wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase F(0) complex subunit j, mitochondrial (6.8 kDa mitochondrial proteolipid protein) (MLQ) (ATP synthase membrane subunit 6.8PL) (P56378)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). Minor subunit required to maintain the ATP synthase population in the mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:24330338}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLQSIIKNIWIPMKPYYTKVYQEIWIGMGLMGFIVYKIRAADKRSKALKASAPAPGHH
Protein: Sigma non-opioid intracellular receptor 1 (Sigma 1-type opioid receptor) (Sigma1-receptor) (Sigma1R) (O55242)
Organism: Mus musculus (Mouse)
Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Lanosterol 14-alpha demethylase
- Squalene monooxygenase
- Ergosterol biosynthetic protein 28 homolog
- Sigma intracellular receptor 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Lathosterol oxidase
- 7-dehydrocholesterol reductase
- Delta
- Methylsterol monooxygenase 1
Sequence:
MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
Protein: Potassium voltage-gated channel subfamily KQT member 5 (Q8MQC5)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein eS6
Sequence:
MSQASQEDNDGGDLLSPESPMTPDGMILARMPWHPGLIGNWNTVKSVSCSMLNGDETDQAAPSDEQQEAGSSSAIGQESRKTVVFQEPDIGFPSEHDQLTTLHDSEEGNRKMSLVGKPLTYKNYRTDQRFRRMQNKMHNFLERPRGWKAATYHLAVLFMVLMCLALSVFSTMPDFEVNATIVLYYLEIVFVIWLATEYICRVWSAGCRSRYRGISGRIRFATSAYCVIDIIVILASITVLCIGATGQVFAASAIRGLRFFQILRMLRIDRRAGTWKLLGSVVWAHRQELLTTVYIGFLGLIFSSFLVYLCEKNTNDKYQTFADALWWGVITLSTVGYGDKTPETWPGKIIAAFCALLGISFFALPAGILGSGFALKVQQHQRQKHLIRRRVPAAKLIQCLWRHYSAAPESTSLATWKIHLARELPPIVKLTPNGSNNATGLINRLRQSTKRTPNLNNQNLAVNSQATSKNLSVPRVHDTISLVSTSDISEIEQLGALGFSLGWKSKSKYGGSKKATDDSVLQSRMLAPSNAHLDEEEAVGYQPQTIEEFTPALKNCVRAIRRIQLLVARKKFKEALKPYDVKDVIEQYSAGHVDLQSRVKTVQAKLDFICGKNIEKIEPKISMFTRIATLETTVGKMDKKLDLMVEMLMGRQASQRVFSQNTSPRGEFSEPTSARQDLTRSRRSMVSTDMEMYTARSHSPGYHGDARPIIAQIDADDDDEDENVFDDSTPLNNGPGTSSC
Protein: Klingon (LD10776p) (Q9VCT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- U3 small nucleolar RNA-associated protein 15 homolog
- Dysfusion, isoform D
- Phenoloxidase-activating factor 2
- GH08353p
- Structural maintenance of chromosomes protein
- Probable G-protein coupled receptor CG31760
- Gustatory and pheromone receptor 32a
- HDC05827
- MIP12702p
- AT29763p
Sequence:
MNIISRSIRTGALAPPITAHASANANASGLRKSSQRRNRAPLQMNCPILIVISLGWLLHAHAGSGGFAVEAAISNRGSNSRSMSNVQQSAVAASTLTATLPRFLSRGHTYRAVVGDTLVLPCQVENLGNFVLLWRRGTNVLTASNIMVTRDERVRLIDGYNLEISDLEPQDAGDYVCQISDKINRDQVHTVEILVPPSVRAIPTSGQLQARKGGPITLECKGSGNPVPSIYWTKKSGANKSTARIGDGPILTLEKLERQQAGVYQCTADNGVGDPVTVDMRLDVLYPPDIQVEKSWIHSGEGFEAKLVCIVFADPVATVSWYQNSFPIQSTDRRIMATRANRHMLTIRHIQQEDFGNYSCVADNSLGRSRKYMELSGRPGAAEFYSPKWGRSPDSYNLTWKIDSYPPLEEVRLLYRRVQMNETYQQPGRWHDFILTPEHRPASEPLTHIMSYTIKNLHPGGYYEAIVQAKNRYGWNEVSDIFQFVVATNSQDIGPEDAEVVASSKSRSNSASIGSLPGSTVLHTALLLALALSNCQFDRRRLGLG
Protein: Sarcoplasmic reticulum glycoprotein, putative (Q584E9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
Sequence:
MSSHGKLVRKAEDLQEDLSWDSHIKHVLIELEKIYFQRIRPIEVKFDYDMCCPSWFGESMVQKKPFITFLGPFSAGKSTFINYLLQGNLLSTGPQPVTDRFTVISHAKDVQKIPGRVLMADSKQPFRGLNQFGGVFGEVLEGITHPHPILQSVTLIDTPGVLETAGNAHSRRYDYVNACRWFVEKSDLVFVMFDPTKLDSGEELRAVFQQALRGHESKIRIILNKADTVEPQELMRVYGALFWNLSALVATTEPPRVFISSFWEQPYRMGTDHELFTEEKADLIYHITTVVPMQALDRRVASVLQRATRVIAFAILCATYKTKMPSLFGKAKARKQFIEDLPQICEDLANKYRCSVADFPKKEVLENFFSRAKTSDFFDMNQLLKRKWIELMRITVDRDLPMLLKPLEESAVVDPNDRKHALLLQREYFKRMSMEAHGQLFVEDVCQNLGTVPMIQSQFTDRPAICDVPANNTSMQLQSTAPPNGAGGNVNQEQLAVMMQMMQTMMAAQQGQKPSPQQQGVPLISQQAYAPQQVQPEQGGPLFPPSQQISTTTQQMNPYQQMQTMDTLQQGVPQFPPSQVCIEMPQSNPYQQGQPTFMPYGGFPSDPQGQGLPQNPQQQGQLFP
Protein: Autophagy and beclin 1 regulator 1 (A0A8I6AF66)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGNIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPNSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLNETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGTASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLLSEPGQLAERGLSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDSSNVGEAAGPSGEPRNR
Protein: Amino acid transporter (E1JHQ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
- LD37241p
- GH04846p
- LD25378p
- Amino acid transporter protein JHI-21
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MEMEKSGKFSDYLFAKMGPPTSTELPPKTTECSDAPVELTGYRRWLSENLMLLVTLSGVLLGVILGLSLRPLNLHGDSIMLISYPGELFMRVLKLMILPLVISSLIAGSASLNAKMNGKIALRTLVYFASTSFFNAALGIALVLLIHPGNPDLHNADDRSTDRRAVNLLDSLLDLGRNVFPDNLFQASIQQAHTVYLPKPSILHVFNETMNDTLASGSEAQRLSEDLTEDVVLVRDIQYRSGTNTLGIVFFCLVFGTFLGTIGQKGQVVVDFFAAIFEVIMKMVTCVMWLTPVGISSVIAGKILSVGDLGLVMSQLMWFIVTVAIGVFIYQFVVMQAIYFVVVRRNPFKFYAGLIQAMLTAFATASTAAALPITFRCMNEKLKVDPRITRFVLPIGCNINMDGTALYIAVASIFIAQMSGMVLGFGELLTVLLTSTAASMSSASVPSAALVLLLVVLTAIDAPVQDVTLLFAVDWFVDRIRTTNNMLGDCYTAAVVEELSRKELMALDAASVNYQDMPAGTPNGHGHGHGHHDGGLLEGQTELETSSKCVMTMTDSVVVDISAVMNNVNLQQEHCNRRV
Protein: Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) (P25037)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin
- Ubiquitin-ribosomal protein eL40A fusion protein
- SAGA complex subunit SGF29
- SAGA complex subunit SUS1
- Ubiquitin carboxyl-terminal hydrolase YUH1
- Ubiquitin carboxyl-terminal hydrolase 2
- SAGA complex subunit SPT3
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SGF73
Sequence:
MDLFIESKINSLLQFLFGSRQDFLRNFKTWSNNNNNLSIYLLIFGIVVFFYKKPDHLNYIVESVSEMTTNFRNNNSLSRWLPRSKFTHLDEEILKRGGFIAGLVNDGNTCFMNSVLQSLASSRELMEFLDNNVIRTYEEIEQNEHNEEGNGQESAQDEATHKKNTRKGGKVYGKHKKKLNRKSSSKEDEEKSQEPDITFSVALRDLLSALNAKYYRDKPYFKTNSLLKAMSKSPRKNILLGYDQEDAQEFFQNILAELESNVKSLNTEKLDTTPVAKSELPDDALVGQLNLGEVGTVYIPTEQIDPNSILHDKSIQNFTPFKLMTPLDGITAERIGCLQCGENGGIRYSVFSGLSLNLPNENIGSTLKLSQLLSDWSKPEIIEGVECNRCALTAAHSHLFGQLKEFEKKPEGSIPEKLINAVKDRVHQIEEVLAKPVIDDEDYKKLHTANMVRKCSKSKQILISRPPPLLSIHINRSVFDPRTYMIRKNNSKVLFKSRLNLAPWCCDINEINLDARLPMSKKEKAAQQDSSEDENIGGEYYTKLHERFEQEFEDSEEEKEYDDAEGNYASHYNHTKDISNYDPLNGEVDGVTSDDEDEYIEETDALGNTIKKRIIEHSDVENENVKDNEELQEIDNVSLDEPKINVEDQLETSSDEEDVIPAPPINYARSFSTVPATPLTYSLRSVIVHYGTHNYGHYIAFRKYRGCWWRISDETVYVVDEAEVLSTPGVFMLFYEYDFDEETGKMKDDLEAIQSNNEEDDEKEQEQKGVQEPKESQEQGEGEEQEEGQEQMKFERTEDHRDISGKDVN
Protein: Small ribosomal subunit protein eS30A (40S ribosomal protein S30-A) (P0CX33)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS5
Sequence:
MAKVHGSLARAGKVKSQTPKVEKTEKPKKPKGRAYKRLLYTRRFVNVTLVNGKRRMNPGPSVQ
Protein: Probable alpha-L-arabinofuranosidase A (ABF A) (Arabinosidase A) (EC 3.2.1.55) (A2Q7E0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MVAFSALSGVSAVSLLLSLVQNAHGISLKVSTQGGNSSSPILYGFMFEDINHSGDGGIYGQMLQNPGLQGTAPNLTAWAAVGDATIAIDGDSPLTSAIPSTIKLNIADDATGAVGLTNEGYWGIPVDGSEFHSSFWIKGDYSGDITVRLVGNYTGTEYGSTTITHTSTADNFTQASVKFPTTKAPDGNVLYELTVDGSVAAGSSLNFGYLTLFGETYKSRENGLKPQLANVLDDMKGSFLRFPGGNNLEGNSAENRWKWNETIGDLWDRPGREGTWTYYNTDGLGLHEYFYWCEDLGLVPVLGVWDGFALESGGNTPLTGDALTPYIDDVLNELEYILGDTSTTYGAWRAANGQEEPWNLTMVEIGNEDMLGGGCESYAERFTAFYDAIHAAYPDLILIASTSEADCLPESMPEGSWVDYHDYSTPDGLVGQFNYFDNLNRSVPYFIGEYSRWEIDWPNMKGSVAEAVFMIGFERNSDVVKMAAYAPLLQLINSTQWTPDLIGYTQSPGDIFLSTSYYVQEMFSRNRGDTIKEVTSDSDFGPLYWVASSAGDSYYMKLANYGSETQDLTVSIPGTSTGKLTVLADSDPDAYNSDTQTLVTPSESTVQASNGTFTFSLPAWAVAVLAAN
Protein: Melanoma-associated antigen B2 (Cancer/testis antigen 3.2) (CT3.2) (DSS-AHC critical interval MAGE superfamily 6) (DAM6) (MAGE XP-2 antigen) (MAGE-B2 antigen) (O15479)
Organism: Homo sapiens (Human)
Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
Interaction partners:
Sequence:
MPRGQKSKLRAREKRRKARDETRGLNVPQVTEAEEEEAPCCSSSVSGGAASSSPAAGIPQEPQRAPTTAAAAAAGVSSTKSKKGAKSHQGEKNASSSQASTSTKSPSEDPLTRKSGSLVQFLLYKYKIKKSVTKGEMLKIVGKRFREHFPEILKKASEGLSVVFGLELNKVNPNGHTYTFIDKVDLTDEESLLSSWDFPRRKLLMPLLGVIFLNGNSATEEEIWEFLNMLGVYDGEEHSVFGEPWKLITKDLVQEKYLEYKQVPSSDPPRFQFLWGPRAYAETSKMKVLEFLAKVNGTTPCAFPTHYEEALKDEEKAGV
Protein: Neurotrimin (GP65) (Q62718)
Organism: Rattus norvegicus (Rat)
Function: Neural cell adhesion molecule.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MGVCGYLFLPWKCLVVVSLRLLFLVPTGVPVRSGDATFPKAMDNVTVRQGESATLRCTIDNRVTRVAWLNRSTILYAGNDKWCLDPRVVLLSNTQTQYSIEIQNVDVYDEGPYTCSVQTDNHPKTSRVHLIVQVSPKIVEISSDISINEGNNISLTCIATGRPEPTVTWRHISPKAVGFVSEDEYLEIQGITREQSGEYECSASNDVAAPVVRRVNVTVNYPPYISEAKGTGVPVGQKGTLQCEASAVPSAEFQWFKDDKRLVEGKKGVKVENRPFLSRLTFFNVSEHDYGNYTCVASNKLGHTNASIMLFGPGAVSEVNNGTSRRAGCIWLLPLLVLHLLLKF
Protein: Ion transport domain-containing protein (Q688B3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLSSQHKKPVRSSYVESDRVEWALKIACTISMITVCIHTPRTIELFQPLNYIILAADFISVSIFMLDSVLRIHYEGIFRCDSSYLSNRWSQFSVFISIIHLLSFLLHCYQLIDNFFPFLHLNYRAWYGAIRSIRPFIIIRLIPLVVKFKLPKNRIEQLLKRSSQQVKNVTLFFVFFMTLYAIFGIQLFGRMDYHCVQPKTDPNNVTIMDLAIPDTMCAPEGIGGYECPAPMVCMQLNLNAKGEGFYGMFNDFGASVFTVYLAASEEGWVYVLYDCMDSLPSYLAFLYFCTLIFFLAWLVKNVFIAVITETFAEIRVQFSEMWQKKEVTLDEGFRKKLEKTDDGWRLIRLDGEVEPEGPKQKLQWMLRSMYFQCFVIIFVVINAIGNAMFVYRHDETDKPRKYNFYLFEVGFTILFNVECIIKILCYGFRNFIRRGIFKFELILCLGSSLNCVKFFYERNYFTYFQTFRLLRLIKASPILEDFVWKIFSPGKKLGGLVIFTIAFICCYSAISLQLFYSVPNLHHFRTFPQAFMSMFQIITQEGWTDFVVEVLRATDDNLVPLVALYFVAYHLFVTLIVLSLFVAVILDNLEMDEELKKVKQLRAREATTSMRSTLPWRLRVFEKFPTRPQMAAMRKADSDFPMPKVRGSFTHQFAVDHSLETTDVIESDFEFPKRIMKSAGKRKISKSGLTFRQIGSTSLRCSLNNLLEKSRSMTGKFLQTAVRNKQFNMYSENGDLSRPSDSAPKKNAKQGEIDIRALQQKRQLAEITRNRIEEDMRENHPFFDRPLFLVGRASQLREFCKKMVHSKYDSQDDGTNGGAKTKKRFKEIRALIGIMPYIDWAMATVTIVSCISMLFESPWPTTGENLVMNNGYLQISDYFFVLSMTFELCVKIIANGLFFTPKAVVRDVGGVMNLFIYFTSVIFLAWMPKHVEINSLAQFLMICRAMRPLRIYTLVPHIRRVVLEFFRGFKEILLVTILMIVVMFIFASFGVQIVGGKLAACNDPTVSSRENCTGVFWQKLFVTRLEVYGKDTEAMHPKIMVPRVWTNPRNFNFDHVGNAMLALFETLSFKGWNVIRDILWSRHGPWAVVFIHIYVFIGCMIGLTLFVGVVIANYTQNRGTALLTVDQRRWHDLKARLKMAQPLHVPPKPSESARLRTKLYDLTMSRWFNQAFALLVVLNSFTLVIPWNVEEEEQRATYVFTVTALAAFMNMLFVIEIILKVIAYTFSGFWQSRRNRVDLLITVFGVIWIFLHFFVALPSSKIDVDVQVELKKFTYTFGYLVVILRFFTIASRNSTLKMLMLTVIMSMFRSFFIITALFLLVLFYAYTGVILFPMVKYGMAVSKHVNFRTASEALVVLFRCLTGEDWNDIMHDCMRSAPFCYWNEGMNYWETDCGNFYGAIIYFCSFYLIITYIVRNLLVAVIMENFSLFYSSEEDALLSYADIRNFQYVWNMVDQEQKRTIPVERVKFLLRLLKGRLEVDPEKDRILFKHMCYEMERLHNGEEVSFHDVLYMLSYRSVDIRKSLQLEELLQREELEFIIEEEVAKQTIRTWLEGCLRKMRNPSQKDAEGVLPFGGGHPVIHSSGHSSISHEETVAQRLRFENIRGDSVDTEETESSEEETPPPIRKKAAVKNRRGSIPDVLSRTGLFQEAARKFMVGSSSEKKQVKSRSPETVQLLPKRANSEIRKGSGQPKNFHLQLNVYDLPDVEERGEDSPFSPKNLSDDFNGEHSPLVITPSLPVPPTHGSPRPLMPCETTKDIEKWWNSLVD
Protein: Tubulin beta-6 chain (Tubulin beta class V) (Q9BUF5)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-1C chain
- Tubulin alpha-1A chain
- Tubulin alpha-4A chain
- Tubulin alpha-8 chain
- Tubulin alpha chain-like 3
- Tubulin alpha-3C chain
- Tubulin alpha-3E chain
- Gap junction alpha-1 protein
- Microtubule-associated protein tau
Sequence:
MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQYQDATANDGEEAFEDEEEEIDG
Protein: Low affinity immunoglobulin gamma Fc region receptor III (IgG Fc receptor III) (Fc-gamma RIII) (FcRIII) (CD antigen CD16) (P08508)
Organism: Mus musculus (Mouse)
Function: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor which binds to IgG1, IgG2a and IgG2b. Mediates neutrophil activation by IgG complexes redundantly with Fcgr4.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17558411}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- B-lymphocyte antigen CD19
- T-cell surface glycoprotein CD3 zeta chain
- High affinity immunoglobulin gamma Fc receptor I
- Neural cell adhesion molecule 1
- Low affinity immunoglobulin gamma Fc region receptor III-A
- Tyrosine-protein kinase SYK
- Myeloid cell surface antigen CD33
- Monocyte differentiation antigen CD14
- TYRO protein tyrosine kinase-binding protein
Sequence:
MFQNAHSGSQWLLPPLTILLLFAFADRQSAALPKAVVKLDPPWIQVLKEDMVTLMCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQRVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYKSNFSIPKANHSHSGDYYCKGSLGSTQHQSKPVTITVQDPATTSSISLVWYHTAFSLVMCLLFAVDTGLYFYVRRNLQTPREYWRKSLSIRKHQAPQDK
Protein: Transient receptor potential cation channel subfamily V member 5 (TrpV5) (Calcium transporter 2) (CaT2) (Epithelial calcium channel 1) (ECaC1) (Osm-9-like TRP channel 3) (OTRPC3) (Q9JIP0)
Organism: Rattus norvegicus (Rat)
Function: Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine. Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification (By similarity). A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (By similarity). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10875938}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9NQA5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NQA5}. Note=Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells (By similarity). The expression of the glycosylated form in the cell membrane is increased in the presence of WNK3 (By similarity). {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9NQA5}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Protein kinase C beta type
- Protein kinase C gamma type
- non-specific serine/threonine protein kinase
- Protein S100-A10
- Mucolipin 3.
- Klotho
- Plasma membrane calcium-transporting ATPase 1
- Transient receptor potential cation channel subfamily M member 4
Sequence:
MGVKKPWIQLQKRLNWWVREQDWNQHVDQLHMLQQKSIWESPLLRAAKENDMCTLKRLQHDQNCDFRQRGALGETALHVAALYDNLDAAIMLMETAPYLVTESTLCEPFVGQTALHIAIMNQNVNLVRALLARGASASARATGSAFHRSSHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYNLLLSHDGGDHLKSLELVPNNQGLTPFKLAGVEGNTVMFQHLMQKRKHIQWSLGPLTSSIYDLTEIDSWGEDLSFLELVVSSKKKEARQILEQTPVKELVSLKWKKYGQPYFCLLGMLYIFYMICFTTCCVYRPLKFRDANRTHVRDNTVLEQKPLQEAYVTYQDKVRLVGELVTVIGAVVILLIEIPDIFRVGASRYFGHTVLGGPFHVIIITYASLVLLIMVMRLTSMNGEVVPISMALVLGWCSVMYFSRGFQMLGPFTIMIQKMIFGDLLRFCWLMAMVILGFASAFYIIFQTEDPESLGEFSDYPTAMFSTFELFLTIIDGPANYSVDLPFMYHLTYFAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWPRSGICGCEYGLGDRWFLRVEHHQEQNPYRVLRYVEAFKSSDKEEVQEQLSEKQPSGTETGTLARGSVVLQTPPLSRTTSLSSNSHRGWEILRRNTLGHLNLGQDLGEGDGEEIYHF
Protein: C3H1-type domain-containing protein (MEX-1) (G5ECB9)
Organism: Caenorhabditis elegans
Interaction partners:
- PIP-1
- K Homology domain-containing protein
- Zinc finger-interacting factor 1
- Nanos-type domain-containing protein
- ATP-dependent RNA helicase cgh-1
- Pharynx and intestine in excess protein 1
- Pumilio domain-containing protein 5
- Protein meg-1
- Zinc finger protein mex-6
- Female germline-specific tumor suppressor gld-1
Sequence:
MQSSNGEHHQQKQTPYFMNAPCDPALLALAQQTFLGFQPQKNMYQHGFPPMLPHRNLIPSLAAAIPEMDKLMLEEPIEAGSMPYRRATNKNISVSDDSFNNMHRSSSSSQYRRHSAQWETMTDDERESVQRQKRKEEAFKTALCDAFKRSGSCPYGEACRFAHGENELRMPSQPRGKAHPKYKTQLCDKFSNFGQCPYGPRCQFIHKLKKGLPLSEYNRALQEGEISPARDDEITNPDESSSQVEDLSELHHRQHQQQQQYQQRYRRPPFNNFHDMSDSGYSAPRRRLHHQFEHLGSEQQQQQQQQTPAPKIVYPSMQVVNIEMATGDGPKRSDNHHYHHHHHQRRHIPAPPSTGPLSSLIDQADYEASMASGKMFGKPENIRTYGAMIRANEEHVERNQTGVVKKERATVLPKRDLSLIREEDTLLVDGSHLNMTSSAILPAHQIPSTTTTSTSSPVQEQPWYEKIFGKMTMIQEESSMGGEDDDAHEDHYSR
Protein: Prolylcarboxypeptidase (E9PNF7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQALADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH