wanglab/gogpt-training-data huggingface dataset:
Protein: ER degradation-enhancing alpha-mannosidase-like protein 1 (Q925U4)
Organism: Mus musculus (Mouse)
Function: Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- DnaJ homolog subfamily C member 10
- ER degradation-enhancing alpha-mannosidase-like protein 3
- Calnexin
- Protein sel-1 homolog 1
- ER degradation-enhancing alpha-mannosidase-like protein 2
- Alpha-mannosidase 2C1
- Protein OS-9
- Endoplasmic reticulum chaperone BiP
- Derlin-1
- Derlin-2
Sequence:
MQWRALVLGLVLLRLGLHAVLWLVFGLGPSMGFYQRFPLSFGFQRLRDPDGSGPVGPPGGPAWLHRPRRGTEGRLETPPEPGPTPGPGVCGPAHWGYALGGGGCGPDEYERRYSGAFPPQLRAQMRDLARGMFVFGYDNYMAHAFPQDELNPIYCRGRGPDRGDPSNLNINDVLGNYSLTLVDALDTLAIMGNSSEFQKAVKLVINTVSFDKDSTVQVFEATIRVLGSLLSAHRIITDSKQPFGDMTIEDYDNELLYMAHDLAVRLLPAFENTKTGIPYPRVNLKTGVPPDSNNETCTAGAGSLLVEFGILSRLLGDSTFEWVARRAVKALWNLRSNDTGLLGNVVNIQTGHWVGKQSGLGAGLDSFYEYLLKSYILFGEKEDLEMFNAAYQSIQSYLRRGREACNEGEGDPPLYVNVNMFSGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDVLFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKVKCGYATLHHVIDKSKEDRMESFFLSETCKYLYLLFDEENPVHKSGTRYMFTTEGHIISVDKRLRELPWKEFFSEDGERDQEEKFVHRPKSQELRVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGLI
Protein: Hydrolase, alpha/beta fold family, putative (Q582C8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acyl carrier protein
Sequence:
MSQADNAELKSKDARTFAVNFAEVGICPKSGVPIRLCYQTFGEPAAPNGAVLLIMGLALSQQLWDVKFCMRLASCGYYVIRFDNRDIGKSTILVGRKVLPSGTTESSDEGDIWEDSNFLSHSPPEGGADGSKSCMYIQLAHAGIAANGHRKFQEVYSLEDMAKDSVGLLDVLKISRAHIVGMCMGGMIAQIIAIQYPNRVESLSLISTHSSSPLLSSPSLRVMIGVATFAIRCVRKGVAIPLSDSMAEKQGRKPLTSREKDDLAQVLAQFVTSFAGGKESAFPIDHKALLRQTRRIVHWSEDFSGFARQYVAMIKAPCRVSQLRGLSVPCVVIHGTDDLLVPYRNGKKLADVIPGSKLVGIEGLGHILHPLSRERIIGALVENMGQSTNALSRSGAVAAKL
Protein: Interleukin-25 (IL-25) (Interleukin-17E) (IL-17E) (Q8VHH8)
Organism: Mus musculus (Mouse)
Function: Cytokine produced by various cells such as eosinophils, T-helper type 2 (Th2) cells or epithelial cells that plays a role in internal safety of adaptive immune responses by regulating cytokine production. Promotes and augments T-helper type 2 responses locally or systemically. Exerts its activity via its receptor composed of IL17RA and IL17RB for signal transduction. In turn, stimulates the JAK2-STAT5A pathway and promotes the secretion of type-2 associated cytokines including IL4, IL9 and IL13. Induces also the release of IL8, and IL6 from eosinophils through the combined activation of MAPK and NF-kappa-B pathways. Inhibits the differentiation of T-helper (Th17) cells via the production of IL4, IL5 and IL13.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9H293}.
Interaction partners:
- Interleukin-17 receptor B
- Interleukin-17 receptor A
- Interleukin-17B
- Interleukin-17 receptor E
- Interleukin 17D
- Interleukin-17F
- Interleukin-17 receptor C
- Interleukin-17 receptor D
- Interleukin-22
- Interleukin-17A
Sequence:
MYQAVAFLAMIVGTHTVSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVSPPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRDLNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPLYHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACVCVRPRVMA
Protein: Acetyl-Coenzyme A acyltransferase 1 (Peroxisomal 3-oxoacyl-Coenzyme A thiolase), isoform CRA_a (Epididymis secretory sperm binding protein) (A0A024R2M6)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Frizzled-4 (Transmembrane receptor) (G5EF44)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGPFRGYLGVTWLLLLFVIGVDGQRCQKVDHEMCNDLPYNLTSFPNLVDEESWKDASESILTYKPLLSVVCSEQLKFFLCSVYFPMCNEKLANPIGPCRPLCLSVQEKCLPVLESFGFKWPDVIRCDKFPLENNREKMCMKGPNEQGAIQDERAKFAAKESEDDGNDRVEDIQREVDRLNGKCPQDEVFLNRSSKCVPLCSNPQKVGQTDRESATRLLLFLSLSSVILTILSVFIVGLSRLEMLHSLTETAMFFSCISFCATSVIYIVSISFKDQFQISCTDYTHHLLFVVGGLSHVPCSSVASLIYYTATCSRLWWLLICVSWNKATRTSHILDDSRTRVIMLILGIPLAPLMLALLAKAVAANPLTGLCFIGAASPGTDWIFNFCRELILFLISSIALSSACCRLLGSDEQDVNGFAGVIAAVYPIAGLFYMLSFVNDATQPFLSLDRSFNAVSATKFSFDLLLSFIMCAFCLIYLLFKLTRSSSKVSKEGYQPAVPKLPQPAIPGSVRSNTYASTFRTNNMI
Protein: PTTG1 interacting protein (A8MZH8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAPGVARGPTPYWRLRLGGAALLLLLIPVAAAQEPPGAACSQNTNKTCEECLKNVSCLWCNTNKACLDYPVTSVLPPASLCKLSSARWGVCWGLFKEENPYARFENN
Protein: Cilia- and flagella-associated protein 53 (Coiled-coil domain-containing protein 11) (A0A0R4IFG5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). May play a role in the beating of primary cilia and thereby be involved in the establishment of organ laterality during embryogenesis.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25504577}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25504577}. Note=In cilia of the pronephric kidney tubules, prominent localization along the axonemes and also detected at the ciliary base (PubMed:25504577). In cilia of Kuppfer's vesicle and the spinal canal, localizes exclusively to the ciliary base where it overlaps with the ciliary basal bodies (PubMed:25504577). {ECO:0000269|PubMed:25504577}.
Interaction partners:
- Cilia and flagella-associated protein 52.
- Coiled-coil domain-containing 114.
- Si:zfos-223e1.2.
- Tektin
- Dynein regulatory complex protein 10
- Coiled-coil domain containing 151
- Armadillo repeat containing 4
- IQ motif and ubiquitin domain-containing
- Matrix metallopeptidase-21
- EF-hand domain-containing family member C2
Sequence:
MLTAQRSRIRCREITGPAHSVALKARPPLSRDIDDIFVRRRKQEATRGEVLEFTKDQSSCDVRMRWERNTQRRVVSATVNRHLQDALDQYQMGIDEKRERLRELLESEELELFKEMEAKKETVLERQAKMHERAKTLRERRESERQRVVADKLDQLFREQSEELRAVQIKRRQDQVCTERESQIRTKEEVRRVQEEEEKLFAQMWESDRLAKEERHNLELQRQRENNLQQKAVLQTQMDMAEQQRIQAKELKQEEAQLLKDQREMLRLEAEREHRQKLQDQEKRRKQLDLSLRLKMKRLTRDRQEELALDMSILEQLLAQEKDEKQDEVLKKLERQEEQRRYREYLSQQLEEQKRLEAETEQLFESELQQAWARREAQWRLEKTARDRLMKDVMDTLRLQIQEKLNENMQKQAEAFKEKEELDRIIQANKLLDEEEKAHFREATKEYQADLLAQMMYRQRIREAEEAEKEYEFQKGLMYEEQYNKKIQDILSRPISSTTAVHPFRRRDRRCSSSGGQMS
Protein: Zinc finger, MYND domain containing 11 (Q08CT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRVVKKRQADPKVVQYVWSAIEVIRNQKQIANMDRISKYLSRVYGMHPKDTARQLVLAVKDGLVVETLTVGCKGSKAGIEQEGYWLPGDEMEQMSEGSKPSLPSEALFPDDWGAESHDWYCFECHLPGDVMECDGCFRVYHLRCVSEDHRPRDTTSHWQCGICRGSKRKNLNKQEMTTYLKFILGRMKERAVDLHKRGKEAKQPIYKRLIHTPLDVENIQENISDGKYKSFEEFRADAQLIVHNTAILHGVNSDQTEIARLLYNDTCHELNELMLCRTCFYLSNARPDNWFCYPCSPNHELVWARMKGFGYWPAKVMQREGNQVDVRFFGHQHQRAWIPSDNIQDITVSVQQLQVKRSSGWKKACDELELHQRFVREGRTWKGKPEEKNDRSERHERQEERQEEAESSISSTSNEQSRVNQEPKAKKSRRSQVAEPKEEEPEPEMEAVSSSQEIPTAVPHQPERMSVSTQTKKSSSPSSSSSPAPRMIHKGTQTVNEGNCQNMCHDKYSKIFSDVKEMMKAENKRETERVLKEALDKLRGEMEEEKRQAVNKAVSSTQAEMERKCKQVKEKCKEELMEEMKKMVSQHKQLLSQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHADHKRTCRRKR
Protein: Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial (COX) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (P36552)
Organism: Mus musculus (Mouse)
Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:8407975}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- Ferrochelatase, mitochondrial
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- 5-aminolevulinate synthase, non-specific, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Heme oxygenase 2
- Mitoferrin-1
Sequence:
MALRLGRLGSDPWWRAVLGDYAQLRAASPRCASARVCQLPGTAGPQPRRGLGYGPWARGGSGLGTRLAATLAGLAGLAAAAFGHVQRAEMVPKSSGARSPSPGRREEDGDELARRCSTFMSSPVTELRELRRRPEDMKTKMELMIMETQAQVCRALAQVDGVADFTVDRWERKEGGGGITCVLQDGRVFEKAGVSISVVHGNLSEEAANQMRGRGKTLKTKDSKLPFTAMGVSSVIHPKNPYAPTMHFNYRYFEVEEADGNTHWWFGGGCDLTPTYLNQEDAVHFHRTLKEACDQHGPDIYPKFKKWCDDYFFIVHRGERRGIGGIFFDDLDSPSKEEAFRFVKTCAEAVVPSYVPIVKKHCDDSYTPRDKLWQQLRRGRYVEFNLLYDRGTKFGLFTPGSRIESILMSLPLTARWEYMHSPPENSKEAEILEVLRHPKDWVH
Protein: VIP peptides [Cleaved into: Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P01284)
Organism: Sus scrofa (Pig)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
- Vasoactive intestinal polypeptide receptor 1
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Vasopressin V1a receptor
- Vasoactive intestinal peptide receptor 2
- Glucagon-like peptide 1 receptor
- Guanylate cyclase
- 5-hydroxytryptamine receptor 6
- Somatostatin
- Pro-neuropeptide Y
- Adenosine receptor A2
Sequence:
HADGVFTSDFSRLLGQLSAKKYLESLIXXXXXXXXXXXXXXXXXHSDAVFTDNYTRLRKQMAVKKYLNSILNGKR
Protein: Epididymis secretory protein Li 84 (V9HW95)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKERVVRPDSELGERPPEDNQSFQYDHEAFLGKEDSKTFDQLTPDESKERLGKIVDRIDNDGDGFVTTEELKTWIKRVQKRYIFDNVAKVWKDYDRDKDDKISWEEYKQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKAADLNGDLTATREEFTAFLHPEEFEHMKEIVVLETLEDIDKNGDGFVDQDEYIADMFSHEENGPEPDWVLSEREQFNEFRDLNKDGKLDKDEIRHWILPQDYDHAQAEARHLVYESDKNKDEKLTKEEILENWNMFVGSQATNYGEDLTKNHDEL
Protein: Acyl-CoA synthetase X3 (EC 6.2.1.3) (GH20840p) (Q9VDU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MPYRPASYYDADRKIWSGDQLEYYFDPHLSIGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDVKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVTITNSRQILNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDAKYKQLNGGAIIVEDLVRSPNGKTNRMANKAFFLEAKSSAK
Protein: Calcium-activated chloride channel regulator 1 (EC 3.4.-.-) (Calcium-activated chloride channel family member 3) (mCLCA3) (Protein gob-5) (Q9D7Z6)
Organism: Mus musculus (Mouse)
Function: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12019299, ECO:0000269|PubMed:15919655, ECO:0000269|PubMed:16895902}. Note=The 75 kDa N-terminal and a 35 kDa C-terminal products are fully secreted into extracellular environment as a soluble complex of two glycoproteins.
Interaction partners:
- Mucin-2
- Mucin-2
- Anterior gradient protein 2 homolog
- Mucin-2
- Zymogen granule membrane protein 16
Sequence:
MESLKSPVFLLILHLLEGVLSESLIQLNNNGYEGIVIAIDHDVPEDEALIQHIKDMVTQASPYLFEATGKRFYFKNVAILIPESWKAKPEYTRPKLETFKNADVLVSTTSPLGNDEPYTEHIGACGEKGIRIHLTPDFLAGKKLTQYGPQDRTFVHEWAHFRWGVFNEYNNDEKFYLSKGKPQAVRCSAAITGKNQVRRCQGGSCITNGKCVIDRVTGLYKDNCVFVPDPHQNEKASIMFNQNINSVVEFCTEKNHNQEAPNDQNQRCNLRSTWEVIQESEDFKQTTPMTAQPPAPTFSLLQIGQRIVCLVLDKSGSMLNDDRLNRMNQASRLFLLQTVEQGSWVGMVTFDSAAYVQSELKQLNSGADRDLLIKHLPTVSAGGTSICSGLRTAFTVIKKKYPTDGSEIVLLTDGEDNTISSCFDLVKQSGAIIHTVALGPAAAKELEQLSKMTGGLQTYSSDQVQNNGLVDAFAALSSGNAAIAQHSIQLESRGVNLQNNQWMNGSVIVDSSVGKDTLFLITWTTHPPTIFIWDPSGVEQNGFILDTTTKVAYLQVPGTAKVGFWKYSIQASSQTLTLTVTSRAASATLPPITVTPVVNKNTGKFPSPVTVYASIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKNDGVYSRFFTAFDANGRYSVKIWALGGVTSDRQRAAPPKNRAMYIDGWIEDGEVRMNPPRPETSYVQDKQLCFSRTSSGGSFVATNVPAAAPIPDLFPPCQITDLKASIQGQNLVNLTWTAPGDDYDHGRASNYIIRMSTSIVDLRDHFNTSLQVNTTGLIPKEASSEEIFEFELGGNTFGNGTDIFIAIQAVDKSNLKSEISNIARVSVFIPAQEPPIPEDSTPPCPDISINSTIPGIHVLKIMWKWLGEMQVTLGLH
Protein: Tubulinyl-Tyr carboxypeptidase 2 (EC 3.4.17.17) (Vasohibin-2) (Vasohibin-like protein) (Q8C5G2)
Organism: Mus musculus (Mouse)
Function: Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Acts as an activator of angiogenesis: expressed in infiltrating mononuclear cells in the sprouting front to promote angiogenesis. Plays a role in axon formation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86V25}. Secreted {ECO:0000250|UniProtKB:Q86V25}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q86V25}. Note=Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. Associates with microtubules (By similarity). {ECO:0000250|UniProtKB:Q86V25}.
Interaction partners:
- Small vasohibin-binding protein
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
Sequence:
MTGSAADTHRCPHPKITKGTRSRSSHARPVSLATSGGSEEEDKDGGVLFHVNKSGFPIDSHTWERMWLHVAKVHPRGGEMVGAIRNAAFLAKPSIPQVPNYRLSMTIPDWLQAIQNYMKTLQYNHTGTQFFEIRKMRPLSGLMETAKEMTRESLPIKCLEAVILGIYLTNGQPSIERFPISFKTYFSGNYFHHVVLGIYCNGYYGSLGMSRRAELMDKPLTFRTLSDLVFDFEDSYKKYLHTVKKVKIGLYVPHEPHSFQPIEWKQLVLNVSKMLRADIRKELEKYARDMRMKILKPASAHSPTQVRSRGKSLSPRRRQASPPRRLGRRDKSPALTEKKVADLGTLNEVGYQIRI
Protein: Transcription factor egl-46 (Egg-laying defective protein 46) (G5EFY4)
Organism: Caenorhabditis elegans
Function: Transcription factor. Represses expression of genes involved in differentiation of touch receptor neurons (TRN), probably acting as a heterodimer with egl-44, perhaps by occupying similar cis-regulatory elements as an unc-86/mec-3 heterodimer. Plays a role in cell fate specification of neurons, including the hook neuron HOB, the gas-sensing neuron BAG and touch receptor neurons. Plays a role in neuron differentiation by repressing the expression of zag-1 in FLP neurons, probably acting as a heterodimer with egl-44; because zag-1 represses expression of egl-46 and egl-44, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates. Acts downstream of egl-44 to prevent touch cell differentiation in FLP neurons. Involved in male mating behavior, acting in concert with egl-44, via modulation of expression of polycystins lov-1 and pkd-2, homeodomain protein ceh-26, and neuropeptide-like protein nlp-8. Modulates the expression of a subset of terminal differentiation genes involved in O(2)- and CO(2)-sensing, acting in parallel to ets-5 and egl-13. May act upstream of RFX transcription factor daf-19 to regulate gene expression specifically in the HOB neuron. Plays a role in specifying commissural dendrites of the PVD nociceptive neurons, acting in concert with egl-44. In association with egl-44, regulates cell cycle exit in the neuronal Q cell lineage.
Subcellular location: Nucleus {ECO:0000269|PubMed:11274062, ECO:0000269|PubMed:23946438}. Note=Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts. {ECO:0000269|PubMed:23946438}.
Interaction partners:
- Transcription enhancer factor-like protein egl-44
- Transcription factor unc-86
- Spalt-like protein sem-4
- Uncharacterized protein
Sequence:
MVPMNDFWVKAILSSTNPSPVPSTTSTVSNDENLDKTLDFDCSTQTVFPTLPMFWNPTLVQQMLALYQIQQQQIQFSAKLAPQPLFQEPTIQKEFLPFPHQSRKRPLPIDPKKTKLRKLNEDTVTSSPVSGMFIKEEADVKSVEELQKEADLLDETAAYVEVTEESRQKIDEIPNVIGDCICRLCKVKYEDVFKLAQHKCPRIAHEEYKCPDCDKVFSCPANLASHRRWHKPRNELGGSPPAQSSTIVSCSTCFNSFPTKKMLKLHSSTCQRSPLQDLLSRVIPTM
Protein: Epidermal growth factor receptor kinase substrate 8-like protein 2 (EPS8-like protein 2) (Epidermal growth factor receptor pathway substrate 8-related protein 2) (EPS8-related protein 2) (Q9H6S3)
Organism: Homo sapiens (Human)
Function: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. In the cochlea, is required for stereocilia maintenance in adult hair cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14565974}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q99K30}. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells. {ECO:0000250|UniProtKB:Q99K30}.
Interaction partners:
- Unconventional myosin-XV
- Twinfilin-2
- Espin
- Whirlin
- Myosin-IIIa
- Espin-like protein
- Epidermal growth factor receptor kinase substrate 8
- Myosin-IIIb
- Peripheral plasma membrane protein CASK
- Gelsolin
Sequence:
MSQSGAVSCCPGATNGSLGRSDGVAKMSPKDLFEQRKKYSNSNVIMHETSQYHVQHLATFIMDKSEAITSVDDAIRKLVQLSSKEKIWTQEMLLQVNDQSLRLLDIESQEELEDFPLPTVQRSQTVLNQLRYPSVLLLVCQDSEQSKPDVHFFHCDEVEAELVHEDIESALADCRLGKKMRPQTLKGHQEKIRQRQSILPPPQGPAPIPFQHRGGDSPEAKNRVGPQVPLSEPGFRRRESQEEPRAVLAQKIEKETQILNCALDDIEWFVARLQKAAEAFKQLNQRKKGKKKGKKAPAEGVLTLRARPPSEGEFIDCFQKIKLAINLLAKLQKHIQNPSAAELVHFLFGPLDLIVNTCSGPDIARSVSCPLLSRDAVDFLRGHLVPKEMSLWESLGESWMRPRSEWPREPQVPLYVPKFHSGWEPPVDVLQEAPWEVEGLASAPIEEVSPVSRQSIRNSQKHSPTSEPTPPGDALPPVSSPHTHRGYQPTPAMAKYVKILYDFTARNANELSVLKDEVLEVLEDGRQWWKLRSRSGQAGYVPCNILGEARPEDAGAPFEQAGQKYWGPASPTHKLPPSFPGNKDELMQHMDEVNDELIRKISNIRAQPQRHFRVERSQPVSQPLTYESGPDEVRAWLEAKAFSPRIVENLGILTGPQLFSLNKEELKKVCGEEGVRVYSQLTMQKAFLEKQQSGSELEELMNKFHSMNQRRGEDS
Protein: ARPIN-AP3S2 readthrough (H0YMK0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSSYNSLAKLEAGTVTKCNFTGDGKTGASWTDNIMAQKCSKGAAAEIREQGDGAEDEEWPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLE
Protein: Signal peptide peptidase-like 1 (AtSPPL1) (EC 3.4.23.-) (Q93Z32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18067581}; Multi-pass membrane protein {ECO:0000269|PubMed:18067581}.
Interaction partners:
- Signal peptidase complex subunit 1
- Solanesyl diphosphate synthase 2, chloroplastic
- Proline-tRNA ligase
Sequence:
METLWTLLYLLEPAPATLIVTAVTVTFASAFRALNYGKEMERNRDFSEASITLDSSQALMIPVMSSCSLLLMFYLFSSVSQLLTAFTAIASVSSLFYWLSPYAVYMKTQLGLSDPFLSRCCSKSFTRIQGLLLVACAMTVVAWLISGHWVLNNLLGISICIAFVSHVRLPNIKICAMLLVCLFVYDIFWVFFSERFFGANVMVAVATQQASNPVHTVANSLNLPGLQLITKKLELPVKIVFPRNLLGGVVPGVSASDFMMLGLGDMAIPAMLLALVLCFDHRKTRDVVNIFDLKSSKGHKYIWYALPGYAIGLVAALAAGVLTHSPQPALLYLVPSTLGPVIFMSWRRKDLAELWEGPALSNPIEKSHEIEI
Protein: Roundabout guidance receptor 2 (A0A0G2JZA1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Slit homolog 1 protein
- Slit homolog 2 protein
- Slit homolog 3 protein
- SLIT-ROBO Rho GTPase-activating protein 2
- SLIT-ROBO Rho GTPase-activating protein 1
- SLIT-ROBO Rho GTPase-activating protein 3
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase PAK 5
- Cytoplasmic protein
- Tyrosine-protein kinase
Sequence:
MTPLMFTLLLLFGFLCIRTDGSRLRQEDFPPRIVEHPSDVIVSKGEPTTLNCKAEGRPTPTIEWYKDGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRRSKPDEGTYVCVARNYLGEAVSRNASLEVALLRDDFRQNPTDVVVAAGEPAILECQPPRGHPEPTIYWKKDKVRIDEKEERISIRGGKLMISNTRKSDAGMYTCVGTNMVGERDSDPAELTVFERPTFLRRPINQVVLEDEPAEFRCQVQGDPQPTVRWKKDDADLPRGRYDIKDDYTLRIKKAISADEGTYVCIAENRVGKVEASATLTVRVRPVAPPQFVVRPRDQIVAQGRTVTFPCETKGNPQPAVFWQKEGSQNLLFPNQPQQPNSRCSVSPTGDLTITNIQRSDAGYYICQALTVAGSILAKAQLEVTDVLTDRPPPIILQGPINQTLAVDGTALLKCKATGEPLPVISWLKEGFTFLGRDPRATIQDQGTLQIKNLRISDTGTYTCVATSSSGETSWSAVLDVTESGATISKNYDTNDLPGPPSKPQVTDVTKNSVTLSWQPGTPGVLPASAYIIEAFSQSVSNSWQTVANHVKTTLYTVRGLRPNTIYLFMVRAINPQGLSDPSPMSDPVRTQDISPPAQGVDHRQVQKELGDVTVRLHNPVVLTPTTVQVTWTVDRQPQFIQGYRVMYRQTSGLQASTVWQNLDAKVPTERSAVLVNLKKGVTYEIKVRPYFNEFQGMDSESKTIRTTEEAPSAPPQSVTVLTVGSHNSTSISVSWDPPPADHQNGIIQEYKIWCLGNETRFHINKTVDATIRSVVIGGLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITENNNSITEQITDVVKQPAFIAGIGGACWVILMGFSIWLYWRRKKRKGLSNYAVTFQRGDGGLMSNGSRPGLLNTGDPSYPWLADSWPATSLPVNNSNSGPNEIGNFGRGDVLPPVPGQGDKTATMLSDGAIYSSIDFTTKTTYNSSSQITQATPYATTQILHSNSIHELAVDLPDPQWKSSVQQKSDLMGFAYSLPDQNKGNNGGKGGKKKKTKNSSKAQKNNGSTWANVPLPPPPVQPLPGTELGHYPAEQENGYDSDSWCPPLPVQTYLHQGMEDELEEDEDRVPTPPVRGVASSPAISFGQQSTATLTPSPREEMQPMLQAHLDELTRAYQFDIAKQTWHIQSNTPPPQPPVPPLGYASGALISDLETDVPDEDADDEEEPLEIPRPLRALDQTPGSSMDNLDSSVTGKAFTSSQRQRPTSPFSTDSNTSAAQNQSQRPRPTKKHKGGRMDPQPVLPHRREGMPDDLPPPPDPPPGQGLRQQIGLSQHSGNVESSTERKGSSLERQQAANLEDTKSSLDCPAKTTVEWQHQTQDWINSTERQEETRKAPHKPGVGSEESLVPYSKPSFPSPGGHSSSGTASSKGSTGPRKAEILRGSHQRNANDLLDIGYVGSNSQGQFTGEL
Protein: DNA replication complex GINS protein psf1 (Q9P7X6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The GINS complex plays an essential role in the initiation of DNA replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA replication complex GINS protein sld5
- DNA replication complex GINS protein psf3
- DNA replication complex GINS protein psf2
- DNA replication licensing factor mcm2
- DNA polymerase epsilon subunit B
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm6
Sequence:
MENGLGNRSNKLIRDSKRTQYLDYLPPYQADTVNDVVNEIRAADRESLGILQNVTHEASQPFQPQDHPSEAAALLMFHSSSIYNKRCLMAYHNLRLQRLRQYCWSGGKRMESCLDTSLSTYERDYLTRYSELLAAYKGAWSELDLTGSLVPPKNLFIDVRVLKDVGDIETEYGTINLTKNSQLHVRATDVERLIAQGFLAKL
Protein: Ninjurin-A (dNINJ-A) [Cleaved into: Secreted ninjurin-A] (Q8MPP0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Homophilic transmembrane adhesion molecule involved in non-apoptotic necrotic cell death. Promotes cell adhesion by mediating homophilic interactions via its extracellular region (By similarity). Probably involved in non-apoptotic necrotic cell death by mediating plasma membrane rupture (cytolysis), leading to release intracellular molecules that propagate the inflammatory response.
Subcellular location: [Ninjurin-A]: Cell membrane {ECO:0000269|PubMed:23028562, ECO:0000305|PubMed:16815999}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secreted ninjurin-A]: Secreted {ECO:0000269|PubMed:16815999}.
Interaction partners:
Sequence:
MSNLEHITLEMDKVPLGDNKTLVRNTENISKHSYGGAIDGRTRNTLRVPRAVPETDDDDNDDRPFVKDGNDNPGVDDGLFSTVGGNGGNGGNVNVNVPNGGRRPSFSFPGYNGPGFVTINGVETPIPDVNAYQHKKTLAQGMMDLALLSANANQLRYVLETSSQHPYFYPSLLFISLSIIFQIAVGVGLILNGQYNIKNGHDICRANRINNYTVSGIFIVTVVNVLISAFTVDRDTVPALPANTT