSDDTWMFAPLAYNGMNMDLGHTLAENQE
Protein: Receptor homology region, transmembrane domain- and RING domain-containing protein 2 (AtRMR2) (ReMembR-H2 protein JR702) (Q8VZ14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the trafficking of vacuolar proteins. May function as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) (By similarity).
Subcellular location: Protein storage vacuole membrane {ECO:0000269|PubMed:10953001}. Golgi apparatus membrane {ECO:0000305|PubMed:10953001}; Single-pass type I membrane protein {ECO:0000305|PubMed:10953001}. Note=Traffics through the Golgi apparatus before reaching the vacuolar compartment.
Interaction partners:
- AT4G21215 protein
- Protein POLAR-like 1
- Vacuolar-sorting receptor 1
- Thiamine phosphate phosphatase-like protein
- non-specific serine/threonine protein kinase
- ARM repeat superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Phosphatidylglycerophosphate phosphatase 1, chloroplastic/mitochondrial
- ARM repeat superfamily protein
- Vesicle-associated protein 2-2
Sequence:
MNRALVLLLYVCTVSCLASSKVILMRNNITLSFDDIEANFAPSVKGTGEIGVVYVAEPLDACQNLMNKPEQSSNETSPFVLIVRGGCSFEEKVRKAQRAGFKAAIIYDNEDRGTLIAMAGNSGGIRIHAVFVTKETGEVLKEYAGFPDTKVWLIPSFENSAWSIMAVSFISLLAMSAVLATCFFVRRHRIRRRTSRSSRVREFHGMSRRLVKAMPSLIFSSFHEDNTTAFTCAICLEDYTVGDKLRLLPCCHKFHAACVDSWLTSWRTFCPVCKRDARTSTGEPPASESTPLLSSAASSFTSSSLHSSVRSSALLIGPSLGSLPTSISFSPAYASSSYIRQSFQSSSNRRSPPISVSRSSVDLRQQAASPSPSPSQRSYISHMASPQSLGYPTISPFNTRYMSPYRPSPSNASPAMAGSSNYPLNPLRYSESAGTFSPYASANSLPDC
Protein: RanBP21 (Q9BP41)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQHGGTEALAAELASAIDLVMNPMTQQQARLEAYMACERFKEESPMCAQVGLFLASSPQSNQQVRHFGLQLIEYTIKYRWNCITHEEKVYIKDNAIKMLNVGVGPAEDRSLLPTKDALSRIIVEMIKREWPQQWSDLLPELSQACTKGEAQTELVLLVFLRLVEDVALLQTIESNQRRKDMYQALNNNMNDIFEFFLRLVEQHVTAFRETTRLCNYTKANAHSRVVEMVLLTLSGFVEWVSIQHIMSSNGKLMHFLCILLNDKAFQCNAAECLAQITNRKGQTKERKPLLQLFNEEPLRYIYQASQIPADTSSTLAVEQHLNFLKKLLQVLNGMAQQLVALWGKDDATQRPVHLEVLLECLLLLVQHPSLGLSHGSALIWQLLLKHEPSSKDFAMVNYIPKLIHTIAPRIVKLPYPASASSPASLSTEAYIRLEHDSEEEYALYFFRCRTDFLEIFRLATLVQPLVTYGYCEQWLQQRLRNAQIEADAEVKSGNVSCSVLDPVYLEWDALVSVLDGVLSRILLVAERPSVPAGLRLLEECLKLETINPLTYSILLSCISALFVFLSMSACQITATNCVAMSGVSLLPRVLDKIFRALVMKPPNELEKVQAKSAKNLRRHAASLLVKLAHKYPLLLLPVFEQINGHVELLLKEPGKHQLCRLMRTTLQEALILISNHFCDFERQTLFIEHIVQDKRTEWLAFGDALKSPLDFMSFVGLDKPPIFAVKEAVTLQNRSRFLDALHVVLGVVKRCTWPDDPERAQRGGFVIGCTELGNPICRNPATKHIVPLLSHVLSLMRVLNELFAPEALQALSEGYRGIHGMMEHEKKLLMGICALPTDPLDTTIRSEPTAFEKMQTFMMMVTEGCYHLMGSAGPSLGRDLYQLMGLSDAIVTNVFSRMDLVPDYRLRPIIRVFFKPFVYSCPPSFYDSVLVPLFAHLAPLMCERLTRRWIYIASLYESGQLDGEVNDTQEVLEDQLNRTLTREYLDVLKIALVGGQIGADHVAAGANANSNSVAMENEEHSMDSAPQSRAIQSALLSDIISDLGGKLLRNGLIGNYVLMTLLKAIAWNDGMCSMKAVNIAAPVMRFLAAEKLMDENKAVTAFTAVLQGMQVHGQHEANQSGLVTLGVQFYELLRPQFPILSEVLQHIPSVNAADIQKFDEKIAVAPVKGNKVDRAKKDIFKKLTAQLVGRSVNQLFRHEVQIANLPPMQSHKAKGSMGTTADIMDSNQNASLARLFGPEK