wanglab/gogpt-training-data huggingface dataset:
Protein: Transient receptor potential cation channel subfamily M member 8 (Cold menthol receptor 1) (Q8R455)
Organism: Rattus norvegicus (Rat)
Function: Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonists menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8R4D5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7Z2W7}. Membrane raft {ECO:0000269|PubMed:19176480}. Note=Lipid raft association of TRPM8 modulates channel activity. {ECO:0000269|PubMed:19176480}.
Interaction partners:
- Transient receptor potential cation channel subfamily V member 1
- Transient receptor potential cation channel subfamily A member 1
- Transient receptor potential cation channel subfamily V member 2
- Transient receptor potential cation channel subfamily V member 3
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Transient receptor potential cation channel subfamily V member 4
- G protein-coupled receptor 55
- Ankyrin 1
Sequence:
MSFEGARLSMRSRRNGTLGSTRTLYSSVSRSTDVSYSESDLVNFIQANFKKRECVFFTRDSKAMESICKCGYAQSQHIEGTQINQNEKWNYKKHTKEFPTDAFGDIQFETLGKKGKYLRLSCDTDSETLYELLTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSRLIYIAQSKGAWILTGGTHYGLMKYIGEVVRDNTISRNSEENIVAIGIAAWGMVSNRDTLIRNCDDEGHFSAQYIMDDFMRDPLYILDNNHTHLLLVDNGCHGHPTVEAKLRNQLEKYISERTSQDSNYGGKIPIVCFAQGGGRETLKAINTSVKSKIPCVVVEGSGQIADVIASLVEVEDVLTSSMVKEKLVRFLPRTVSRLPEEEIESWIKWLKEILESPHLLTVIKMEEAGDEVVSSAISYALYKAFSTNEQDKDNWNGQLKLLLEWNQLDLASDEIFTNDRRWESADLQEVMFTALIKDRPKFVRLFLENGLNLQKFLTNEVLTELFSTHFSTLVYRNLQIAKNSYNDALLTFVWKLVANFRRSFWKEDRSSREDLDVELHDASLTTRHPLQALFIWAILQNKKELSKVIWEQTKGCTLAALGASKLLKTLAKVKNDINAAGESEELANEYETRAVELFTECYSSDEDLAEQLLVYSCEAWGGSNCLELAVEATDQHFIAQPGVQNFLSKQWYGEISRDTKNWKIILCLFIIPLVGCGLVSFRKKPIDKHKKLLWYYVAFFTSPFVVFSWNVVFYIAFLLLFAYVLLMDFHSVPHTPELILYALVFVLFCDEVRQWYMNGVNYFTDLWNVMDTLGLFYFIAGIVFRLHSSNKSSLYSGRVIFCLDYIIFTLRLIHIFTVSRNLGPKIIMLQRMLIDVFFFLFLFAVWMVAFGVARQGILRQNEQRWRWIFRSVIYEPYLAMFGQVPSDVDSTTYDFSHCTFSGNESKPLCVELDEYNLPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGIVQENNDQVWKFQRYFLVQEYCNRLNIPFPFVVFAYFYMVVKKCFKCCCKEKNTESSACCFRNEDNETLAWEGVMKENYLVKINTKANDNAEEMRHRFRQLDTKLNDLKGLLKEIANKIK
Protein: Signal recognition particle receptor subunit alpha homolog (SR-alpha) (Docking protein alpha) (DP-alpha) (O43032)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the SRP (signal recognition particle) receptor (SR). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32916}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32916}; Cytoplasmic side {ECO:0000250|UniProtKB:P32916}. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
Interaction partners:
- Signal recognition particle receptor subunit beta
- Signal recognition particle subunit SRP54
- Signal recognition particle sec65 subunit
- Signal recognition particle subunit srp68
- Signal recognition particle subunit srp72
- Uncharacterized protein C17H9.07
- Signal recognition particle subunit srp14
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL23B
- Large ribosomal subunit protein uL23A
Sequence:
MIDLFAIVNKGGIVLWKKTNSLVNLKCLQVLFHEAFLSEQRTVNNTVTFDRYTMQYQEATQYSIVFVVVFQDLKCMAYSQSLLNSAHNIFLNLFKEKLEDRQVPNEAEVEKLFAPIFNRKSAQLENETDTKSLPVEANNDNSARKKNEYEMKKKGAQSKQTNAPKKGKKQLRKWDDQITEEEQAALNYSSQASSASQTVDNSQLSSIVGNNNKFQKTGSGDVIISDLEMDPNQTISNKSASSAFSLFSNLIGGKYLKEEDLSPILKQMQEHLTKKNVANSIALELCESVKASLINKKVGSFDTVKNTVNKAFRDRLTQILTPSTSLDLLHSIRSVRKNENRPYTISLIGVNGVGKSTTLAKIAYWLLSNNFRILVAACDTFRSGAIEQLGVHVKNLQSLKGSSIELFAQGYGKDSSFVVKNAVEYAKQNSFDVILIDTAGRRHNDQRLMGSLEKFTKATKLDKIFQVAEALVGTDSLAQAKHFQASLYHRPLDGFIISKVDTVGQLVGVMVGMVYAVRVPIIFVGIGQTYSDLRTLSVDWVVDQLMK
Protein: Acetylcholine receptor subunit gamma precursor (Cholinergic receptor, nicotinic, gamma) (E7F9V1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Acetylcholine receptor subunit alpha
- 43 kDa receptor-associated protein of the synapse
- Docking protein 7.
- Cholinergic receptor, nicotinic, alpha 4b
- Cholinergic receptor, nicotinic, alpha 2a
- Cholinergic receptor, nicotinic, alpha 7
- Cholinergic receptor, nicotinic, beta 1
- Muscle, skeletal receptor tyrosine-protein kinase isoform 3 precursor
- Acetylcholine receptor subunit epsilon precursor
- Cholinergic receptor, nicotinic, beta 4
Sequence:
MDQNLSSKIIWLWILLFRFSGALCNLEGSLHRDLMVGYNKNIRPVESHEDIIDVKIKMTLTNLISLNEKEETLTTCVWIEMQWRDYRLRWANRTGFEVYENITRMRLPSKTIWLPDIGLENNVDGRFEVALYANTLIDPDGSVYWLPPAIYRSSCAIKVNYFPFDWQNCSMVFRSQTYNSNEITLMLSDEDNVTMEWIEIDPEAFTENGEWMIKHRPAKKVINKRYRPDELEHQEIIFFLIIQRKPLFYVINIIVPCVLFSSLGLLVYFLPAKAGGQKCTMTICILLGQTVFLFLIAKKVPETSQAVPLIGKYLMFVMSVTTITVMNCVVVLNVSLRTPNTHPMSNTIRKVLLNILPRVLRMTMQRWTPEQEEGDFKMFALGNGTPLRRRRRSSLGLIAKADEYMFRTARSELMFSRLKERKGLLKNTLEKIQNGLGGNTAQDLECSLAAASPEVQQCVSSCKHIAESTKHQNDFQSKNEEWFLVARVIDRMCFFVMALLFILGTIGIFLTGHFNQAPSQPFPGDPKKYLPEISAGDIPG
Protein: Interferon 1ha4 (Interferon zeta) (Q8BQT1)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLPVHLFLVGGVMLSCSPASSLDSGKSGSLHLERSETARFLAELRSVPGHQCLRDRTDFPCPWKEGTNITPMTLGETTSCYSQTLKQVLHLFDTEASRAAWHERALDQLLSSLWRELQVLKRPREQGQSCPLPFALAIRTYFRGFFRYLKAKAYSACSWEIVRVQLQVDLPAFPLSARRGPR
Protein: Histone H3-like centromeric protein CSE4 (CENP-A homolog) (CENPA homolog) (Chromosome segregation protein 4) (Q6CTI2)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P36012}. Chromosome, centromere {ECO:0000250|UniProtKB:P36012}.
Interaction partners:
- Histone H4
- KLLA0C17710p
- KLLA0F05115p
- Inner kinetochore subunit OKP1
- Histone H2A.Z
- Inner kinetochore subunit AME1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Inner kinetochore subunit MCM21
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone H2A
Sequence:
MEQSIRSIDGSRSLSNVGASLIDRESINQRALQLLQRNRRRRLLLNRSEDKARYIQPERSASSQQIHPPEHHISAHERITKARGTRYKPTDLALAEIRKYQRSTDLLISRMPFARLVKEVTDQFTTESEPLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMRKDMQLARRIRGQFI
Protein: Rho GTPase activating protein 4 (A0A8I6AIK5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAHGKLRRERGLQPEYEAQVKVMRGQLSEQLHCLELQGELRRDLLLELAEFMRRRAEVELEYSRGLDKLAERFTSRSGRLGGSSREQQSFRKEPTLLSPLHCWAMLLEHTRQQSRESATLSEVLAGPLAQRLSHIAEDVGRIVKKTKKTYHVYHLESMNAETKLREAERQEEKRSGKSALPTTTAASATTTITIETELHRKGSLKKGGRLVEKRQAKFLEHKLKCTKARNEYLLSLASVNAAVSNYYLHDILDLMDCCDTGFHLALEQALRSYTAAESRTQTSHMQGLGSLEEALEALDPPGDKAKVLEVHAMAFCPPLRFDYQPHEGDEVAEIQVEMELRDEILPRAQNIQSRLDQKTIETEEVNKTLKATLQALLEVVASEDGDILDSLQASPSTESLKSTSSDPGTRQAGRRRNQQQETETFYITKLQEYLSGRSILAKLQAKHEKLQEAIQRGNKEEQETSSWTQCTERKFHKSHHPYPGSQCTQRLFGGDLEKFIQSTGQPVPLVVKSCIRFINLNGLQHEGIFRVSGAQARILEIRDAFERGEDPLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPLDMFNELLASAELEVVGERVELVSHLLSRLPRPVLVVLRYLFTFLNHLAQYSDENMMDSYNLAVCFGPTLLPVPAGQDPVALQGRVNQLVQTLILQPAWVFPPTAMLPGPIYEKCMAPPSASCLGDGQLESLAGEPELELKTGTKAQEDDSEGVVEAVACFAYTGRTAQELTFQQGDTLRLYARASSDWWRGEHAGVRGLIPHKYITLSEGDEKQMTGSGLQAMGESLSHPESVLTLEFTNRLELGTPPEALGPSGHRRHCLVPTSPEQHVEMDKAVAQNMDSVFKELLGKAAVRQGHGLASTASPSLGTRNLKPLACSSFSKNKVFSRGPGAPVSPSVSHPQGPDSTRKPV
Protein: Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5) (Q9I8K8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P receptor is critical for cell migration and epithelial integrity during vertebrate embryogenesis. Receptor for the chemokine-like protein FAM19A5 (By similarity). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Sphingosine kinase 2.
- Sphingosine kinase 1.
- Sphingosine-1-phosphate transporter SPNS2
- G-protein alpha 12 alpha 12) alpha 12a)
- Membrane-bound transcription factor site-1 protease
- Multidrug resistance-associated protein 1
Sequence:
MTTCRLFAGFCQAVTMSKYSQYFNKTLIQVHYLTAKEMTAEELRDRIESKQSLSSLNILFVVICSIIILENLLVLIAVFRNKKFHSAMFFFIGNLAFSDLLAGSAYIANIFLSGPRTFHLTPVQWFIREGTAFIALSASVFSLLAIAIERYIAITKVKVYGSNKTCRMFLLIGACWVMSILLGGLPIIGWNCINNLDDCSAVLPLNTRYYIRFVVTIFSIILLSIVILYVRIYLIVRTSHQEATNSPAYALLKTVTIVLGVFIICWLPAFTILLLDTSCKMKQCPILNNAGIFFSFATLNSALNPLIYTLRSKDMRKEFLRVLCCWGLLNCGRPPHRCMVPLKSSSSMEHCTNKHEHQSIPIMQDCTTCV
Protein: Chromatin remodeling protein EBS (Protein EARLY BOLTING IN SHORT DAYS) (F4JL28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chromatin remodeling factor that binds to methylated histone (e.g. H3K4me2/3) to prevent their acetylation (e.g. H3K9K14Ac), likely by recruiting histone deacetylase (HDAC) complexes, and thus regulating the transcription of target genes. Negative regulator in developmental processes in a gibberellic acid- (GA-) dependent manner, such as germination, flowering induction, and flower organ specification, probably by modulating developmental gene expression. Involved in the chromatin-mediated repression of floral initiation and controls genes regulating flowering. Negatively regulates the expression of the floral integrator FT epigenetically, by preventing high levels of H3 acetylation, thus maintaining an inactive chromatin conformation at FT locus.
Subcellular location: Nucleus {ECO:0000269|PubMed:12837946}.
Interaction partners:
- Histone H3.3
- Histone H3.1
- PHD finger family protein / SWIB complex BAF60b domain-containing protein / GYF domain-containing protein
- Zinc ion binding / DNA binding protein
- PHD finger protein MALE MEIOCYTE DEATH 1
- Cysteine/Histidine-rich C1 domain family protein
- B3 domain-containing protein At5g25475
- Protein TRAUCO
- Protein RBL
- Histone H3-like centromeric protein CENH3
Sequence:
MAKTRPGVASKIKTGRKELDSYTIKGTNKVVRAGDCVLMRPSDAGKPPYVARVEKIEADARNNVKVHCRWYYRPEESLGGRRQFHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENVGAEDYYCRFEYKAATGAFTPDRVAVYCKCEMPYNPDDLMVQCEGCKDWYHPACVGMTIEEAKKLDHFVCAECSSDDDVKKSQNGFTSSPADDVKVRLSLFSHLLYRCSITYL
Protein: Biotin biosynthesis cytochrome P450 (EC 1.14.14.46) (P53554)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid.
Interaction partners:
- 8-amino-7-oxononanoate synthase 2
- L-Lysine--8-amino-7-oxononanoate transaminase
- ATP-dependent dethiobiotin synthetase BioD
- Biotin synthase
- 6-carboxyhexanoate--CoA ligase
- Polyketide synthase PksJ
- Uncharacterized protein YtbQ
- Surfactin synthase subunit 3
- Dimodular nonribosomal peptide synthase
- Polyketide synthase PksN
Sequence:
MTIASSTASSEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDARFKVRTPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTESYQPYIIETVHHLLDQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDREQLKEWAASLIQTIDFTRSRKALTEGNIMAVQAMAYFKELIQKRKRHPQQDMISMLLKGREKDKLTEEEAASTCILLAIAGHETTVNLISNSVLCLLQHPEQLLKLRENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTIRQGEQVYLLLGAANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAINTLLQRMPSLNLADFEWRYRPLFGFRALEELPVTFE
Protein: Fructose-like PTS system EIIBC component [Includes: PTS system fructose-like EIIB component (EC 2.7.1.202) (Fructose-like phosphotransferase enzyme IIB component); PTS system fructose-like EIIC component (Fructose-like permease IIC component)] (P32154)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FrvAB PTS system is involved in fructose transport.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000305|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427}.
Interaction partners:
- 1-phosphofructokinase
- PTS system fructose-like EIIA component
- ATP-dependent 6-phosphofructokinase isozyme 2
- Putative frv operon regulatory protein
- Putative aminopeptidase FrvX
- Multiphosphoryl transfer protein 2
- Multiphosphoryl transfer protein 1
- Multiphosphoryl transfer protein
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
- PTS system beta-glucoside-specific EIIBCA component
Sequence:
MESSLRIVAITNCPAGIAHTYMVAEALEQKARSLGHTIKVETQGSSGVENRLSSEEIAAADYVILATGRGLSGDDRARFAGKKVYEIAISQALKNIDQIFSELPTNSQLFAADSGVKLGKQEVQSGSVMSHLMAGVSAALPFVIGGGILVALANMLVQFGLPYTDMSKGAPSFTWVVESIGYLGFTFMIPIMGAYIASSIADKPAFAPAFLVCYLANDKALLGTQSGAGFLGAVVLGLAIGYFVFWFRKVRLGKALQPLLGSMLIPFVTLLVFGVLTYYVIGPVMSDLMGGLLHFLNTIPPSMKFAAAFLVGAMLAFDMGGPINKTAWFFCFSLLEKHIYDWYAIVGVVALMPPVAAGLATFIAPKLFTRQEKEAASSAIVVGATVATEPAIPYALAAPLPMITANTLAGGITGVLVIAFGIKRLAPGLGIFDPLIGLMSPVGSFYLVLAIGLALNISFIIVLKGLWLRRKAKAAQQELVHEH
Protein: Large ribosomal subunit protein mL66 (39S ribosomal protein S18-3, mitochondrial) (MRP-S18-3) (39S ribosomal protein S18a, mitochondrial) (MRP-S18-a) (Mrps18a) (S18mt-a) (Large ribosomal subunit protein bS18a) (Q9NVS2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein mL42
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS5m
Sequence:
MAALKALVSGCGRLLRGLLAGPAATSWSRLPARGFREVVETQEGKTTIIEGRITATPKESPNPPNPSGQCPICRWNLKHKYNYDDVLLLSQFIRPHGGMLPRKITGLCQEEHRKIEECVKMAHRAGLLPNHRPRLPEGVVPKSKPQLNRYLTRWAPGSVKPIYKKGPRWNRVRMPVGSPLLRDNVCYSRTPWKLYH
Protein: FI01422p (Serpin 43Ab) (A1Z6V5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- GH14088p
- Cyclin-dependent kinase 9
- Cyclin-dependent kinase 12
- Transcription elongation factor SPT5
- Cyclin-T
- Serpin 77Bb
- Transcription elongation factor SPT4
- Transcription elongation factor SPT6
- Serine protease inhibitor 42Dd
Sequence:
MAVIISCLLLLLATVSQSKTVGYDAAADRNLLAADLYNAVAADHLNENVVISPATIQSSMALAFVGAKGQTASELQQGLRLGPGDADAVSQRSGSYQQALTRDNNFRLANNIYINENLEFKGSFRDVAQRQFDSNIDKLDFHPPYNKRTADGINRAVATKTNGKITDILRAELLNDRTEGVIVNGVSYSAAWQKAFRLDKTEKRSFRTGSGQSVKVDTMWTLQNFNYAEVNSLDAKVVELPYQNPDFSMLLLLPNRKDGLRSLQQSLSGKNLLAEIGAMSQQKVEVLLPKFSVTFGLGLEGPFKKLGVHTMFSRDGDFGNMYRMFVSHFINAVEHKANVEVTEAGVDQPLETGLLKGLFSRSKKFEADHPFVFAIKYKDSIAFIGHIANYAYV
Protein: Peroxiredoxin-like 2A (Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes) (Protein PAMM) (Redox-regulatory protein FAM213A) (Q9BRX8)
Organism: Homo sapiens (Human)
Function: Involved in redox regulation of the cell. Acts as an antioxidant. Inhibits TNFSF11-induced NFKB1 and JUN activation and osteoclast differentiation. May affect bone resorption and help to maintain bone mass. Acts as a negative regulator of macrophage-mediated inflammation by inhibiting macrophage production of inflammatory cytokines, probably through suppression of the MAPK signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19951071}. Secreted {ECO:0000269|PubMed:26438880}. Note=Secreted from mature adipocytes but not from preadipocytes. {ECO:0000269|PubMed:26438880}.
Interaction partners:
- Heat shock protein HSP 90-beta
Sequence:
MSFLQDPSFFTMGMWSIGAGALGAAALALLLANTDVFLSKPQKAALEYLEDIDLKTLEKEPRTFKAKELWEKNGAVIMAVRRPGCFLCREEAADLSSLKSMLDQLGVPLYAVVKEHIRTEVKDFQPYFKGEIFLDEKKKFYGPQRRKMMFMGFIRLGVWYNFFRAWNGGFSGNLEGEGFILGGVFVVGSGKQGILLEHREKEFGDKVNLLSVLEAAKMIKPQTLASEKK
Protein: Complement component C6 (P13671)
Organism: Homo sapiens (Human)
Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
Subcellular location: Secreted.
Interaction partners:
- Complement C5
- Complement component C9
- Complement component C7
- Complement component C8 gamma chain
- Complement component C8 alpha chain
- Complement component C8 beta chain
- Immunoglobulin heavy variable 3-43D
- Non-selective voltage-gated ion channel VDAC1
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Sequence:
MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIETKKRVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRSEYGAALAWEKGSSGLEEKTFSEWLESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEYAAKFDPCQCAPCPNNGRPTLSGTECLCVCQSGTYGENCEKQSPDYKSNAVDGQWGCWSSWSTCDATYKRSRTRECNNPAPQRGGKRCEGEKRQEEDCTFSIMENNGQPCINDDEEMKEVDLPEIEADSGCPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQRTECIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNSWTPPISNSLTCEKDTLTKLKGHCQLGQKQSGSECICMSPEEDCSHHSEDLCVFDTDSNDYFTSPACKFLAEKCLNNQQLHFLHIGSCQDGRQLEWGLERTRLSSNSTKKESCGYDTCYDWEKCSASTSKCVCLLPPQCFKGGNQLYCVKMGSSTSEKTLNICEVGTIRCANRKMEILHPGKCLA
Protein: Transforming acidic coiled-coil containing protein (Q9XZL7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEFDDAENGLGMGFGGRGVLREINKNDGGIKLSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEDRHLMQTHILSVTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKMIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFYSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVEATEDTGADEVYEWDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEHTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNLILNSSDFDYLYTKGSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTNSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: GH14967p (Sidestep VII, isoform A) (Sidestep VII, isoform B) (Q9VH85)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Uncharacterized protein, isoform B
- Beaten path Ia, isoform B
Sequence:
MELLLLFMLALQLIESSIGSKDVPIHQIESIVGENIYLPCNVTTYDGDEPVLVLWYRDDKGTPIYSIDIRAGVSKAPKRWSDDSVFGDRAYFIFDKEPGKLSIQNTQASDSGTYRCRVDFLKAQTINSRIRLNVISPPKQVIIRDSSNVERSTVVGPYSEGDIVSLKCQVIGGYPTPTISWYRDGIEIPCELSHLAGGKIIECEITLPSLGREDLNSRLTCRALSHPRAPIVEAVVQIDMNFAPLNIRLLGAHQPLSAGRRYDLLCQSAGSRPPAVITWWQNGIRLEKTTETTSSDGNQTTSTLSISLSKSDAGKYLSCKAYNHAVPSEPLEDGWKLDIQYVPEAYVRLGTSLDPSTLREGTDVYFDCLVMAHPNVFRIEWRHNEQPLSHNISLGVIISNHSLVLQGVTRATAGNYSCVGFNAEGEGISAPFALNILYAPTCAQNQKKVYGIAKQEDAKVMCTVDANPREVEFSWTFNNSAESIDVATNHIIRSGTTSIVTYTPITELDYGTLLCLASNKIGKQRVPCVFHIIAAGRPEKVHNCTVNNISMTSLTVTCSDGFNGGLPQSFNLELLDSYTQEIKANITSTIPKFTVPGLSPGSIYRLNIYAFNTKGRSDPAIVNAAMLRMPEKQLTSEQTHNLRAELLFSPVMSLTIGLTLAVLVAVLAIILALRIPCTASSRRRQKELSNENISRDESPGPSDKSSGSKEVDDCDEKNPDVVPESIEPDEQAESIRKRQQISTIDTNRSPNRGIFVNEQQHLTAAEISLRASHGIGYCTLRSGMHAQAQSSVGEISINVTPHVYSNSISQCTLPRQSSQNVWNNYNCNITGARPTSTFHQLTFPQGRVNVGGHNPAQPLHGHAPSPSQASNSSMASSTNTLPQPHPHGRTIAMHHMNQAQCGRVCIGIASDGIHSAEQNVSDDEVTVQTPLMIKRDSTV
Protein: Arginine vasopressin-induced protein 1 (AVP-induced protein 1) (Q5T686)
Organism: Homo sapiens (Human)
Function: May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling.
Interaction partners:
Sequence:
MGTPASVVSEPPPWQAPIEARGRKQASANIFQDAELLQIQALFQRSGDQLAEERAQIIWECAGDHRVAEALKRLRRKRPPRQKPLGHSLHHCSRLRILEPHSALANPQSATETASSEQYLHSRKKSARIRRNWRKSGPTSYLHQIRH