wanglab/gogpt-training-data huggingface dataset:
Protein: Cobalt transport protein CbiN (Energy-coupling factor transporter probable substrate-capture protein CbiN) (ECF transporter S component CbiN) (O68104)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. A Cbi(MN) fusion protein has about 70% import capacity, but the holo-Cbi(MN)QO complex cannot be isolated, suggesting CbiN may destabilize it.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cobalt import ATP-binding protein CbiO
- Cobalt transport protein CbiQ
- Cobalt transport protein CbiM
- Fused nickel transport protein NikMN
- Nickel transport protein NikQ
- Nickel import ATP-binding protein NikO
- DUF4198 domain-containing protein
- Precorrin-6Y C5,15-methyltransferase
- Cobalamin biosynthesis protein CbiG
Sequence:
MSSKRTLWLLAGTVALVVVPLLMGGEFGGADGQAAELIEATVPGFAPWADPLWEPPSGEVESLFFALQAALGAFVVGLVIGRRQGAAKTREQNAPAPRSFPAE
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (Q4Q833)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03004, ECO:0000256|PIRNR:PIRNR016255}.
Interaction partners:
- RRM domain-containing protein
- Uncharacterized protein
- Putative eukaryotic translation initiation factor 3 subunit 8
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Putative translation initiation factor
- CSN8/PSMD8/EIF3K domain-containing protein
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit L
- Putative elongation initiation factor 2 alpha subunit
- Translation initiation factor-like protein
Sequence:
MDMLTKLLPYMDKHLALGLLNHYAQSGEDVQDAMMKLIETTGLNADGSIKAETEEMMAKATAAAQPALKEFFDESEDDHSTYQFKLTETEIGERRTQGELSHEFLSEKKGITAAVMNALYKLAYLYYDTGAYGDASELLTLCQCVSGYDNIRSDTILWGKLMSDIGAVNWQSAMRIAEEIRRVHNASEEDLFGAPNTTTVRARVWLLHWVLFPFFKGGLQYSLQLLYFIFDHRHDQTYRKAVETVCPHYLRYICAAVLLHRTRYSNFVSAAELVESIYEYSDPLTQLVSLIQKASFEDAIALLPEVRRMIKEDYFLADYEDELIENAKRMIFSKYMSLHSVVSIPYVAEQLDMSKADAEVWLVNLISESVKHRAKIDSVNEQLNVEPQTRSLESLIYDKLDTVMR
Protein: Sorting nexin-11 (Q9Y5W9)
Organism: Homo sapiens (Human)
Function: Phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26818531}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome {ECO:0000269|PubMed:23615901}. Cytoplasm {ECO:0000269|PubMed:26818531}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
Sequence:
MGFWCRMSENQEQEEVITVRVQDPRVQNEGSWNSYVDYKIFLHTNSKAFTAKTSCVRRRYREFVWLRKQLQRNAGLVPVPELPGKSTFFGTSDEFIEKRRQGLQHFLEKVLQSVVLLSDSQLHLFLQSQLSVPEIEACVQGRSTMTVSDAILRYAMSNCGWAQEERQSSSHLAKGDQPKSCCFLPRSGRRSSPSPPPSEEKDHLEVWAPVVDSEVPSLESPTLPPLSSPLCCDFGRPKEGTSTLQSVRRAVGGDHAVPLDPGQLETVLEK
Protein: LD29423p (Q95RH4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVPAAAAVAAAPMGGKTTTRQLDENGNALGDGFGGSAASGSSGASGASAAASSSNGNGNANQFTALITPTVGSSVPTSTVAHRQNSVSTLLSTGTNTTTTAMAAAAVAASYSQLQQAPVGGAAGTVSGIGIGMQQPTKQKTKKKSQQERNTTTVDVESVAGYRGNDPVEQLVKYIENDVNGGGNSAAGQRKKERKKQNKLKKSNSLEELRTCSKMEVDDLKRQSATTEMMRHKKGTNNASSGGSSSTASGSSNSGKHNSASVADINKNCNKEQQQQSTPTVQVRNSNNPGTQQRKGERRSWGTEELQYLGDHQEISAAWSELETVGQKELPLALPALARMSELDALNTVLSETAEFHVVTKKKKPKKQRAVTMDDAAVAAAAVTGGNLQRMQQITKSASSNIMSQRMHYYTPYNSNNGGGSVNYKQQQQQSQQYQEHYQAPQGQHHHHHHHHHHHHHHHSGSAVSNQVDSSRRKSTSSMPPSEKSDSSDLDSVHSLPIQTGKKKSLGGGNNKQRGAPSASQRQAKQNNNAAAPISYADIARNKQEALNNATASDTELELGDKMQIKSGGKSKSRPDFPELPGAVTAVAASGGAANQATVVSSQNTPPSSSSSISYSQSLNATPPSSSSDAESTNSPELLAQVQIPAYSMITPTLTASMISSVSSSVASTSSTSCSPPALQKSKSVEHDTSYSCNSSNLDQQYPALEKTVKRHSTNNVSVAVAASTSASASSSLYNFAAAAKQQLTENTHSAVSPPAAVTTTSTAVAASAPAPTTVTVPAAVTVPCYSSSSTHGSTQTSTSTASSAIAALPSGKAKAKPKELSPSSSCSKKPTKPSQDVPSISLSISTTPRATTSTSTTTTQKTTAATQTEGAKKLIGGIHKLPSSSCIAKGAGAVLEATAGRRAVIILNDDREAGRSNNEFIFGDFNEDELKLFDDNLDDEEEGQHKQSSNKKQQTEGESDVTQDDTEDVDQDLDKELECLGRRPEKKQERQQDISASSDQHLNDSGAASDAVNSSASLDMLSISAEAAQSSPNAGATATSSSVASPINSSTPSGASSASASTSTSSSSVSISSSSGGNGAACLASVSGMLGGVANQSGDSGIYAAANTSIKEHVNTFLSKASSSEETLPSPNSISMQQLETCNDIEAAIIAAARAAAAARSTSCSRSNSQEQDALQPQVKTKATPNPEAKMVLPVFVTYNNNNNDDDDDEEDDESLQELSFMADLKADAATEDIAMQPPPPSCPAMMTNTELIVDYIAKTWNAIANSKYVTYYNEQEQEQET
Protein: CTP pyrophosphohydrolase (EC 3.6.1.65) (P77788)
Organism: Escherichia coli (strain K12)
Function: Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP.
Interaction partners:
Sequence:
MKMIEVVAAIIERDGKILLAQRPAQSDQAGLWEFAGGKVEPDESQRQALVRELREELGIEATVGEYVASHQREVSGRIIHLHAWHVPDFHGTLQAHEHQALVWCSPEEALQYPLAPADIPLLEAFMALRAARPAD
Protein: Zinc finger MYND domain-containing protein 10 (Q6AXZ5)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in axonemal structure organization and motility. Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (By similarity). May act by indirectly regulating transcription of dynein proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23891469}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:23891469}. Apical cell membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q5FWU8}.
Interaction partners:
- Leucine-rich repeat-containing protein 6
- Dynein axonemal assembly factor 5
- Unc-79 homolog, NALCN channel complex subunit
- Outer dynein arm-docking complex subunit 2
- Sperm-associated antigen 1
- Radial spoke head 1 homolog
- Dynein axonemal intermediate chain 2
- Dynein axonemal intermediate chain 1
- Axonemal dynein light intermediate polypeptide 1
- Junctional cadherin complex regulator
Sequence:
MGDLELLLPGEAEVLVQGLHSFQLREMGSEGWSKQHENLEKLNMQAILDATVSQAEPIQELLVTHGKIPTLVEELIAVEMWKQKVFPVLCRLEDFKPQNTFPIYMVVHHEASIINLLETVFFHKEVCESADDTVLDLVDYCHRKLILLVARKGGGDLSEEERFQDSTPMQELQKQAEMMEFEISLKALSVLRYITDCMDSLSLSTLNRMLTTHNLPCLLVELLEHSPWSRREGGKLQHFESGRWQTVAPSEHQKLNKLDGQVWIALYNLLLSPEARTRYCLTNFAKGQLLKLQAFLTDTLLDQLPNLADLKSFLAHLALVETQPPKKDLVLEQIPEIWDRLERENKGKWQAIAKHQLQHVFSLSEKDLRQQAQRWAETYRLDVLEAVAPERPRCAYCSAEASKRCSRCQKVWYCCRECQVKHWEKHGKTCVLAAQGDRAK
Protein: 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory complex subunit p42B) (26S proteasome regulatory subunit Rpn6) (Q7KLV9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly (By similarity). May act as linker between 19S regulatory subunit and the 20S proteasome core.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 13
- Regulatory particle triple-A ATPase 4
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 14
Sequence:
MAGATLFERAQALSSVNREEQDSSLLNKLVRDQEGAENDEERIRIKEQGILQQGELYKQEGKAKELADLIKVTRPFLSSISKAKAAKLVRSLVDMFLDMDAGTGIEVQLCKDCIEWAKQEKRTFLRQSLEARLIALYFDTALYTEALALGAQLLRELKKLDDKNLLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKVQGALDLQSGILHAADERDFKTAFSYFYEAFEGFDSVDSVKALTSLKYMLLCKIMLGQSDDVNQLVSGKLAITYSGRDIDAMKSVAEASHKRSLADFQAALKEYKKELAEDVIVQAHLGTLYDTMLEQNLCRIIEPYSRVQVAHVAESIQLPMPQVEKKLSQMILDKKFSGILDQGEGVLIVFEETPVDKTYERVLETIQSMGKVVDTLYQKAKKLS
Protein: Calcineurin-like phosphoesterase domain-containing protein (O69651)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAAVLPTLIRTGAVALGSAIAGIGYAALVERNAFVLREVTMPVLTPGSTPLRVLHISDLHMLPNQHRKQAWLRELASWEPDLVVNTGDNLAHPKAVPAVVQTLSDLLSRPGVFVFGSNDYFGPRLKNPMNYLTSPDHRVRGAALPWQDLRAAFTERGWLDLTHTRREFEVAGLHIAAAGVDDPHIDRDRYDTIAGPASPAANLRLGLTHSPEPRVLDRFAADGYQLVLAGHTHGGQLCLPLYGALVTNCGLDRSRAKGASHWGANMRLHVSAGIGTSPFAPVRFCCRPEATLLTLIATPMGGRDSSSNLGRSQPTVSVR
Protein: Krueppel-like factor 3 (Basic krueppel-like factor) (CACCC-box-binding protein BKLF) (TEF-2) (Q60980)
Organism: Mus musculus (Mouse)
Function: Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- Four and a half LIM domains protein 3
Sequence:
MLMFDPVPVKQEAMDPVSVSFPSNYIESMKPNKYGVIYSTPLPDKFFQTPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVMAAALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDNSNSGMPVPVIESYEKPLLQKKIKIEPGIEPQRTDYYPEEMSPPLMNPVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
Protein: Dynein regulatory complex protein 10 (IQ domain-containing protein D) (F1RKB1)
Organism: Sus scrofa (Pig)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8J0N6}.
Interaction partners:
Sequence:
MALDILAVAPLYQGPDINKIRLMAETTKKSTTPPKPLTPSRTKLTTIETKRIMSVLDETIHKVELVTLLSNVASSSQSLEGMLGEDIMKAVREHVDLCQTLLDHVNYLQEEEQRLQEEEGFEDEPWFRDLVFSIELQKSRLPPLRQQIRESTKNVLRLLLRNPQAASLLQVQSLGRSEEAQSFIDSLVELRGFLFEKLLTSPMEARDKTQFIQDITRRNRRNQEIIDTLENELAACMRNRDAEVEKENFVVQELKNHLHQVLKFSENSLLRTKQEAEKQQKADFRASQARVAKIQQEILLLRSQFHNLVMENREAEQALRKKKYKVETEIENWIQKYDLEMSEKQDEYEELDIIHKEEKLQLEELKQRHSVLVEEFSQIQAEREIKAKERLEAEQEMVRMVRAATLIQALWKGYLVRSMLRSKKKKRNKGKVKDKEKGKGKEKGKGKGKEKGKGKEKGKGKKGKGKK
Protein: Elongation factor Tu (A1Z9E3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
- 40S ribosomal protein S15
- Small ribosomal subunit protein uS17
Sequence:
MSHAFAAAVCRSTASMSLALRCSRRAMSSARMLRMAGATATSTACKDWQRNGLLAAPRTGNMQQYLREYANEKKVFERTKPHCNVGTIGHVDHGKTTLTAAITKVLADKQLAESKKYNEIDNAPEEKARGITINVAHVEYQTETRHYGHTDCPGHADYIKNMITGTAQMDGAILVVAATDGAMPQTREHMLLAKQIGIDHIVVFINKVDAADEEMVDLVEMEIRELLTEMGYDGDKIPVVKGSALCALEDKSPEIGKEAILKLLQEVDSFIPTPVRELDKPFLLPVENVYSIPGRGTVVTGRLERGVVKKGMECEFVGYNKVLKSTVTGVEMFHQILEEAQAGDQLGALVRGVKRDDIKRGMVMCKPGSVKALDQLEAQVYILSKDEGGRTKPFMSFIQLQMFSRTWDCAVQVQIPDKEMVMPGEDTKLILRLIRPMVLEQGQRFTLRDGNLTLGTGVVTSTLPPLTESQRSELTEGKKAREKKVAAKK
Protein: Transmembrane 9 superfamily member 7 (Endomembrane protein 5) (Transmembrane nine protein 7) (AtTMN7) (Q9LIC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role as effector of cellular copper homeostasis.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:P32802}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q940G0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative pentatricopeptide repeat-containing protein At3g16890, mitochondrial
- Pentatricopeptide repeat-containing protein At1g06140
- Pentatricopeptide repeat-containing protein At1g74900, mitochondrial
- Pentatricopeptide repeat-containing protein At1g51965
- Pentatricopeptide repeat-containing protein At2g44880
- Pentatricopeptide repeat-containing protein At1g62260
- Pentatricopeptide repeat-containing protein At4g14850
- RNA helicase
- NADH dehydrogenase subunit 2.
- Pentatricopeptide repeat-containing protein At4g14050, mitochondrial
Sequence:
MKKTKGSSFRFYATLLLSFLSFSLSRAFYLPGVAPRDFQKGDPLYVKVNKLSSTKTQLPYDYYYLNYCKPPKILNNAENLGEVLRGDRIENSVYTFQMLEDQPCKVGCRVKLNADSTKNFKEKIDDEYRANMILDNLPVAVLRQRRDGSQSTTYEHGFRVGFKGSYEGSKEEKYFIHNHLSFRVMYHRDQESDSARIVGFEVTPNSILHEYKEWDEKNPQLTTCNKDTKNLIQGNTVPQEVEQGKEIVFTYDVSFKESEIKWASRWDTYLLMNDDQIHWFSIINSLMIVLFLSGMVAMIMMRTLYKDISNYNQLETQDEAQEETGWKLVHGDVFRPPVNSGLLCVYVGTGVQIFGMSLVTMMFALLGFLSPSNRGGLMTAMVLLWVFMGIFAGYSSSRLHKMFKGNKWKRMTLKTAFMFPGILFAIFFVLNALIWGEQSSGAIPFGTMFALFCLWFGISVPLVFVGSYLGYKKPAIEDPVKTNKIPRQVPEQPWYMKPVFSILIGGILPFGAVFIELFFILTSIWLNQFYYIFGFLFIVFLILIVTCAEITVVLCYFQLCSEDYNWWWRAYLTAGSSAFYLFLYSIFYFFTKLEITKLVSGMLYFGYMIIISYAFFVLTGTIGFYACFWFVRKIYSSVKID
Protein: Uncharacterized protein (Q9Z107)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
GNPGQQAQPPITEEPGANLDQPVTMIFMGYQNIEDEEETKKVLGYDETIKAELVLIDEDDEKSLREKTVTDVSTIDGNAAELVSGRPLSDTTEPSSPEGKEESLATDPAPASGWSTVLLQGDELTADPIGTNADMAIQ
Protein: Phosphotriesterase, putative (Q9RVU2)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Interaction partners:
- Dihydroorotase
- Triosephosphate isomerase
Sequence:
MTAQTVTGAVAAAQLGATLPHEHVIFGYPGYAGDVTLGPFDHAAALASCTETARALLARGIQTVVDATPNDCGRNPAFLREVSEATGLQILCATGFYYEGEGATTYFKFRASLGDAESEIYEMMRTEVTEGIAGTGIRAGVIKLASSRDAITPYEQLFFRAAARVQRETGVPIITHTQEGQQGPQQAELLTSLGADPARIMIGHMDGNTDPAYHRETLRHGVSIAFDRIGLQGMVGTPTDAERLSVLTTLLGEGYADRLLLSHDSIWHWLGRPPAIPEAALPAVKDWHPLHISDDILPDLRRRGITEEQVGQMTVGNPARLFG
Protein: Beta-peptidyl aminopeptidase BapA (EC 3.4.11.25) [Cleaved into: Beta-peptidyl aminopeptidase BapA alpha subunit; Beta-peptidyl aminopeptidase BapA beta subunit] (Q52VH2)
Organism: Sphingosinicella xenopeptidilytica
Function: Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.
Subcellular location: Periplasm {ECO:0000303|PubMed:16109932}.
Interaction partners:
Sequence:
MTSTQRLWSGALPLLTALIVSIAATASLAGPRARDLGVPFEGTPGALNAITDVAGVEVGHTTVISGDGAMVIGKGPYRTGVTIIHPLGKTSLDGVAAGRAVINGTGEWTGMHLVDEVGQFLGPIALTGTGNVGLVHQSMMDWSVGKVPEEALFSRLLPVVAETLDNRLNDVFGHGLTRDHVFAALDGAKGGPVAEGNVGGGTGMIAYTFKGGIGTSSRVVSAGDTRYTVGVLVQANHGDRNDLRIAGVQIGKEIKGAWPEVNGIVAAGPDAGKPQDKNSLLIVIATDAPLMPHQLERMARRAALGVGRNGSTAGALSGEFALAFSTSHVIPLGGKPRLPAIINDTDSETMNALFRGVVQATEEALVNQLVASETMTGANNAKVYGIPHDQLARIMKARFPRR
Protein: Rho GTPase-activating protein 17 (Neuron-associated developmentally-regulated protein) (Nadrin) (Rho-type GTPase-activating protein 17) (Q99N37)
Organism: Rattus norvegicus (Rat)
Function: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere (By similarity). Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1.
Subcellular location: Membrane {ECO:0000269|PubMed:10967100}; Peripheral membrane protein {ECO:0000269|PubMed:10967100}. Cytoplasm {ECO:0000269|PubMed:10967100}. Cell junction, tight junction {ECO:0000250}. Note=Associates with membranes and concentrates at sites of cell-cell contact. {ECO:0000250}.
Interaction partners:
- Angiomotin
- Cell division control protein 42 homolog
- Angiomotin-like protein 2
- Ras-related C3 botulinum toxin substrate 1
- InaD-like protein
- Cdc42-interacting protein 4
Sequence:
MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQLEESLLGKMLETCGDAENQLAFELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQHADWFFPGEVEFNVSEAFVPLATPNSNHSSHTGNDSDSGTLERKRPASMAVMEGDLVKKESFGVKLMDFQAHRRGGTLNRKHISPAFQPPLPPTDGNALAPAGPELPSQSSRADSNSVGGPVPSSSGILEQGLSPGDSSPPKPKDSVSAAAPVAGRNSNQITTVPNQAQTGGNSHQLSVGTAHSAAGPSPHTLRRAVKKPAPAPPKPGNPPPGHPGGQSSPGTGTSPKPSTRSPSPPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTPGMRRCSSSLPPIQAPNHPPPQPPTQPRLGEQGPEPGPTPPQTPTPPSTPPPAKQNSSQSETTQLHGTLPRPRPVPKPRNRPSVPPPPNPPGTHMGDGGLTPSVPTASRIVTDTNSRVSESLRNIFPEIHSDLASKEVPGHILLDIDNDTESTAL
Protein: Release factor glutamine methyltransferase (RF MTase) (EC 2.1.1.297) (M.EcoKHemKP) (N5-glutamine methyltransferase PrmC) (Protein release factor methylation C) (Protein-(glutamine-N5) MTase PrmC) (Protein-glutamine N-methyltransferase PrmC) (P0ACC1)
Organism: Escherichia coli (strain K12)
Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2.
Interaction partners:
- Peptide chain release factor RF1
- Peptide chain release factor RF2
- Protein YchQ
- 2-dehydro-3-deoxyphosphooctonate aldolase
- UPF0162 protein YchA
- Glutamyl-tRNA reductase
- Ribosomal protein L11 methyltransferase
- NH
Sequence:
MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ
Protein: LD32760p (RE66939p) (Q960V7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MITKIRTSKLFDGKVYAKGAPKSCAVNVNNSLEFDLKMRYNDLECNVRQSAYGRYMNDIVIQHHDMIVTSSDLGLAVSCQYDLTNKTVVNNVDLGVTGEIESTLSEEIIVDSPNVIMKITARDGSDMKRIAEVGDPLALRFEIVDANSPYEIFVRELVAMDGTDSAEITLIDANGCPTDQYIMSAMQKLANNRKVLLSQFDAFKFPSSELVQFRALVTPCIPRCEPVICDNDENGELKSLLSYGRRKRSVLNGTDGVELAIKSERQKRDVSHQAAGDENILLVQSIQITDKFAFNGADAPGGSGSEAGGLDGLAKLQLDLGTKSDTCINGYGFIIAGALFLLLQLTVIAVWDNMQKRALHKR
Protein: Adipose-secreted signaling protein (Q9GZN8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9D1K7}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Sequence:
MAAANKGNKPRVRSIRFAAGHDAEGSHSHVHFDEKLHDSVVMVTQESDSSFLVKVGFLKILHRYEITFTLPPVHRLSKDVREAPVPSLHLKLLSVVPVPEGYSVKCEYSAHKEGVLKEEILLACEGGTGTCVRVTVQARVMDRHHGTPMLLDGVKCVGAELEYDSEHSDWHGFD
Protein: Leukotriene C4 synthase (LTC4 synthase) (EC 4.4.1.20) (Glutathione S-transferase LTC4) (EC 2.5.1.-) (Leukotriene-C(4) synthase) (Q925U2)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (By similarity).
Subcellular location: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}.
Interaction partners:
- Leukotriene A-4 hydrolase
- Polyunsaturated fatty acid 5-lipoxygenase
- Glutathione hydrolase 5 proenzyme
- Cysteinyl leukotriene receptor 1
- Cysteinyl leukotriene receptor 2
- Leukotriene B4 receptor 1
Sequence:
MKEETALLATVTLLGVLLQAYFSLQVISARRTFHVSPPLTSGPPEFERVFRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLFYLFARLRYFQGYARSAQHRLDPLYASARALWLLVAMAALGLLVHFLPGTLRAALFRWLQVLLPMA
Protein: Protein O-mannosyl-transferase 2 (EC 2.4.1.109) (F1Q8R9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6A1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Fukutin.
- Ribitol-5-phosphate transferase
- Protein O-mannosyl-transferase 1
- Protein O-mannose kinase
- Ribitol-5-phosphate xylosyltransferase 1
- Dolichol kinase.
- Dolichol-phosphate mannosyltransferase subunit 3
- Dystroglycan 1
Sequence:
MDVRPKENFSQRQDTSAVRHRKTCKVNERAEIPSQPHNGTINGVNKRITKREGGEHISSPSRDAHVPVFILALVIVLSVSTRFYKITEPPHVCWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLTGYDGTFPFIKPGDKYEHHNYWGMRAFCAALGSCLPPFAFLVVLELSQSSTAALIAASLLIFDTGCITLSQYILLDPILMFFIMGSVLCMVKFNTQRLGPFSFSWWFWLLLTGLCLSGSLGVKFVGLFVILLVGINTALDLWRLLGDLSLSLVDFGKHLLARVFGLIMLPLFLYTTIFAIHFIVLNRSGPGDGFFSSAFQSRLIGNNLHNASMPEYLAYGSVITVKNLRIAGGYLHSHWHLYPEGVGAHQQQVTAYLHKDYNNLWLVKRLDNSDDLTGSPELVRHGDIIRLEHKETTRNLHSHFHEAPLTKKHLQVTGYGINGSGDVNDLWQVEVCGGRKGDPVKVLRSKVRFLHRATGCVLCSSGKTLPKWGWEQVEVTCSPYVKETPNSQWNIEDHINPKLPNISLAVLKPTFLEILWESHIVMIRGNSGLKPKDNEMNSKPWHWPINYQGLRFSGVNETEYRVYLLGNPVIWWLNLLSLALFVILLTVASLAVQRRVKMEGMMKVHCHTLMEGGGMLFLGWLLHYLPFYIMGRILYYHHYFPAMMFSSMLTGITLDILLQNLQLLFSSSLSHYLMRGGQSVLLLGFIYSFYLFHPLSYGMRGPLAHDSASSMAGLRWMESWEF
Protein: Putative phosphonates utilization ATP-binding protein PhnK (P16678)
Organism: Escherichia coli (strain K12)
Function: Belongs to an operon involved in alkylphosphonate uptake and C-P lyase. Exact function not known. PhnK is not required for the ribophosphonate triphosphate (RPnTP) synthase reaction.
Interaction partners:
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Probable transcriptional regulator PhnF
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Phosphonates-binding periplasmic protein
- Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
Sequence:
MNQPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQN