wanglab/gogpt-training-data huggingface dataset:
Protein: Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (MuLK) (Multi-substrate lipid kinase) (Q9ESW4)
Organism: Mus musculus (Mouse)
Function: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Phosphorylates ceramide but not sphingosine. Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol. Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q53H12}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q53H12}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q53H12}. Note=Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. {ECO:0000250|UniProtKB:Q53H12}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim29
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim22
- Lysocardiolipin acyltransferase 1
- Monoglyceride lipase
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- Glycerol-3-phosphate acyltransferase 3
Sequence:
MTAFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMESTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVYAMTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPRERPPIEPEETPPRPSLYRRILRRLASFWAQPQDASSREVSPEVWKDVQLSTIELSITTRNTQLDLMSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECLQASHCTLVLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLRFFCDPRKREQMLPSTSQ
Protein: AAA-ATPase At3g28520 (EC 3.6.1.-) (Q9LH83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLEVGTIWGFTSTTMASIMFLWPMYKQFVPYQLREYLENTIQKYLDKLFRRDSNFVYIRFPEYTGEGLSKSRAYDEIGNYLSSISTARAKRLKAKESENSKSLVLCLDDDEAVVVVFQGVNVVWSSTVVDKEDKHNSKEGRYLTLTFENHHRDIITNTYIDHVLREGKEIALKNRERKLYTNNDSSSYSSWWEGLWSNVPFNHHASFETLGMDLDKKEEIKKDLIKFTKGKDYYRKVAKPWKRGYLLFGPPGTGKSTMISAIANFLEYDVYDLELTTVKDNAELKKLMLDTKGKSIVVIEDIDCSLELTEHRKKKKEEDEDKEEKKEAENLKRVSGNNESNVTLSGLLNAIDGLWSACSDEKIIIFTTNFVDNLDPALIRRGRMDYHIEMSYCRFEAFKVLAKNYLENESHDLYGEIGRLLEEVDVSPADVAENLMPKSDEDDADICFRRLVKSLEEEKKKKIEKEARKNKKKAEDNVKQEKQNKVKGMVTK
Protein: Probable oxidoreductase EphD (EC 1.-.-.-) (P9WGS3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable epoxide hydrolase EphC
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycocerosic acid synthase-like polyketide synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Possible epoxide hydrolase EphE
- Probable short-chain type dehydrogenase/reductase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MPATQQMSRLVDSPDGVRIAVYHEGNPDGPTVVLVHGFPDSHVLWDGVVPLLAERFRIVRYDNRGVGRSSVPKPISAYTMAHFADDFDAVIGELSPGEPVHVLAHDWGSVGVWEYLRRPGASDRVASFTSVSGPSQDHLVNYVYGGLRRPWRPRTFLRAISQTLRLSYMALFSVPVVAPLLLRVALSSAAVRRNMVGDIPVDQIHHSETLARDAAHSVKTYPANYFRSFSSSRRGRAIPIVDVPVQLIVNSQDPYVRPYGYDQTARWVPRLWRRDIKAGHFSPMSHPQVMAAAVHDFADLADGKQPSRALLRAQVGRPRGYFGDTLVSVTGAGSGIGRETALAFAREGAEIVISDIDEATVKDTAAEIAARGGIAYPYVLDVSDAEAVEAFAERVSAEHGVPDIVVNNAGIGQAGRFLDTPAEQFDRVLAVNLGGVVNGCRAFGQRLVERGTGGHIVNVSSMAAYAPLQSLSAYCTSKAATYMFSDCLRAELDAAGVGLTTICPGVIDTNIVATTGFHAPGTDEEKIDGRRGQIDKMFALRSYGPDKVADAIVSAVKKKKPIRPVAPEAYALYGISRVLPQALRSTARLRVI
Protein: ATP synthase subunit beta (EC 7.1.2.2) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta) (P26527)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
Interaction partners:
- ATP synthase subunit c
- ATP synthase subunit a
- ATP synthase subunit alpha
- ATP synthase subunit b
- ATP synthase subunit delta
- ATP synthase gamma chain
- ATP synthase epsilon chain
- ATP synthase subunit b'
- Large ribosomal subunit protein uL16
- Inorganic pyrophosphatase
Sequence:
MVAVKEATNVGKITQVIGPVIDAQFPSGKLPRIYNALKVQGRNSAGNEVAVTCEVQQLLGDNQVRAVAMSSTDGLVRGMDVVDTGAPISVPVGTGTLGRIFNVLGEPVDNKGPVPAGETFPIHRPAPKLVDLETKPQVFETGIKVIDLLTPYRQGGKIGLFGGAGVGKTVIMMELINNIAIQHGGVSVFGGVGERTREGNDLYNEMIESNVINADKPEESKIALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTDVGDLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDGTTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGSEHYDTAREVQSTLQRYKELQDIIAILGLDELSEEDRLTVDRARKIERFLSQPFFVAEVFTGAPGKYVSLADTIKGFKAILAGELDDLPEQAFYLVGDIEEAKAKGAKLKEG
Protein: HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1) (Q7TSE9)
Organism: Rattus norvegicus (Rat)
Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:19913549}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus membrane {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle {ECO:0000269|PubMed:15159385}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000269|PubMed:19913549}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited, and in response to cellular stress caused by arsenite (in vitro). {ECO:0000250|UniProtKB:O00165}.
Interaction partners:
Sequence:
MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDEDDEEEEDSGAWGRESYAFDGFHPTEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGVRLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESSKPAPDWGSQGPFHRLDDTWPVSPHSRAREDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEEHRTVVDSEGRRETTVTHQEAHDSSRSDPDPPRSSALDDPFSILDLLLGRWFRSR
Protein: Disintegrin and metalloproteinase domain-containing protein 2 (ADAM 2) (Fertilin subunit beta) (PH-30) (PH30) (PH30-beta) (Q63202)
Organism: Rattus norvegicus (Rat)
Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 1
- Hyaluronidase PH-20
- Protamine-2
Sequence:
MWLLLLLLSGLSRLGGLSEPQTEGTREKLHVQVTVPEKIRSITSEGYETQVTYSLKIEGKTYILNLMQKAFLPPNFRVYSYDSTGIMRPLEQKFQNICYFQGYIEGYPNSMVIVSTCTGLRGVLQFGNVSYGIEPLESSSGFEHVIYQVEPKKGDTLLYAEKDMDLRDPQYKIRSIKPQRTVSHYLEIHIVVEKQMFEHIGADTAVVTQKIFQLIGLTNAIFAPFNLTVILSSLEFWMDENKISTTGDANKLLYRFLKWKQSYLVLRPHDMAFLLVYRDTTDYVGATYQGKMCDKNYAGGVALHPKAVTLESLAIILVQLLSLSMGVAYDDVNTCQCGVPICVMNPEALHSSGVRSFSNCSMEDFSKFIVSQSSHCLQNQPHLQPSYKMAVCGNGELEEGEVCDCGQEGCDDKPPPCCNPTTCQLSEGSTCSTGSCCDASCNLKAKGELCRPANQECDVTEYCNGTSEVCEEDFFVQDGHPCAEQKWICINGTCQSGAQQCRDLFGTDADYGTKECYSELNSKSDISGSCGITPTGYKDCAPNDRMCGKLICIYQSEDILKMRSAIVIYANISGQICISLEYPPGHKESKKMCVRDGTVCGSGKVCLNQECVEDTFLNYDCTPEKCNHHGVCNNKKHCHCEPTYLPPDCKNTEDTWPGGSVDSGNQQRAESIPARSYVASAYRSKSARWPFFLIIPFYVVILVLIGMLVKVYSQRKKWRMDDFSSEEQFESESESKD
Protein: D-methionine-binding lipoprotein MetQ (P28635)
Organism: Escherichia coli (strain K12)
Function: This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- D-methionine transport system permease protein MetI
- Methionine import ATP-binding protein MetN
- Vitamin B12 import system permease protein BtuC
- Vitamin B12 import ATP-binding protein BtuD
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Lipoprotein 28
- ATP-dependent lipid A-core flippase
- Ribose import permease protein RbsC
- Lipopolysaccharide export system ATP-binding protein LptB
- Iron
Sequence:
MAFKFKTFAAVGALIGSLALVGCGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKDKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYLDQQLKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDVVENPKNLKIVELEAPQLPRSLDDAQIALAVINTTYASQIGLTPAKDGIFVEDKESPYVNLIVTREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAVKGW
Protein: Protocadherin gamma B2 (Q8K4A9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
IASQSAKTEFNFLNVTPEVAPQDLLCGDDSWVPGTLGDTDVPFVSDSISKQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Nucleus export protein BRL1 (BRR6-like protein 1) (P38770)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mRNA and protein export from nucleus.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:15882446}; Multi-pass membrane protein {ECO:0000269|PubMed:15882446}.
Interaction partners:
- Nucleus export protein BRR6
- Guanine nucleotide exchange factor SRM1
Sequence:
MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRNTLDFSAAKADEEEDDRMEIDEVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQKQEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAATKVEGVVPLPPSANQDDNESSNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNTHNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQLFLNAITTVVIFSFILSFIIALQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPALGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFIDPLNWKTLFVIFCGVITWCFSSNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ
Protein: DnaJ protein ERDJ2 (Chaperone protein dnaJ C43) (OsDjC43) (Endoplasmic reticulum dnaJ domain-containing protein 2) (OsERdj2) (Q7XVN7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May be required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24153418}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Translocation protein SEC62
- Os05g0163250 protein
- Os06g0167000 protein
- SNU114 homolog
- Os10g0498600 protein
- Os01g0263600 protein
- DEAD-box ATP-dependent RNA helicase 21
- DEAD-box ATP-dependent RNA helicase 22
- Os06g0653900 protein
- Protein transport protein Sec61 subunit gamma
Sequence:
MAAAEENSSLFLIFILTMIALPLVPYTIMRLCRAANVKAKTIHCRCSGCHRSGKYRKSIYKRISNFSTCSNLTILLLWIVMIFLVYYIKHVSREVQVFEPYSILGLEPGASESDIKKSYRRLSIQYHPDKNPDPEAHKYFVEFISKAYQALTDPVSRENYEKYGHPDGRQGMQMGIALPKFLLNMDGASGGIMLLGIVGLCILLPLMIAVIYLSRSSKYTGNYVMHQTLSTYYYFMKPSLAPSKVMDVFIKAAEYMEMPVRRSDDEPLQKLFVAVRSELNLDLKNIRTEQAKFWKQHPSLVKMELLIQAHLTGESFALTPALLKDYRHMLELAPRLLDELVKIALLPRSPHGFGWLRPAIGVIELSQNIIQAVPLSARKASGGNSEGIAPFLQLPHFTETVVKKIARKKIRSFQEFCDMPVEERATLLTQVAGLSDEGAQDVELVLEMIPSIEVDIKCETEGEEGIQEGDVVTMYAWVSLHRRNGLTAALPHAPSFPFHKEENFWLLLADAASNEVWLSQKVSFMDETTAITAASKAIQETQEALGASAKEIGIAIREAVDRVKKGSRLVMGKFQAPAEGTHNLTSFCLCDAWIGCDTKTSLKLKVLKRSRAGTRGHVAEEGPVAEDGIEEEEEEEEEEYDDYESEYSDDEEDEKSKGKGKVANGVAHQKANSDIDSGSDD
Protein: BZIP domain-containing protein (G8B7A0)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- BZIP domain-containing protein
- Kinetochore protein SPC25
- Uncharacterized protein
- Kinetochore protein NDC80
- Mtf2-like C-terminal domain-containing protein
- Small ribosomal subunit protein mS37
- Mitogen-activated protein kinase
- Uncharacterized protein
- Mitogen-activated protein kinase
- Protein kinase domain-containing protein
Sequence:
MDVDTTTATTTPLDIVVVDDVNATATTSLDSLKTSTSTLPPRKRAKTQEEKEQRKIERILRNRRAAHASREKKRRHVEYLEVYVVKLEENLHKIATGYQQLLEKLPTEEDQVSIEDLGLENLSELKSQIHSNLNGSRRGGNNSSRKGSQVEEEEEEDHDEDDVEGESDQSHEHDSTPVVEVKVEKLPQSPPSKKRKYSPQMETTTTTPPTSTRSSSITSSPAHAKLEAGEEEEEEEQQQQQQDCNNKNYTHSLQPPQAMNEKTFYNYLSPISLHSSASSPMDFTLNSKSDFNDFTFEEVKQQLQQQTQEQESMGNFSQNTLKDVPTQSQPSSSTEVSTQESNLSIYESGQNSAVILSIEEEKQQPQHTLVEILEKENKIRSAVSV
Protein: G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5) (P34947)
Organism: Homo sapiens (Human)
Function: Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro).
Subcellular location: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Note=Predominantly localized at the plasma membrane; targeted to the cell surface through the interaction with phospholipids. Nucleus localization is regulated in a GPCR and Ca(2+)/calmodulin-dependent fashion.
Interaction partners:
- ARF GTPase-activating protein GIT1
- Beta-arrestin-1
- Beta-arrestin-2
- Calmodulin-1
- Mu-type opioid receptor
- ARF GTPase-activating protein GIT2
- Calmodulin-1
- Beta-2 adrenergic receptor
- Rhodopsin
- S-arrestin
Sequence:
MELENIVANTVLLKAREGGGGKRKGKSKKWKEILKFPHISQCEDLRRTIDRDYCSLCDKQPIGRLLFRQFCETRPGLECYIQFLDSVAEYEVTPDEKLGEKGKEIMTKYLTPKSPVFIAQVGQDLVSQTEEKLLQKPCKELFSACAQSVHEYLRGEPFHEYLDSMFFDRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGDLIRGRVGTVGYMAPEVLNNQRYGLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSHKFSEEAKSICKMLLTKDAKQRLGCQEEGAAEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDHTDDDFYSKFSTGSVSIPWQNEMIETECFKELNVFGPNGTLPPDLNRNHPPEPPKKGLLQRLFKRQHQNNSKSSPSSKTSFNHHINSNHVSSNSTGSS
Protein: COP9 signalosome complex subunit 7 (Dch7) (Signalosome subunit 7) (Q9V4S8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in oogenesis and embryogenesis and is required for proper photoreceptor R cell differentiation and promote lamina glial cell migration or axon targeting. It also promotes Ubl-dependent degradation of cyclin E (CycE) during early oogenesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus {ECO:0000305|PubMed:10531038}.
Interaction partners:
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1b
- COP9 signalosome subunit 1a
- Ubiquitin-like protein NEDD8
- Cullin-4A
Sequence:
MTQDMLLGNEEPSKSKETFLEKFCVLAKSSTGAALLDVIRQALEAPNVFVFGELLAEPSVLQLKDGPDSKHFETLNLFAYGTYKEYRAQPEKFIELTPAMQKKLQHLTIVSLAIKAKSIPYALLLSELEIDNVRHLEDIIIEAIYADIIHGKLFQNTRILEVDYAQGRDIPPGYTGQIVETLQAWVNSCDSVSNCIEMQIKYANAEKSKRLINKERVEQDLINLKKVLKSQTSDSDESMQIDTHGPGTSGGLGQSELRKKPSKLRNPRSAAVGLKFSK
Protein: Alpha-1,6-mannosyltransferase (Q59UR2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mannan polymerase complex subunit MNN9
- Anp1p
- Alpha-1,6-mannosyltransferase
- Alpha-1,6-mannosyltransferase
- Van1p
- Alpha-1,2-mannosyltransferase MNN24
- Uncharacterized protein
- tRNA
- Alpha-1,2-mannosyltransferase MNN21
- Initiation-specific alpha-1,6-mannosyltransferase
Sequence:
MSELPTDLEDTYTKTFKPNKKNAFEFSAVTDFITKYKKIVLFIVTFVCLSLFTNVPYIPHFRQAPPKVVIILAANEGGGVLKWKSPQEWSVERSSIANKKNYAKVHGYGLTIKDMTIKKRYSHEWRESWEKVDILKQTMRQFPDTEWFWWLDLHTYIMEPQISLEKHFLNNLYNATYRTLDTFNPLNLPTDLPYVDYNQPIDMVITQDCGGFNLGSFLIRRSEWSEMLLDIWWDPAMYEQMHMQWEHKEQDALETLYSTQAWIRERIAFLPLRQINAFPPGACSDQADDPQYFFQNHDFVVNMAGCEWGRDCWGEMEHYKALSKKLHKRWWKFWE
Protein: Tetra-spanning protein 1 (Q9Y7Z5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Note=Enriched at the cell equator during mitosis.
Interaction partners:
- Reticulon-like protein 1
- Protein sey1
- Uncharacterized protein ely5
- Triacylglycerol lipase ptl3
Sequence:
MEPKQRVVKPLKERVLPVVKNTQFVWFSGQVIVLISSVLYALQAIPFRSAPPFLFKSAAFGAIVAYAIVLYKTYSPNLTSRASWNKHFFARLMLDDNVQYFILALSMLIDRPILFSLAPYAIYATFHISTYLRSVLLPAIYPNISDAKTASYASRVSNLLNQYTRSQFQPAMQLVASLETFLLFRLFFGVFLRKNSISRLVGYIFFLRMRYTNSHFTRASIKAVSLRMDRLVADNRVPPVIKNAWHTFKTYVSKFGASPVGTAQSRPTASSSTTAPSST
Protein: E3 ubiquitin-protein ligase znrf3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase znrf3) (Zinc/RING finger protein 3) (A5WWA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components. Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ULT6}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- R-spondin-1
- R-spondin-2
- Leucine-rich repeat-containing G-protein coupled receptor 4
- R-spondin-3
- Frizzled-5
- Frizzled class receptor 1
- Frizzled class receptor 2
- Frizzled-4
- Frizzled class receptor 7a
- Frizzled class receptor 10
Sequence:
MMILPRTGFGRGADSVVLVLLWVLGSVLAKDTAFVEVVLFESSPNGDYTTYTTGLQGRFSRAGATISAEGEIVQMHPLGLCNNNDEEDLYEYGWVGVVKLEQPELDPSCLTVLGKAKRAVQRGATAVIFDVSENPDAIDQLNQVSEDPLKRPVVYVKGADAVKLMNIVNKQKVARARIQHRPPRVRPTEYFDMGIFLAFFVVVSLVCLILLIKIKLKQRRSQSSMNRMAIQALEKMETCKFKAKFKGQREASCGASDSVSSSSTSDCAICLEKYIDGEELRVIPCAHRFHKKCVDPWLLQHHTCPHCRHNIIDQKKGNPGAVCLDPGNPVHGRQQRVVLPVHYPGRVHRAGQVTAYPTRTSMDPHGNPITVLTVDQHPEQGLYPSQSSFIRGYPALHLDHTLNPHHCGLEHRGPAYPQTHTFKRPKFHGRNFSRAACFSQYETMYQHYYFQGLTFPQPEGQPSNGLHKGHNRPFQPGLLYPTVVHMAPASSSRLGDSGSTSGLSCYHGHRSVCSGYLADCPGSDSSSSSGQCHCSSSDSMLDCTEVSNQGVYGSCSTFRSSLSSDYDPYVYRSKSPCRGSAGEAGAVFSAAPPADDTSAPVSGMIDCLQPPGGACYSSGDQLSNCSLEPNCSNHSSVETRELTSTTSAGPLEGNVAERSHNSVKPCGEQGVACNCCFEVPKLNLERKGKEGEDRGHCRWATEAQAVASSQNFYSVSTEQLPSPDHVSYDGLPCCFYTEMTVHRGGANHYAEDCSVNIQYAQTDSDGCMGQGCCELAQRIPIIPEDTDCELGLGPEPQTSLLSSRLTTEREERTSSEDTCDLFFTSGQCRGQVYQQPQDEEARALFSSKCNAVSETQGSSTSSFDGSGL
Protein: Uncharacterized protein Rv3127 (P9WL07)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1738
- Universal stress protein Rv3134c
- Universal stress protein Rv1996
- Probable diacyglycerol O-acyltransferase tgs1
- Putative NAD
- Alpha-crystallin
- Probable membrane protein Rv1733c
- Uncharacterized protein Rv1813c
- Dormancy associated translation inhibitor
- Uncharacterized protein Rv0080
Sequence:
MLKNAVLLACRAPSVHNSQPWRWVAESGSEHTTVHLFVNRHRTVPATDHSGRQAIISCGAVLDHLRIAMTAAHWQANITRFPQPNQPDQLATVEFSPIDHVTAGQRNRAQAILQRRTDRLPFDSPMYWHLFEPALRDAVDKDVAMLDVVSDDQRTRLVVASQLSEVLRRDDPYYHAELEWWTSPFVLAHGVPPDTLASDAERLRVDLGRDFPVRSYQNRRAELADDRSKVLVLSTPSDTRADALRCGEVLSTILLECTMAGMATCTLTHLIESSDSRDIVRGLTRQRGEPQALIRVGIAPPLAAVPAPTPRRPLDSVLQIRQTPEKGRNASDRNARETGWFSPP
Protein: Arginine repressor (P9WPY9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Regulates arginine biosynthesis genes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Arginine biosynthesis bifunctional protein ArgJ
- Acetylglutamate kinase
- Acetylornithine aminotransferase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Argininosuccinate synthase
- Ornithine carbamoyltransferase
- Argininosuccinate lyase
- LexA repressor
- Heat-inducible transcription repressor HrcA
Sequence:
MSRAKAAPVAGPEVAANRAGRQARIVAILSSAQVRSQNELAALLAAEGIEVTQATLSRDLEELGAVKLRGADGGTGIYVVPEDGSPVRGVSGGTDRMARLLGELLVSTDDSGNLAVLRTPPGAAHYLASAIDRAALPQVVGTIAGDDTILVVAREPTTGAQLAGMFENLR
Protein: Phosphoprotein (Protein P) (Q9IK91)
Organism: Nipah virus
Function: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W.
Subcellular location: Virion. Host cytoplasm.
Interaction partners:
Sequence:
MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGTDAKYPSAGTENVPGSKSGATRHVRGSPPYQEGKSVNAENVQLNASTAVKETDKSEVNPVDDNDSLDDKYIMPSDDFSNTFFPHDTDRLNYHADHLGDYDLETLCEESVLMGVINSIKLINLDMRLNHIEEQVKEIPKIINKLESIDRVLAKTNTALSTIEGHLVSMMIMIPGKGKGERKGKNNPELKPVIGRDILEQQSLFSFDNVKNFRDGSLTNEPYGAAVQLREDLILPELNFEETNASQFVPMADDSSRDVIKTLIRTHIKDRELRSELIGYLNKAENDEEIQEIANTVNDIIDGNI