wanglab/gogpt-training-data huggingface dataset:
Protein: Gap junction beta-6 protein (Connexin-30) (Cx30) (O95452)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction beta-2 protein
- Gap junction alpha-1 protein
- Gap junction beta-1 protein
- Gap junction gamma-1 protein
- Unconventional myosin-XV
- Consortin
- Gap junction gamma-2 protein
- Gap junction beta-3 protein
- Unconventional myosin-VIIa
- Cadherin-23
Sequence:
MDWGTLHTFIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETTRKFRRGEKRNDFKDIEDIKKQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTIFMISASVICMLLNVAELCYLLLKVCFRRSKRAQTQKNHPNHALKESKQNEMNELISDSGQNAITGFPS
Protein: Transient receptor potential cation channel subfamily V member 1 (TrpV1) (Osm-9-like TRP channel 1) (OTRPC1) (Vanilloid receptor 1) (Q704Y3)
Organism: Mus musculus (Mouse)
Function: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. {ECO:0000250|UniProtKB:O35433}.
Interaction partners:
- Calmodulin-4
- Calmodulin-like protein 3
- Calmodulin 5
- Calmodulin-like protein 4
- Calmodulin-1
- cAMP-dependent protein kinase catalytic subunit alpha
- Transient receptor potential cation channel subfamily A member 1
- Transient receptor potential cation channel subfamily M member 8
- cAMP-dependent protein kinase catalytic subunit beta
- Protein kinase C epsilon type
Sequence:
MEKWASLDSDESEPPAQENSCPDPPDRDPNSKPPPAKPHIFATRSRTRLFGKGDSEEASPMDCPYEEGGLASCPIITVSSVVTLQRSVDGPTCLRQTSQDSVSTGVETPPRLYDRRSIFDAVAQSNCQELESLLSFLQKSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDIARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTADNTKFVTNMYNEILILGAKLHPTLKLEELTNKKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTTAAYYRPVEGLPPYKLNNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSHRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPVESPPHKCRGSACRPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDFRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHSTQPEEVQLKHYTGSLKPEDAEVFKDSMAPGEK
Protein: Folylpolyglutamate synthase (EC 6.3.2.17) (DHFS-FPGS homolog D) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) (Q8W035)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Essential for organellar and whole-plant folate homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11752472}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Folate synthesis bifunctional protein
- Folate synthesis bifunctional protein
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Gamma-glutamyl hydrolase 1
- Gamma-glutamyl hydrolase 2
- GTP cyclohydrolase 1
- Probable gamma-glutamyl hydrolase 3
- Probable dihydroneopterin aldolase 3
Sequence:
MATEDDGELSARYQNTLDALSSLITKRGRLASNNQSHRFRLLFHYLKVLELEDAVSQMKIIHVAGTKGKGSTCTFAESILRCYGLRTGLFTSPHLIDVRERFRLNGIEISQEKFVNYFWCCFHKLKEKTSNEVPMPTYFCFLALLAFKIFTTEQVDVVILEVGLGGRFDATNVIQKPVVCGISSLGYDHMEILGYTLAEIAAEKAGIFKSGVPAFTVAQPDEAMRVLNEKASKLEVNLQVVEPLDSSQRLGLQGEHQYLNAGLAVALCSTFLKEIGIEDKNGLDQTNGLPEKFISGLSNAYLMGRAMIVPDSELPEEIVYYLDGAHSPESMEACAIWFSKQIKQNQERNQKRSEQILLFNCMSVRDPSLLLPRLRSKCIDQGVDFKRAVFVPNVSVYNQVGSSTNVGTRVESMSWQFGLQRIWESLARGEAKSNSKSDSKGKEEEKSFVFSSLPVAVDWLRDNARQSKQVRFQVLVTGSLHLVGDLLRFIKK
Protein: Uncharacterized J domain-containing protein C17A3.05c (O13633)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial protein import protein mas5
- DnaJ protein homolog xdj1
- Ubiquitin conjugation factor E4
- BAG family molecular chaperone regulator 1A
- Probable ubiquitin carboxyl-terminal hydrolase 16
- Heat shock protein homolog pss1
Sequence:
MESSREEALRCIGLARKYLNAGEYDKALKFANKSLRIHATTEGEDFVKQIEKQKLTGSPNPQATPKQENKSNFFSEKQSVRENGNSSAGEKKQKWTSEQHLLVQKIIKYKNHQYYEILDLKKTCTDTEIKKSYKKLALQLHPDKNHAPSADEAFKMVSKAFQVLSDPNLRAHYDRTGMDPESRASAASSSFSSNAGGHPGFSAYPQANMSPEDLFNSFFGDQFFSGPGTFFFGGGPGIRVHQFGGRPRNFARRQQAQDMPPKSIFYQLLPLIVVILFAFLSNFSWSDSTSVNTRYSFQQNYKYTVPRTTAKHNIPYYMSQKDLDKLSSRDIRRLNEKVEHTYTQNVHNACLREQQIKEDEIRRAQGWFFPDKEALKKAKELRLPNCEELNRLGYRTYSNSYYF
Protein: Thyroid hormone receptor interactor 11 (H3BJH8)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSSWLGGLGSGLGQSLGQVGGSLASLTGQISNFTKDMLLEGTEDVPADFPNSGREENEATHSVLRSENERLKKLYTDLEEKHEASELQIKQQSSSYRSQLQQKEEEINHLKARQLALQDELLRLQSAAQSAHLGSGSAPAASASSSFSYGVSHRVSAFHEDDMDFGDVISSQQEINRLSNEVSRLESELGHWRHIAQTKVQGAQSSDQTEICKLQNIIKELKQNRSQDLDDHQHELSALQNAHQQKLTEISRRHREEWLRSYDAENEIMRLRSLNQDISLAEDNQKLQMCV
Protein: Laminin subunit gamma-1 (Laminin B2 chain) (P15215)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
Interaction partners:
- Laminin subunit beta-1
- Laminin subunit alpha
- Integrin beta-PS
- Integrin beta-nu
- LP17136p
- Viking, isoform A
- Nidogen
- Collagen alpha-1
- Wing blister, isoform B
- Uncharacterized protein, isoform A
Sequence:
MKRSRWSHSGSSTARLLLIGVLFASCSTAILGAQRPPINSAGGHELRGTTFMPALECYDPYGRPQKCLPEFINAAYQLQIESTNTCGEQNDNHFCIQTMNQNHKNCEFCKYNDHNPSFLTDLHDPQSPTWWQSETMFEGIQHPNYVNLTLHLGKSYDITYVRILFRSPRPESFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRAIRKGEGEAHALCTSEYSDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDSQVLKSYFYAISDIAVGARCKCNGHASKCVPSTGMHGERTLVCECRHNTDGPDCDRCLPLYNDLKWKRSTSTEVNECKACNCNGLADKCFFDANLFNRTGHGGHCLDCRENRDGPNCERCKENFYMRDDGYCVNCACDPVGSRSLQCNSHGKCQCKPGVTGDKCDRCDNNYYQFGPHGCQQCGCDSGGSHQNTPACDTETGICFCKENVEGRRCNECKPGFFNLDKNNRFGCTPCFCYGHTSECMTAPGYSIVSVTSNFNKFKERWTAADLNQREVDIKYNQYSRSIGTTAQGNEHVYFQAPDRFLGDQRASYNRDLKFKLQLVGQVANTGVSDVILEGAGSRISLPIFAQGNGIPDQGVKEYTFRLHEHHDYQWQPSQSARGFLSILSNLTAIKIRATYSVQGEAILDDVELQTAHRGAAGHPATWIEQCTCPEGYLGQFCESCAPGYRHSPARGGPFMPCIPCDCHGHADICDSETGRCICQHNTHGDNCDQCAKGFYGNALGGTPNDCKRCPCPNDGACLQINEDTVICTECPKGYFGSRCEQCSDGFFGDPTGLLGEVQTCKSCDCNGNVDPNAVGNCNRTTGECLKCIHNTAGEHCDQCLSGHFGDPLALPHGRCDRCSCYEAGTEQDEQSITRCDQVTGQCQCKPNVIGRDCGECQPGYFNIRSGNGCENCLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGCKPCECDESGSKGFQCDQNGQCPCNDNVEGRRCDRCKENKYDRHRGCIDCPDCYNLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGLISKALPDSCFSRNRLEP
Protein: Taste receptor type 2 (Q2AB81)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}.
Interaction partners:
- Sodium channel epithelial 1 delta subunit
- Acid sensing ion channel subunit family member 5
- Polycystin 2 like 2, transient receptor potential cation channel
- Uncharacterized protein.
- Mucolipin 3.
Sequence:
MAEQHNTTSSSSAFVVIFAFQALAGMGINAFIVAASCMAWFKKKGMNSNEKILLFLGCFRFWYLCATWIYLIISVLFPQNLLDTGISLTFAIFMCFLSSSNLWTSTCLYAFYLMKIANFRHHFFIYLKARIDRIVPWLLLSSVVLSLLNCSPFLKVIDEENRTSPNFTTQGIFWKTNEEIRKHFNSIISICTCGFSMAFILVTLFAFFLLFSLCRHKHKMQTSSTRSLSMDAHIKAMKSLLSFFFTFSIHYILLITTVYYSSKENFLVLLLLVLQYSFPVIHSLILIFSNPRLERIALRILPCAKCKECARQPTETPMLCS
Protein: Receptor-type tyrosine-protein phosphatase R (R-PTP-R) (EC 3.1.3.48) (Phosphotyrosine phosphatase 13) (Protein-tyrosine-phosphatase SL) (Q62132)
Organism: Mus musculus (Mouse)
Function: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus. Isoform gamma may have a role in patterning and cellular proliferation of skeletal elements in the precartilaginous/cartilaginous skeleton.
Subcellular location: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. Note=Locates to the areas within the cytoplasm.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Locates to the areas within the cytoplasm.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 11
- Dual specificity protein phosphatase 3
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 10
- Tyrosine-protein phosphatase non-receptor type 5
- Tyrosine-protein phosphatase non-receptor type 7
Sequence:
MRRAVGFPALCLLLNLHAAGCFSRNNDHFLAIRQKKSWKPVFIYDHSQDIKKSLDIAQEAYKHNYHSPSEVQISKHHQIINSAFPRPAYDPSLNLLAESDQDLEIENLPIPAANVIVVTLQMDITKLNITLLRIFRQGVAAALGLLPQQVHINRLIEKKNQVELFVSPGNRKPGETQALQAEEVLRSLNVDGLHQSLPQFGITDVAPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFIIIVTCLMIIYRLKERLQLSLRQDKEKNQEIHLSPIARQQAQSEAKTTHSMVQPDQAPKVLNVVVDPQGQCTPEIRNSTSTSVCPSPFRMKPIGLQERRGSNVSLTLDMSSLGSVEPFVAVSTPREKVAMEYLQSASRVLTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLFESRLSPETVE
Protein: Small ubiquitin-related modifier 3 (AtSUMO3) (Q9FLP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9FLP6}. Cytoplasm {ECO:0000250|UniProtKB:Q9FLP6}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- SUMO-activating enzyme subunit 2
- E3 SUMO-protein ligase SIZ1
- Ubiquitin-like-specific protease ESD4
- SUMO-activating enzyme subunit 1B-1
- SUMO-activating enzyme subunit 1A
- E4 SUMO-protein ligase PIAL2
- E3 SUMO-protein ligase MMS21
- E4 SUMO-protein ligase PIAL1
- Ubiquitin-like-specific protease 1C
Sequence:
MSNPQDDKPIDQEQEAHVILKVKSQDGDEVLFKNKKSAPLKKLMYVYCDRRGLKLDAFAFIFNGARIGGLETPDELDMEDGDVIDACRAMSGGLRANQRQWSYMLFDHNGL
Protein: Hepatocyte nuclear factor 4 alpha (A0A087WXV4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
XMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGTNLNAPNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSRQITSPVSGINGDIRAKKIASIADVCESMKEQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYAYLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGDRGGHRRPL
Protein: 5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Brown locus protein) (Catalase B) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1) (P07147)
Organism: Mus musculus (Mouse)
Function: Plays a role in melanin biosynthesis. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Also to a lower extent, capable of hydroxylating tyrosine and producing melanin.
Subcellular location: Melanosome membrane {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18650808, ECO:0000269|PubMed:26620560}; Single-pass type I membrane protein {ECO:0000269|PubMed:17182842}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:26620560}.
Interaction partners:
- L-dopachrome tautomerase
- P protein
- Membrane-associated transporter protein
- Melanocyte protein PMEL
- Tyrosinase
- Melanocyte-stimulating hormone receptor
- Microphthalmia-associated transcription factor
- Melan-A
- Sodium/potassium/calcium exchanger 5
- G-protein coupled receptor 143
Sequence:
MKSYNVLPLAYISLFLMLFYQVWAQFPRECANIEALRRGVCCPDLLPSSGPGTDPCGSSSGRGRCVAVIADSRPHSRHYPHDGKDDREAWPLRFFNRTCQCNDNFSGHNCGTCRPGWRGAACNQKILTVRRNLLDLSPEEKSHFVRALDMAKRTTHPQFVIATRRLEDILGPDGNTPQFENISVYNYFVWTHYYSVKKTFLGTGQESFGDVDFSHEGPAFLTWHRYHLLQLERDMQEMLQEPSFSLPYWNFATGKNVCDVCTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEEYDTLGTLCNSTEGGPIRRNPAGNVGRPAVQRLPEPQDVTQCLEVRVFDTPPFYSNSTDSFRNTVEGYSAPTGKYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTFPLENAPIGHNRQYNMVPFWPPVTNTEMFVTAPDNLGYAYEVQWPGQEFTVSEIITIAVVAALLLVAAIFGVASCLIRSRSTKNEANQPLLTDHYQRYAEDYEELPNPNHSMV
Protein: Polyadenylate-binding protein (PABP) (Q99LF8)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNAAASSYPMASLYVGDLHSDVTEAMLYEKFSPAGPVLSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVMKGKPIRIMWSQRDPSLRKSGVGNVFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYAFVHFETQEAADKAIEKMNGMLLNDRKVFVGRFKSRKEREAELGAKAKEFTNVYIKNFGEEVDDGNLKELFSQFGKTLSVKVMRDSSGKSKGFGFVSYEKHEDANKAVEEMNGKEMSGKAIFVGRAQKKVERQAELKRKFEQLKQERISRYQGVNLYIKNLDDTIDDEKLRKEFSPFGSITSAKVMLEDGRSKGFGFVCFSSPEEATKAVTEMNGRIVGSKPLYVALAQRKEERKAHLTNQYMQRVAGMRALPASAILNQFQPAAGGYFVPAVPQAQGRPPYYTPNQLAQMRPNPRWQQGGRPQGFQGMPSALRQSGPRPALRHLAPTGNAPASRGLPTTAQRVGSECPDRLAMDFGGAGAAQQGLTDSCQSGGVPTAVPNLAPRAAVAAAAPRAVAPYKYASSVRSPHPAIQPLQAPQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQTMHSNLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHHAKKEAAQKVGTVAAATS
Protein: NalD (Q9HY46)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Transcriptional regulator MexT
- Outer membrane protein OprM
- Outer membrane protein OprJ
- Multidrug resistance protein MexA
- Multidrug resistance operon repressor
- NalC
- HTH-type transcriptional regulator NfxB
- Antirepressor for MexR, ArmR
- Multidrug resistance protein MexB
- Multidrug efflux outer membrane protein OprN
Sequence:
MRRTKEDSEKTRTAILLAAEELFLEKGVSHTSLEQIARAAGVTRGAVYWHFQNKAHLFNEMLNQVRLPPEQLTERLSGCDGSDPLRSLYDLCLEAVQSLLTQEKKRRILTILMQRCEFTEELREAQERNNAFVQMFIELCEQLFARDECRVRLHPGMTPRIASRALHALILGLFNDWLRDPRLFDPDTDAEHLLEPMFRGLVRDWGQASSAP
Protein: N-acetylgalactosaminyltransferase 7 (EC 2.4.1.41) (Polypeptide GalNAc transferase 7) (GalNAc-T7) (pp-GaNTase 7) (Protein-UDP acetylgalactosaminyltransferase 7) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7) (Q80VA0)
Organism: Mus musculus (Mouse)
Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRLKIGFILRSLLVVGSFLGLVVLWSSLSSRPDDQSPLSRMREDRDVNNPLPNRGGNGLAPGDDRFKPVVPWPHVEGVEVDLESIRRKNKAKNEQERHAGGDSQRDVMQRQYLTFKPQTFTYRDPVLRPGVLGNFEPKEPEPHGVVGGPGEKAKPLVLGPEYKQAVQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPIIDVISGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTSREKRLRKTKTEPYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPLYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESKALPYGDISELKKFREDHNCKSFKWFMEEIAYDITAHYPLPPRNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQYFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNNIHSV
Protein: CUB_2 domain-containing protein (Q17420)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine/threonine-protein phosphatase C23G10.1
- Nematode cuticle collagen N-terminal domain-containing protein
- NT-3
- C-type lectin domain-containing protein
- CUB-like domain-containing protein
- CUB domain-containing protein
- NADAR domain-containing protein
- Uncharacterized protein
- Transthyretin-like family protein
Sequence:
MIVPVLFSLFAVCNAQQILNLKDFDVNTGTKISQVAPYAIYVSASTDDTTLLKQINVKTTDNQVKNLYDLSRNHIMQNTGLLQPFVVNVTTEASISTTLSAEQMGKLTGFLYITTSKQLTNNHFLVYNVQEAELIKVPTDDYTIVFLNSNYSILTSQPFQSSSISAWSQTEGSSVKLYEGCPRDDAEKENSQFFSNPAVMINGKQMFFPVVEIFSLSLGAFYFKSSKGVQFVISNEFTDVNNRPTTSKITTGLYMKPITVNDRKVSIFTGHDDKLNGTIGVNVVGSVPANANFSVTYPIKWVTIPTNIIQSWSIPEISDRLGLDTINSVAGEVFVQYYMIQGNQSINPVTTTMLPGRQTTSRGIETTTKSNAIVQLFTSFIITILGARYL
Protein: Probable transcriptional regulatory protein YeeN (P0A8A2)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00918}.
Interaction partners:
- Serine/threonine-protein phosphatase 3
Sequence:
MGRKWANIVAKKTAKDGATSKIYAKFGVEIYAAAKQGEPDPELNTSLKFVIERAKQAQVPKHVIDKAIDKAKGGGDETFVQGRYEGFGPNGSMIIAETLTSNVNRTIANVRTIFNKKGGNIGAAGSVSYMFDNTGVIVFKGTDPDHIFEILLEAEVDVRDVTEEEGNIVIYTEPTDLHKGIAALKAAGITEFSTTELEMIAQSEVELSPEDLEIFEGLVDALEDDDDVQKVYHNVANL
Protein: 5-hydroxytryptamine receptor 3A (5-HT3-A) (5-HT3A) (5-hydroxytryptamine receptor 3) (5-HT-3) (5-HT3R) (Serotonin receptor 3A) (Serotonin-gated ion channel receptor) (P46098)
Organism: Homo sapiens (Human)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:9950429}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}. Cell membrane {ECO:0000305|PubMed:9950429}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}.
Interaction partners:
- 5-hydroxytryptamine receptor 3B
- 5-hydroxytryptamine receptor 3D
- 5-hydroxytryptamine receptor 3C
- 5-hydroxytryptamine receptor 3E
- Protein RIC-3
- 5-hydroxytryptamine receptor 2A
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor 1
- Glutamate receptor 2
Sequence:
MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA
Protein: Alpha-(1,3)-fucosyltransferase fut-3 (EC 2.4.1.65) (Fucosyltransferase fut-3) (G5EFP5)
Organism: Caenorhabditis elegans
Function: Catalyzes the addition of fucose in alpha 1-3 linkage. Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2-Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (GnM3F6) acceptors.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
Interaction partners:
- Galactoside 2-alpha-L-fucosyltransferase
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase
Sequence:
MRVRPASVYRYLLLGVCALLGIYTVYSIIGYDDGSHVPIHRPQRHLYLTVSQDRIGSRFGKLAPKRILYWTTIFGATVPSTALSDCPGLTDRCVIDTNRHQLDSADAVVFHAADISKFPLPVSRKPDQIFVFNSMETPDNSGRFAVPDGFFNWTSTHLYSSDAIHKYGTFLIPTQIAESRGFKVQSYYVQPKRLVKTMKGIFGLISNCHTKSKRELALQELGKHINVTIGGKCASDDRLKSICPAGVECIDVFEQYPFYIAIENTVCNDYVTEKIWSRITVPSIPIVMRRRVYQNILPPKSFIAMDDYKNPSEMANHLRSLEANSTAYGEYFEWRQKGLWTSAPWNAPGYRNGLCRVCELLWKAKDNETEVYKSYDNIWKWFDNESQCETDEFVRSWLSG
Protein: IgA receptor (P13050)
Organism: Streptococcus pyogenes
Function: Binds IgA of both subclasses, and also binds polyclonal IgG weakly.
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}.
Interaction partners:
- LPXTG cell wall anchor domain-containing protein
Sequence:
MARKDTNKQYSLRKLKTGTASVAVAVAVLGAGFANQTEVKAAEIKKPQADSAWNWPKEYNALLKENEELKVEREKYLSYADDKEKDPQYRALMGENQDLRKREGQYQDKIEELEKERKEKQERQEQLERQYQIEADKHYQEQQKKHQQEQQQLEAEKQKLAKDKQISDASRQGLSRDLEASRAAKKELEAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAALTAEHQKLKEDKQISDASRQGLSRDLEASREAKKKVEADLAEANSKLQALEKLNKELEEGKKLSEKEKAELQARLEAEAKALKEQLAKQAEELAKLKGNQTPNAKVAPQANRSRSAMTQQKRTLPSTGETANPFFTAAAATVMVSAGMLALKRKEEN