wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) (P30533)
Organism: Homo sapiens (Human)
Function: Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway.
Subcellular location: Rough endoplasmic reticulum lumen {ECO:0000269|PubMed:7774585}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000269|PubMed:7774585}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:7774585}. Golgi apparatus lumen {ECO:0000269|PubMed:7774585}. Endosome lumen {ECO:0000269|PubMed:7774585}. Cell surface {ECO:0000269|PubMed:11384978}. Note=May be associated with receptors at the cell surface. {ECO:0000269|PubMed:11384978}.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
- Ral guanine nucleotide dissociation stimulator
- Low-density lipoprotein receptor-related protein 2
- Rap guanine nucleotide exchange factor 4
- Sortilin-related receptor
- Rap guanine nucleotide exchange factor 3
- Low-density lipoprotein receptor-related protein 8
- Ras-related protein Ral-A
- E3 ubiquitin-protein ligase MYCBP2
- Very low-density lipoprotein receptor
Sequence:
MAPRRVRSFLRGLPALLLLLLFLGPWPAASHGGKYSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQVTSNSLSGTQEDGLDDPRLEKLWHKAKTSGKFSGEELDKLWREFLHHKEKVHEYNVLLETLSRTEEIHENVISPSDLSDIKGSVLHSRHTELKEKLRSINQGLDRLRRVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLEIAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL
Protein: Peroxisomal ATPase PEX6 (EC 3.6.4.-) (Peroxin-6) (Peroxisomal biogenesis factor 6) (A0A061IR73)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (By similarity). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13608}. Peroxisome membrane {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q13608}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. Localized at the base of the outer segment of photoreceptor cells. {ECO:0000250|UniProtKB:Q13608}.
Interaction partners:
Sequence:
MALAVLRVLDPFPAETPPLAVLLPPGGPWPATGLGLVLALRPASESPAGPALLVAALEGPGSQNGQRGPGPPQLLVSRALLRLLALGPGARVRARPVRRPPALGWALLGSAPGPGPGPRVGPLLVRRGESLPVPGSRVLETRPALQGLLGPGTRLAVTELRGRAKLGPESTQHSRLPPPPVASSFAVSHAVRQLKGVLGGTGDALGVTRSCLRGLGLFQGEWVWVARVGEFPNTSQPHLAKVQLLEPRWDLSERLGPSSGQLGEPLADGLVFVPATLAFNLGCDPLEVGELRIQRYLEGSIIPEDRGSCSLMSGPPFARELHIEIVSSPHYSANGDYDHVLYRHFHTPRVVQEGDVLCVPTVGQVEILEGSPEKLPRWREVFFKVKKAVGEAPDGPASAFLADTTHTSLYMAGSALSRVPLLPSGRSTPWDSLSPPGLEALVNELCAILKPHLQPGGTLLTGTSCVLLQGPPGSGKTTAVTAACSRLGLHLLKVPCYSLCADSSGAVETKLQAAFSRARRCRPAVLLLTAIDLLGRDRDGLDEDARVVATLRHLLLDEDPVSNCPPLMVVATTSRAQDLPTDVHTAFPHELEVPVLSEEQRLSVLQALTAHLPLGQEVNLLQLARRCAGFVVGDLYALLTHTSRVACARIRASGLAGGLSEEDEGELCAAGFPLLAEDFGQALDQLQTAHSQAVGAPKIPSVSWHDVGGLQDVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGASEDRASQLRVLSAITRKFKLEASVSLVNVLDRCPPQLTGADLYSLCSDAMTTALKRRVRDLEEGLEMGSSALLLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC
Protein: Dymeclin (Q18668)
Organism: Caenorhabditis elegans
Interaction partners:
- Nudix hydrolase 3
- HID-1
- Vps54_N domain-containing protein
Sequence:
MGSVITKETVLQENIYLKKLSGLEPVDDYDPFWNKLLSFSLKFDDDDEDTRIALESALDDHLQCLMYNTQTTGNFAAFIRLFLRRATELKTSEQCENKIYLWQTSNALLILRYIARFLTQRMTEKEFVRIFAKSHESTETESSSTSSSSDEEDDDEQKSENENNNGATKYIPIVFQNTAEEFTYELVSILINISVNETTLAIHVEAVRCLLTLLSSQLYNESIVNTSIVFRFFIDGSCAKHAASLTKTLLLNYLIHNSEYHMTVQKPQESIVFGLASSMWSMVQMATGIDSAEEEKKPPLTLGNLSILLLLNLSCHQPLNSSNPFKETLALFQNAQEVSTLPTQIVSFKIDYNGLYERLCATAGQEPPMLLLYMLLQANSGFRNYVLSRINLENLVVPVLRILHDGVATSNNSHHVYLALIVALILSEDDIFCKIIHETMIKDLGWLDSDFSVREISLGGLTTLVLVRAIQKNALKTRDRYLHTNCLAALANMSAFFKNLAPIVCQRLISLLDLLTKRHAKMVDHMRVSSQNDVADGQPINFHDDITALEEGIRTLLEIINSALCGGLRHNSHLIYNLLYHRALFDAYVQHPMFQDLLVNIAAVISHFSSKVIHVPAGDGSTMLQIIEKEANIWPTDRLAKFPELKFRYVEDEYTVDFFVPYVWRLSVQHSGIYFETSRIKIFNAQSIA
Protein: Dolichyl-phosphate beta-glucosyltransferase (EC 2.4.1.117) (Wollknaeuel) (Q9VLQ1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal production of N-glycosylated proteins in the endoplasmic reticulum (ER). Required for embryonic segmentation, dorsal-ventral patterning and gastrulation. Required for chitin orientation and shaping of the apical and lateral plasma membranes of epidermal cells during cuticle differentiation. Also required for correctly shaping apical membrane topology of the epithelia of other organs such as the midgut and the hindgut.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21199819}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dol-P-Man:Man
- Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase Alg3
- Alpha-1,2-mannosyltransferase Alg9
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 1
- dolichol kinase
- Insulin receptor substrate 53 kDa, isoform A
Sequence:
MWTCLCQLCFYLLSTLAVAALSIAALVLYKTKPYPNIKRHKDEETFLDPHTIKTVTFPSLEDSPSLELSVIVPAYNEEQRLPSMLDECLAFLEQKSAGTPNFTYEVIVVSDGSQDATVSVALGYSKKHGAEKVRVLELIENRGKGGAVRMGMLSARGRNLLFADADGATKFPDYDKLEVALKQLAPEWRDDGIAIGSRAHLENDAIATRSFFRTILMHGFHFLVWLFAVRSIRDTQCGFKLFTRTTARKLFTSLHVERWAFDVELLYLAENLKLPMSEVAVRWTEIDGSKLTPFWSWLQMGRDLFMIWVRYLVGAWRIASIQKKEK
Protein: Acid-sensing ion channel 1 (ASIC1) (Amiloride-sensitive cation channel 2, neuronal) (Brain sodium channel 2) (P78348)
Organism: Homo sapiens (Human)
Function: Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12578970, ECO:0000269|PubMed:21036899}; Multi-pass membrane protein {ECO:0000269|PubMed:32915133, ECO:0000269|PubMed:34319232}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q6NXK8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}. Note=Isolated in synaptosomes from the dendritic synapses of neurons. {ECO:0000250|UniProtKB:Q6NXK8}.
Interaction partners:
- Acid-sensing ion channel 2
- PRKCA-binding protein
- P2X purinoceptor 4
- Ubiquitin-conjugating enzyme E2 G1
- Stomatin
- Serine/threonine-protein kinase Sgk3
Sequence:
MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
Protein: Nuclear receptor subfamily 1 group I member 2 (Orphan nuclear receptor PXR) (Pregnane X receptor) (Q9R1A7)
Organism: Rattus norvegicus (Rat)
Function: Nuclear receptor that binds and is activated by a variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, endogenous compounds and drugs. Response to specific ligands is species-specific, due to differences in the ligand-binding domain. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Nuclear receptor coactivator
- Cytochrome P450 2B3
- Cytochrome P450 3A1
- Nuclear receptor subfamily 0 group B member 2
- Ectonucleoside triphosphate diphosphohydrolase 8
- Cytochrome P450 1A2
- Cytochrome P450 3A
- Cytochrome P450 7A1
- Bile salt export pump
Sequence:
MRPEERWNHVGLVQREEADSVLEEPINVDEEDGGLQICRVCGDKANGYHFNVMTCEGCKGFFRRAMKRNVRLRCPFRKGTCEITRKTRRQCQACRLRKCLESGMKKEMIMSDAAVEQRRALIKRKKREKIEAPPPGGQGLTEEQQALIQELMDAQMQTFDTTFSHFKDFRLPAVFHSDCELPEVLQASLLEDPATWSQIMKDSVPMKISVQLRGEDGSIWNYQPPSKSDGKEIIPLLPHLADVSTYMFKGVINFAKVISHFRELPIEDQISLLKGATFEMCILRFNTMFDTETGTWECGRLAYCFEDPNGGFQKLLLDPLMKFHCMLKKLQLREEEYVLMQAISLFSPDRPGVVQRSVVDQLQERFALTLKAYIECSRPYPAHRFLFLKIMAVLTELRSINAQQTQQLLRIQDTHPFATPLMQELFSSTDG
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (E9PM53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDACAGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ
Protein: Rhomboid-related protein 4 (RRP4) (EC 3.4.21.105) (Rhomboid domain-containing protein 1) (Rhomboid-like protein 4) (Q8TEB9)
Organism: Homo sapiens (Human)
Function: Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22795130}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18953687}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Rhomboid-related protein 1
Sequence:
MQRRSRGINTGLILLLSQIFHVGINNIPPVTLATLALNIWFFLNPQKPLYSSCLSVEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLQFAVAEFMDEPDFKRSCAVGFSGVLFALKVLNNHYCPGGFVNILGFPVPNRFACWVELVAIHLFSPGTSFAGHLAGILVGLMYTQGPLKKIMEACAGGFSSSVGYPGRQYYFNSSGSSGYQDYYPHGRPDHYEEAPRNYDTYTAGLSEEEQLERALQASLWDRGNTRNSPPPYGFHLSPEEMRRQRLHRFDSQ
Protein: Uncharacterized protein C23C11.01 (O13909)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- CTP-dependent diacylglycerol kinase 1
- Uncharacterized protein C962.01
- Vesicle-associated membrane protein-associated protein scs2
- Uncharacterized protein C691.05c
- Dolichol kinase sec59
Sequence:
MDQEIRSNNYDISVSTVEDTSFEAMDDSILEIIDDEAPEIQGKPKANISTHFRNMLAMFGNFLSLGFFLVIIVLVGIAFEIGGRFCGLILTLALEVYFFSTALLKLFGLRKIALTLHFFEPLLVFILLIIALNASPSIEQNKYASFLASAWNTALLHFTPLFNLLEGMASLLVVQALGHLSRWLVHNKSENWMFFILLNASSAISMSLYLLYRVSSFSISNPNALMIGFSLATVIVISIYGVASGRANLSEASLMFLYIAYTVYMVCTDFGNPNTSSLEKPKFDYLPPNILQSVHYLISTISATLPRTLYNIVLFMVAAAKTVAPSVFATFAFRISVMYAVTRILPAIQNNIIFLEYSRTSKQGMWSILSPCILIAVYTNLLLQHLYPTPSFTSPVNQILCSAEIWRWVSAILTLLLYAIELAYSKESDTGQALASHFKLD
Protein: SLC29A2 protein (Q96FB2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNHWVTLLSQLPLLLFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLLAMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAELLQSDLADSAVPCVGLHSHPVRLPRHHSHGDQLHQSWEVESVLQPHLLLPPLQHHGLAGTEPDLLLPVARRGQPAAAPAGLPAVPVRAPLHAVPRAPEVPAAHPLPTGCLLHHLHAALCRF
Protein: CG10321 (Q2XY74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ELDKICRLCISERKEMRPLFSEKVPEMLMDCTSVRVEPTEGWPDKICVQCVHAVSRNHAFKTLVERSDKELREYIRGLTVALVMEEQQQQEAANAKQQLQLERKQQRQLQKQQKILEEQLQQQIVQQQQHQPPAKPKLKPLLRKGSRQQKQRHLEAAPAPQSVPQPAPQPQMQLMQEHAPQQPTMQQQIQQIHMPTLQPAPAQLLSAAGATTTMPQQILLPNGQLITTAQIVAPQLAQIISTAPQSTTNGQATAAQSQFLPQLLQTPNGQTLQIVQQPNGTQTLQLVQLVPQRSLAPTGVTTVTTTTNATDMGQHVGASLGDADVQLLEDGCEVEDEELEDVYEQLDSKADHSFETIVLDDDQQQDFLKDHHEHHQVMINEDLTQSESQDHEYFDDLDQQQAMDEIEDEEEQMKPEEDQDTFIIEEIQLEDDEMLDDPDGEEIDQDCEYIGEEQDPHLSGDVDDDLEYSIMEPPDGETSVDIDQAFMDSEQSHHQQHQEEMQSISLENAVVEFSQATTTTEALVGPTMTVSSASPTPKRAKRSNHQIPAGVTLEPCDHQPPAAGSTTSSKLAAANSRQLVQTASVIAAAGADDNYEIDANLVTEFIRQHTSPLGSGRYICHLCSTEFRQFKGLQNHMHSHTNWIRANCKKQPQCQICLKSFKGPGMLRMHMKTHDAESSTPMCTICNRTFKSKAILYRHRQTHQQRAYCCGVANCRKNFSSAVNLKWHVERKHPEVVDPLFKCGECGSLYDNVDSLQLHVESTDHSAEVQISGQDDAFSGAVSIVSNGTTDMSNMMATGQGTTLAGGTGDTHAVVMGSSGEV
Protein: Frizzled-5 (Fz-5) (Xfz5) (P58421)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQD0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQD0}. Note=Localized at the plasma membrane and also found at the Golgi. {ECO:0000250|UniProtKB:Q9EQD0}.
Interaction partners:
Sequence:
MGSFRSGVFALSFVVLLLDYFAPAQAASKAIVCQEITVPMCKGIGYNHTYMPNQFNHDTQDEAGMEVHQFWPLVVIQCSLDLKFFLCSMYTPICLPDYRKPLPPCRSVCERAKAGCSPLMRKYGFAWPERMNCDRLPEHGDPDTLCMYYNWTETTTTLPPTHPPKVKTPTSDCDGVCKCREPFVSITRESHPLYNRIKTGQVPNCAMPCFQPYFTQDEKMFVTFWIGLWSILCFISTFTTVATFLIDMERFRYPERPIIFLSACYLFVSIGYVVRLIVGHENVACNKDHIHYETTGPALCTIVFLLIYFFGMASSIWWVILTFTWFLAAGMKWGNEAIASYSQYFHMAAWLIPSVKSIAVLALSSVDGDPVAGICYVGNQNLDNLRGFVLAPLVVYLFSGTMFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFSVLYTVPATIVVACYIYEQHYREHWEKTHNCSCPGDKQRYRPDYAVFMLKYLMCLVVGITSGVWIWSGKTLESWKRFTGRCCRNSKPINASAYSEASRALTPRTGLSNLTLPHKQVPLSHV
Protein: Uncharacterized membrane protein C61.05 (O94349)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein MIX23
- Bifunctional purine biosynthesis protein ade10
- Meiotic expression up-regulated protein 27
- Aspartic proteinase yapsin-1
Sequence:
MRINFVLLITLILPWFVSGDSSEEAVDAPLDVKDDTGNKDYYKDSTGAYHFDKLIVTPLEYRDGESWKQSVIYCDLIFAKENKEEKGSFVKAQLKEDAEHPFIYRLLKLQTPLETYRGFIDGKNTEILDEIKSINLFEDFLSESLVPEISPSVNIPIDETALYCFIGIQETEPIRIPWPVLTVEFYGDAPPPESYFRTIKSTLLAISMFLGFITLTWLLRCIKSQSGVQPAQISLAFWVFIFVFTHSYQVYSMVAIGRGSFSTWYVVSFLFSLVFEEGLEQSAYTSFLLVLCFGLGITKPALVKYYVYLAFVAFVQGLFVTFAPLSYPVMSFYGVRGILLKLIWNIYTFVYYGLPFFAVYRLYKQAGESRKLGFEAKYSLLRTCYIALAAVTVSNCLFLGVVRPLLGSQLSLGFQLITSCITFVDFLVFAFLFDCSKFVFLKYQPIPFEWYALESMESLNLEPAPDRKV
Protein: Uncharacterized transcriptional regulatory protein C27B12.11c (O13658)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- Probable metabolite transport protein C1271.09
- Acid phosphatase
- Uncharacterized transporter C3B8.04c
- Putative inorganic phosphate transporter C8E4.01c
- Serine/threonine-protein kinase csk1
- Probable cyclin-dependent kinase 9
- UPF0400 protein C337.03
- Chromatin structure-remodeling complex subunit sfh1
- Putative D-3-phosphoglycerate dehydrogenase
- DNA polymerase epsilon catalytic subunit A
Sequence:
MQKKVVQSASKNEELDPHYKRSSVPFPYGLPDYDAEYQFINHHMQQLLTRPVEGTHSASVHPSTSSTSHISSPSAFSVQNPNPNDAPFVGNIGLDASGFSSGGMSEYYPRSVSMQQSQDVHFQNTEIPYYHRSPSSDSFSPGVVASVNPNSNNSPTFYSNPPALSNIPIPLNNSPYRPEDAYFQLQGAGVKADINPYNLSPYSQYGPEGTAYSNAQAHHQDGAPLQRVCSAPDPPKTSMPPFGSAGSPSPNRSLNVSNNTTPPLSTVNKIIKKPKATTGKVKKRLPQAKRACAKCQKDNKKCDDARPCQRCIKAKTDCIDLPRKKRPTGVRRGPYKKLSDTSNNTKSTTASSGHSTQDSLSSKMLDPSSDNQFAMSSRQMDENGMAQYPSSAIKQELNLQPQILVSSASKNFQPNVTPPFAVHHDHFNSTSMDGVAVSNMDETGTSSAGSKPFNRKSRNRSFTNPVGMTEEHFLREYAQHSVANPSLLIHQIHGLPSEQVHGLLSHTELGNAMHNQPTYNESSIAAENVNNWMLETNDHENLSMQSHFEVPDLKMNHHDSSFFDRHIDQTAMPGQNQHGTVKNMETMHHFYPDVHNSEFPAAPNPVKSQVPYYYQSQAADDEEEDVPDHQPSWRGRIHSFSIATDSSQHVVERPCIHSLRGIHGQQDGGLEQHDGDHVNMLPDTHAEELAYTSMLLFHDIPTRDIRPDFNVHELVDHGTYPNFHQNQADSFKNHPFRQ
Protein: Epsin-3 (EPS-15-interacting protein 3) (Q9H201)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11359770}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359770}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:11359770}. Nucleus {ECO:0000305|PubMed:11359770}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus.
Interaction partners:
- Epidermal growth factor receptor substrate 15
- Clathrin heavy chain 2
- Clathrin coat assembly protein AP180
- Clathrin heavy chain 1
- Huntingtin-interacting protein 1-related protein
- Intersectin-1
- Epidermal growth factor receptor substrate 15-like 1
- Intersectin-2
- Epsin-2
- Phosphatidylinositol-binding clathrin assembly protein
Sequence:
MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIGIGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQLQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQSSILDLADIFVPALAPPSTHCSADPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILGEALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQVAKTRNPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPFL
Protein: Calcium uptake protein 1, mitochondrial (A0A286YF11)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MFRLNSLSALAELAVGSRWYHGGSQPIQIRRRLMMVAFLGASAVTASTGLLWKRAHAESPPCVDNLKSDIGDKGKNKDEGDVCNHEKKTADLAPHPEEKKKKRSGFRDRKVMEYENRIRAYSTPDKIFRYFATLKVISEPGEAEVFMTPEDFVRSITPNEKQPEHLGLDQYIIKRFDGKDFWQTEKISQEREKFADEGSIFYTLGECGLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQRKLQHDVLKLEFERHDPVDGRITERQFGGMLLAYSGVQSKKLTAMQRQLKKHFKEGKGLTFQEVENFFTFLKNINDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRLMRGLEKPKDMGFTRLMQAMWKCAQETAWDFALPKQ
Protein: Adaptin medium chain homolog APM2 (Adaptin-mu1-II) (P38700)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates of cargo protein sorting in clathrin-coated vesicles. AP-1R has a specific role in SNARE SNC1 sorting. In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:26658609}; Peripheral membrane protein {ECO:0000269|PubMed:26658609}. Early endosome membrane {ECO:0000269|PubMed:26658609}; Peripheral membrane protein {ECO:0000269|PubMed:26658609}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:26658609}; Peripheral membrane protein {ECO:0000269|PubMed:26658609}.
Interaction partners:
- AP-1 complex subunit sigma-1
- AP-1 complex subunit beta-1
- AP-1 complex subunit gamma-1
- AP-2 complex subunit beta
- AP-3 complex subunit delta
- AP-2 complex subunit alpha
- AP-2 complex subunit mu
- Methyltransferase OMS1, mitochondrial
- OTU domain-containing protein 2
- tRNA pseudouridine synthase 4
Sequence:
MSSSLFILDENLEPLVSKNIRALPNLSSVLSSFKQCYHDGSPPILSQNDWFFIHLKRDFLHFVSVIHTTDKPNIDLMTILAFLEQFYHLLQKYFEIEVLTKNVILDNILLVLELIDECIDFGIVQVTDPSIIKDYIRVKVNVPRVTVDNEEWSPGEESSSSSGSDSDSEYSNTNKRKDKKKKRKKKKGTKGKSVGKSKLKSIMVNNKENRGINVVETVKETLRNKNDTGKEAANDELPNDGNDLYINGDIAKTIIMPISWRTKGIHYAKNEFFLDVIERVQYLMDFEKGVIRKNLIHGEIVCRCYLSGMPKLKISINKILNRDPQFMSNSSFHQCVSLDSINTIEKDEEKNSDDDAGLQAATDAREIEFIPPDGEFVLCQYELKRHVKDAPMVRLKDFEIKPKLKKFKIQIVTKIQTNFKPTNSTSKLNVRIPLTKVFQEYKIDLSKQIRFKANIGKVVFNLSDDFLLWEIQTMKGHREHSTNKSSQYNSDEDDPNTCASMVAEFPLFNQEEYDRLQEEMKTSMNPPPLRTGPRLEELYRQVHDQQTSHVTPRDKLVNIDFEIPYCTCSGLKVEYLKVEEPQLQYQSFPWVRYKTVSDEEYAYIV
Protein: Pituitary homeobox 3 (Bicoid-like homeodomain transcription factor Pitx3) (Homeobox protein PITX3) (Paired-like homeodomain transcription factor 3) (Q6QU75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional regulator which may play a role in the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons (By similarity). Required for lens and retinal development and for pituitary pre-placode formation and cell specification.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35160, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
Interaction partners:
- Nuclear receptor subfamily 4, group A, member 2a.
- Nuclear receptor subfamily 4, group A, member 2b.
- Forkhead box E3
- Beta-crystallin B2
- Transporter
- Tyrosine 3-monooxygenase
Sequence:
MDFNLLTDSEARSPALSLSDSGTPQHDPGCKGQDNSDTEKSHQNHTDESNPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGAQFNGLMQPYDDMYSGYSYNNWATKSLASSPLSAKSFPFFNSMNVSPLSSQPMFSPPSSIPSMNMASSMVPSAVAGVPGSGLNNLGNLNNLNSPTLNSAAVSAAACPYATTAGPYMYRDTCNSSLASLRLKAKQHANFAYPAVQNPVSNLSPCQYAVDRPV