wanglab/gogpt-training-data huggingface dataset:
Protein: Poly(A) binding protein cytoplasmic 4 (H0YEU6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRQAELKRKFEQLKQERISRYQGVNLYIKNLDDTIDDEKLRKEFSPFGSITSAKDGRSKGFGFVCFSSPEEATKAVTEMNGRIVGSKPLYVALAQRKEERKAHLTNQYMQRVAGMRALPANAILNQFQPAAGGYFVPAVPQAQGRPPYYTPNQLAQMRPNPRWQQGGRPQGFQGMPSAIRQSGPRPTLRHLAPTGSECPDRLAMDFGGAGAAQQGLTDSCQSGGVPTAVQNLAPRAAVAAAAPRAVAPYKYASSVRSPHPAIQPLQAPQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQTMHSNLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHHAKKEAAQKVGAVAAATS
Protein: E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2) (Q69ZI1)
Organism: Mus musculus (Mouse)
Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing its dynamin-dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000269|PubMed:14504284, ECO:0000269|PubMed:22959435}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:14504284}. Note=Colocalizes, with AKT2 in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:14504284}.
Interaction partners:
- Mitogen-activated protein kinase 9
Sequence:
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRPWKPGPGGGGGTTCTNTLRAQGSTVVNCGSKDLQSSQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVSGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAQSTSASKHPDTKKNTRKRHSFTSLTMANKSSQGSQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFTFPSDVPYQAALGSMNPPLPPPPLLAATVLASTPSGATAAVAAAAAAAAAAGMGPRPVMGSSEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVSMSTAGQASRGVTMVSPSTAGGPTQKPQGNGVAGNPSVVPTAVVSAAHIQTSPQAKVLLHMSGQMTVNQARNAVRTVAAHSQERPTAAVTPIQVQNAACLGPASVGLPHHSLASQPLPPMAGPAAHGAAVSISRTNAPMACAAGASLASPNMTSAMLETEPSGRTVTILPGLPTSPESAASACGNSSAGKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGAGEAPLQGAVGPELPLGGSHGRVGSCPTDGDGPVAAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
Protein: Cell division protein SepF (P9WGJ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01197}. Note=Localizes to the division site, in a FtsZ-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01197}.
Interaction partners:
- Cell division protein FtsZ
- Cell division protein FtsQ
- Pyridoxal phosphate homeostasis protein
- Purine nucleoside phosphorylase Rv2149c
- Probable peptidoglycan glycosyltransferase FtsW
- Cell wall synthesis protein Wag31
- Possible conserved transmembrane protein
- Peptidoglycan glycosyltransferase RodA
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramate--L-alanine ligase
Sequence:
MSTLHKVKAYFGMAPMEDYDDEYYDDRAPSRGYARPRFDDDYGRYDGRDYDDARSDSRGDLRGEPADYPPPGYRGGYADEPRFRPREFDRAEMTRPRFGSWLRNSTRGALAMDPRRMAMMFEDGHPLSKITTLRPKDYSEARTIGERFRDGSPVIMDLVSMDNADAKRLVDFAAGLAFALRGSFDKVATKVFLLSPADVDVSPEERRRIAETGFYAYQ
Protein: Aconitate hydratase 1 (Aconitase 1) (EC 4.2.1.3) (Citrate hydro-lyase 1) (Q42560)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance. May have a role in respiration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14671022}. Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Peroxisomal isocitrate dehydrogenase
- Isocitrate dehydrogenase, chloroplastic/mitochondrial
- Cytosolic isocitrate dehydrogenase
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Citrate synthase 1, peroxisomal
- Citrate synthase 2, peroxisomal
- Citrate synthase 5, mitochondrial
- Isocitrate lyase
- ATP-citrate synthase beta chain protein 1
Sequence:
MASENPFRSILKALEKPDGGEFGNYYSLPALNDPRIDKLPYSIRILLESAIRNCDEFQVKSKDVEKILDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSNAFHNMLVVPPGSGIVHQVNLEYLARVVFNTNGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLTGKLRDGMTATDLVLTVTQMLRKHGVVGKFVEFHGEGMRELSLADRATIANMSPEYGATMGFFPVDHVTLQYLRLTGRSDDTVSMIEAYLRANKMFVDYSEPESKTVYSSCLELNLEDVEPCVSGPKRPHDRVPLKEMKADWHSCLDNRVGFKGFAVPKEAQSKAVEFNFNGTTAQLRHGDVVIAAITSCTNTSNPSVMLGAALVAKKACDLGLEVKPWIKTSLAPGSGVVTKYLAKSGLQKYLNQLGFSIVGYGCTTCIGNSGDIHEAVASAIVDNDLVASAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFETQPIGTGKDGKQIFFRDIWPSNKEVAEVVQSSVLPDMFKATYEAITKGNSMWNQLSVASGTLYEWDPKSTYIHEPPYFKGMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRRDFNSYGSRRGNDEIMARGTFANIRIVNKHLKGEVGPKTVHIPTGEKLSVFDAAMKYRNEGRDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVISKSFERIHRSNLVGMGIIPLCFKAGEDAETLGLTGQELYTIELPNNVSEIKPGQDVTVVTNNGKSFTCTLRFDTEVELAYFDHGGILQYVIRNLIKQ
Protein: Low conductance mechanosensitive channel YnaI (P0AEB5)
Organism: Escherichia coli (strain K12)
Function: Mechanosensitive channel that protects cells against hypoosmotic stress when highly overexpressed.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22874652}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22874652}.
Interaction partners:
- Moderate conductance mechanosensitive channel YbiO
- Large-conductance mechanosensitive channel
Sequence:
MIAELFTNNALNLVIIFGSCAALILMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSIINYVIENYKLKFITPGVIDFICTSLIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSRIIKITIIVVLVLLYGEHFGMSLSGLLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFSIGDWIRSPDRNIEGTVAEIGWRITKITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTTIGLRYEDAAKVGVIVEAVREMLKNHPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWAEWLAAQQDVYLKIIDIVQSHGADFAFPSQTLYMDNITPPEQGR
Protein: threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (Q57W54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L17, putative
- Ribosomal protein
- GPI mannosyltransferase 1
- Ribosomal protein L11, putative
- Large ribosomal subunit protein uL3m
- 50S ribosomal protein L17, putative
- Tyrosyl/methionyl-tRNA synthetase, putative
- 40S ribosomal protein S14
Sequence:
MATAVVGKKKGGATVDLKQLQEPDFWKTRNAIFDELYAAQQEKYKSMQSPISITLNDGKQLPATSWLTTPIDIAKKLSNSLAERVVAARVNEEIWDLTRPFEGDATLELLDWDDADARHVFWHSSSHVLGYALERVFQTRLSVGPALEEGGFFYEGETNRPVTEADYTTIETAMQELVKMKVPFQRLTVKKEDALRLFQYTEFKSKILASKVPENGTCTVYRCGNLIDPCRGPHLPDTGRVKSFSLTKNSSSYFEGKAENAVLQRVYGISFPKQTMLTEWKKLQEEAARRDHRTIGRHQQLFHFHEASPGNAFWLPHGARIYNTLIEFQRKQYRRRGFEEVVSPNMFSSRLWMVSGHWDKYADNMFLINVEKEDHGMKPMNCPGHCLMFAMQPHSYRELPIRYADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCRMDQVKDEIHSALIFLKDVYDVLGFKFFLKHSTRPENKLGSDEMWDEAESYLQAALNSFCGIPDELPDPFNKGSTFVYDGRKESVKKLRAMLKKRGDKKNDENSPADDVWPGPTHEDAWEENTGDGAFYGPKIDIVVEDALRRRHQCATIQLDFNLPKRFGLKYTLPSNAAGDDGPAPKATECHKDPNAELKADKPEGKVEAAAGAPKSSYEKAAHELNIDQRLDANQARPVMIHRAIFGSLERCIAILCEHYGGDWPFWLSPRQVIVVPVSLENAAYAQTVRDTFFAAGFFADVDNGTATLEKKIRNAELARYNFILVVGQAEQEGQSVNVRTRDNRRHGTKTLDEALQWLRELADKYDPSF
Protein: D-glucuronyl C5-epimerase (EC 5.1.3.17) (Heparan sulfate C5-epimerase) (Hsepi) (Heparin/heparan sulfate:glucuronic acid C5-epimerase) (Heparosan-N-sulfate-glucuronate 5-epimerase) (O18756)
Organism: Bos taurus (Bovine)
Function: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}.
Interaction partners:
- Heparan-sulfate 6-O-sulfotransferase
- Heparan sulfate 2-O-sulfotransferase 1
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Sulfotransferase
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Heparan-sulfate 6-O-sulfotransferase
- Heparan-sulfate 6-O-sulfotransferase
- [heparan sulfate]-glucosamine N-sulfotransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
Sequence:
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQVPRHLSSGFRVDALEKKAAASESNNYVNHMAKQSEEAFPQEQQKAPPVVGGFNNNGGGRVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNSKPNDWTVPKGCFMASVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTVHYVSNTQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTRIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPIFKEFVKRWKSYLKGSRAKHN
Protein: Serine palmitoyltransferase (SPT) (EC 2.3.1.50) (A7LXM2)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Involved in de novo bacterial ceramide synthesis. Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine (By similarity). Also capable of using alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa). Contributes to the levels of endogenous sphingolipids in its host.
Interaction partners:
Sequence:
MGLLQEKLAKYDLPQKFMAQGVYPYFREIEGKQGTEVEMGGHEVLMFGSNAYTGLTGDERVIEAGIKAMHKYGSGCAGSRFLNGTLDLHVQLEKELAAFVGKDEALCFSTGFTVNSGVIPALTDRNDYIICDDRDHASIVDGRRLSFSQQLKYKHNDMADLEKQLQKCNPDSVKLIIVDGVFSMEGDLANLPEIVRLKHKYNATIMVDEAHGLGVFGKQGRGVCDHFGLTHEVDLIMGTFSKSLASIGGFIAADSSIINWLRHNARTYIFSASNTPAATASALEALHIIQDEPERLEALWEATNYALKRFREAGFEIGATESPIIPLYVRDTEKTFMVTKLAFDEGVFINPVIPPACAPQDTLVRVALMATHTKDQIDRAVEKLVKAFKALDLL
Protein: V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) (Q16864)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit G 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit H
Sequence:
MAGRGKLIAVIGDEDTVTGFLLGGIGELNKNRHPNFLVVEKDTTINEIEDTFRQFLNRDDIGIILINQYIAEMVRHALDAHQQSIPAVLEIPSKEHPYDAAKDSILRRARGMFTAEDLR
Protein: Serine/threonine-protein kinase Nek7 (EC 2.7.11.34) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7) (Q9ES74)
Organism: Mus musculus (Mouse)
Function: Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity). Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity. Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1. Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:26188091}. Cytoplasm {ECO:0000269|PubMed:26188091}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TDX7}. Note=Present at centrosome throughout the cell cycle (By similarity). Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (By similarity). Interaction with ANKS3 prevents its translocation to the nucleus (PubMed:26188091). {ECO:0000250|UniProtKB:Q8TDX7, ECO:0000269|PubMed:26188091}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 3
- Serine/threonine-protein kinase Nek9
- Caspase-1
- Ankyrin repeat and SAM domain-containing protein 3
- Gasdermin-D
- Ankyrin repeat and SAM domain-containing protein 6
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MDEQSQGMQGPPVTQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRASCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALDHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNICINPDPEKRPDIAYVYDVAKRMHACTAST
Protein: SET domain-containing protein (O45995)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein atz-1
- DUF1624 domain-containing protein
- CABIT domain-containing protein
- Cilia- and flagella-associated protein 157
- F-box domain-containing protein
- F-box C protein
- F-box domain-containing protein
- Major sperm protein 63
Sequence:
MQPSTVPTETLQSRMSGFNERLKKATNVTEQVAVMEDMKKDSEVYDSWSKHRQAQLKYAYTSFPTKFREMMGGSSIREEETEEIDTQNSSETEEPSIADAIASRQEFLNKLVETTDQLIDITVDKFISQLKNCHIRKPETPSEPSREASPAPRLSSPFERIIDETTELLAKCASSGPPDHSLRSSILETLFSEIKGKSSDVSLVTISEESEKSEESEESKEDKGSQSLNTSSISTEPSPVQTSILKPPPMYPETASFPHRKIRSGAYSLYPPPQPSQQFVHSHNFHQPKFDASSMLSTGYCPSRNVATFKVDKPYGTVFTYDHQNRKFQEHCCVECREQIEENDLYPLYAVWCEKISNHVIFMEIGFTEEIGQFVFSFKTGGFEQVDFPELVFSEHVEYNGSFVAMIAGEGEDKVIIERDESGEKVRKLLHKFGHSVQIPYAPVRPLWMQKAEEPVEEDVEPESDAEPEETLDAEHVSYITSLPTYKKEYCQTYEMDVLYMLQPNGQYLKYSLNDDENELNLHVCDCCKTGTTENDLIPKYSEYCAKTCKYIIHVQNQFTEKMETYAYDCEKKRFHQVTCPGLVYDSEKVQEGNIFFILEQNSMQGVEVIMRDDDGQLRKEQFCMVKKQFVKLPKTTVATFAVQIAEKKMKNLLPNVEIFLPWPQRFTPSLSQCSSVQAMVIPETNHQLISSPQPTPSEID
Protein: Succinate dehydrogenase hydrophobic membrane anchor subunit (P0AC44)
Organism: Escherichia coli (strain K12)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- Fumarate reductase iron-sulfur subunit
- Fumarate reductase flavoprotein subunit
- 2-oxoglutarate dehydrogenase E1 component
- Fumarate hydratase class I, aerobic
- Fumarate reductase subunit D
Sequence:
MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFFASAFTKVFTLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV
Protein: Aquaporin-5 (A0A1D5P9U9)
Organism: Gallus gallus (Chicken)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004439}.
Interaction partners:
- Aquaporin 11
- Aquaporin
- BRICHOS domain-containing protein.
- Aquaporin 3
- Uncharacterized protein
- Aquaporin 9
Sequence:
MKREILTLAFARAVFVEFISTLIFVFIGLGSALKWPSALPSILQISLAFGLAIGTLVQAFGHISGAHINPAVTIAFFVGNQISFLRTLFYVIAQLVGAIAGAGILYGVTPANTRGNLAINSLNNNTTPGQAVVVEMILTFQLAACIFASTDNRRNGNVGSPALSIGLSVAVGHLVGIYFTGCSMNPARSFGPAVIVRKFSSTHWVFWVGPILGACLAALLYFYILVPYCMNMSDRVAIVKGTYESEEEWEEQREERKKSMELTPP
Protein: Lethal giant larvae 1 (Lethal(2) giant larvae protein homolog 1) (I0BWE2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MMKFRFRRQGNDPHREKIKQDLFAFNKTVEHGFPNQPSALAYDPKLQLMAIGTKSGAIKIYGAPGVEMTGLHKDTAAVTQIHFLCGQGRILSLLDDNTIHLWEIVQRENRSHLLEVHSFNLPGRPGIESTSATRVTVMLLNLSCNLLALGTEGGGVHFLELPTLTLLNKSLFQDEIMQSVPEEYKCGKSLGPVESLQEHPKDSDKILIGYSRGLVVLWDLSSRHVDNLFLGKQQLESLVWERSGNSFVSSHSDGGYMVWAVSSSNPCTHDPVSSTIPYGPFPCKAVNKILWRTTESGAPLVLFSGGMPRASYGDRHCLTILQDSSHVTLDFTSRVIDFFTIHCTDTEKDFDEPSALVVLLEEELVVIDLQMPGWPTVPAPYLAPLHSSAITCSCHISNVPPKLWERVISAGQQQCPLQNYENWPICGGKNLAPDPKQKELLLTGHEDGTVRFWEASGVSLKPLYKLSTASIFQTDCEHNDSLTQAGEEEWPPFRKVGCFDPYSDDPRLGIQKISLCKYSGKLVVAGTAGQVIVMVLGDEKSDHMIDVATVDLLQDREGFTWKGHDRLPPKSGSVVFAPGFQPVVLVQCLPPAAVTAVTLHAEWNLIAFGTSHGFGLFDYHRRSPVLARCTLHPNDSLAMEGPLSRVKSLKKSLRQSFRRIRKSRVSGKKRVVVNSPTSKVQEANAHLADHDAEVTPVQRRIEPRSADDSLSGVVRCLCFADTFLRDGTHHGPTMWAGTNSGSVYAYAPDVPSQEKFSEQSVEALLGKEIQLMHRAPVVSIAVLDGRGNPLPEPYEVSRDLAKAPDMQGSHSVLIASEEQFKVFMLPKVSAKTKFKLTAHEGCRVRKVALANFTSVSSEDYSENALVCLTNMGDIHMFSVPALRPQVRYDCVRKEDISGIASCVFTKTGQGFYLISPSEYERFSLSARVITEPLCGVDIERPHDVSAHSSSTTLPPQANGTHKSQAESKSAETEDLLEEMRSVLSSPILDSPNSSADITLDTTGDLTVEDVKDFLMTVDEAENNFRNITEEDGRSAGILIN
Protein: SIGLEC-H (Q3Y597)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLLSLLLPLLWVLKWASGNCFILPREVIGTYPSLTLELQSVTVQEGLCVLVPCHLIEYPMNRWSDAAFGYWFHEGENTHPDSLVATNKPYQLVQKEMQSRFHFSGDCSLDIRDAQKGDNGSYFFRLEKGGKTWNFCEERISVHVTDLTHSPNISIPQTLELGRPTNVMCSVPWACERGTPPIFSWMSAALISLGPTTTLSSVLTLTPRLQDHGTNLTCQVTFPGAGVTVQKTIQLNVTYNSQNSTAHVSGRVGPGKPRPLADVVQVAMGEAAIKFLLLGICFFFLSKRSHTKRVERPATHMDQAHAVMD
Protein: Chorion-specific transcription factor GCMa (hGCMa) (GCM motif protein 1) (Glial cells missing homolog 1) (Q9NP62)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes. Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer. Binds to the SYDE1 promoter. Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00245}.
Interaction partners:
- Chorion-specific transcription factor GCMb
- Serine protease HTRA4
- F-box/WD repeat-containing protein 2
Sequence:
MEPDDFDSEDKEILSWDINDVKLPQNVKKTDWFQEWPDSYAKHIYSSEDKNAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCGRDCLAEEGRKIYLRPAICDKARQKQQRKRCPNCDGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPKPETKLEAEARRAMKKVNTAPSSVSLSLKGSTETRSLPGETQSQGSLPLTWSFQEGVQLPGSYSGHLIANTPQQNSLNDCFSFSKSYGLGGITDLTDQTSTVDPMKLYEKRKLSSSRTYSSGDLLPPSASGVYSDHGDLQAWSKNAALGRNHLADNCYSNYPFPLTSWPCSFSPSQNSSEPFYQQLPLEPPAAKTGCPPLWPNPAGNLYEEKVHVDFNSYVQSPAYHSPQEDPFLFTYASHPHQQYSLPSKSSKWDFEEEMTYLGLDHCNNDMLLNLCPLR
Protein: Serine/arginine-rich splicing factor RS31A (At-RS31A) (At-RSp31A) (AtRS31A) (Arginine/serine-rich splicing factor RS32) (At-RSp32) (Q9ZPX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in intron recognition and spliceosome assembly.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:P92964}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P92964}.
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Serine/arginine-rich splicing factor RSZ22A
- Serine/arginine-rich splicing factor RSZ21
- Nuclear cap-binding protein subunit 2
- Splicing factor U2af large subunit A
- Serine/arginine-rich SC35-like splicing factor SCL30A
- Nuclear protein-like
- Nuclear cap-binding protein subunit 1
- Serine/arginine-rich SC35-like splicing factor SCL33
- Serine/arginine-rich splicing factor SR45
Sequence:
MRHVYVGNFDYDTRHSDLERLFSKFGRVKRVDMKSGYAFVYFEDERDAEDAIRRTDNTTFGYGRRKLSVEWAKDFQGERGKPRDGKAVSNQRPTKTLFVINFDPIRTRERDMERHFEPYGKVLNVRMRRNFAFVQFATQEDATKALDSTHNSKLLDKVVSVEYALREAGEREDRYAGSRRRRSPSPVYRRRPSPDYTRRRSPEYDRYKGPAPYERRKSPDYGRRSSDYGRARARSPGYDRSRSPIQRARG
Protein: GldK (A5FIS8)
Organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
Interaction partners:
- GldL
- GldM
- GldN
- SprA
- SprT
- SprE
- GldD
- GldB
- Gliding motility lipoprotein GldH
- GldO
Sequence:
MKKFIAFAAMLTLVIGCGKSGDKGELVGVTGGKWHPEKPYGMTLVPGGSFIMGKSDGDLANVEDAPTRTVTVRSFYMDETEITNSEYRQFVEWVKDSTMRVRLAILADETGQKSTGDKGKKGGSIADYAFNDSEPDKMTAYDKYMYDNYYSVGTKDDPYAGRKLNKKVKLIRDTKAYPDEYYAEVMDSMYLPIEESYNGLRTIDVNKLKFRYSWMDIQAAAKAKVGKRKDFVKTEQVNVYPDTTVWIKDFAYSYNEPMHNDYFWHKAYGDYPVVGVTWKQAKAFCAWRTLNKNSYIKSKKKGRDLVNAFRLPTEAEWEYAARGGLESATYPWGGPYTKSDRGCFMANFKPNRGDYAADEALYTVEAKSYEQNGYGLYNMAGNVSEWTDSAYNPNAYEYVSTMNPNVIDGNNQRKVVRGGSWKDVAYFLQVSTRDHEYADSARSYIGFRTVQDYMGTQVTGGGRK
Protein: Olfactory receptor 6E1 (Olfactory receptor 118-1) (Olfactory receptor 49) (Olfactory receptor I-C6) (Q9Z1V0)
Organism: Mus musculus (Mouse)
Function: Odorant receptor. Activated by (-)-citronellal and to a lesser extent by (+)-citronellal. Not activated by carvone or limonene.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MANSTTVTEFILLGLSDACELQVLIFLGFLLTYFLILLGNFLIIFITLVDRRLYTPMYYFLRNFAMLEIWFTSVIFPKMLTNIITGHKTISLLGCFLQAFLYFFLGTTEFFLLAVMSFDRYVAICNPLRYATIMSKRVCVQLVFCSWMSGLLLIIVPSSIVFQQPFCGPNIINHFFCDNFPLMELICADTSLVEFLGFVIANFSLLGTLAVTATCYGHILYTILHIPSAKERKKAFSTCSSHIIVVSLFYGSCIFMYVRSGKNGQGEDHNKVVALLNTVVTPTLNPFIYTLRNKQVKQVFREHVSKFQKFSQT
Protein: Sporulation-specific protease YabG (EC 3.4.-.-) (P37548)
Organism: Bacillus subtilis (strain 168)
Function: Cleaves the spore coat proteins SpoIVA and SafA. May cooperate with tgl to mediate the temperature-dependent cross-linking of coat proteins like GerQ.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:10714992}. Note=Synthesized in the mother cell compartment and assembled on the surface of the forespore.
Interaction partners:
- Uncharacterized protein YlbD
- Stage IV sporulation protein A
- Probable sporulation protein YtaF
- Protein YxeE
Sequence:
MQFQIGDMVARKSYQMDVLFRIIGIEQTSKGNSIAILHGDEVRLIADSDFSDLVAVKKDEQMMRKKKDESRMNESLELLRQDYKLLREKQEYYATSQYQHQEHYFHMPGKVLHLDGDEAYLKKCLNVYKKIGVPVYGIHCHEKKMSASIEVLLDKYRPDILVITGHDAYSKQKGGIDDLNAYRHSKHFVETVQTARKKIPHLDQLVIFAGACQSHFESLIRAGANFASSPSRVNIHALDPVYIVAKISFTPFMERINVWEVLRNTLTREKGLGGIETRGVLRIGMPYKSN