wanglab/gogpt-training-data huggingface dataset:
Protein: HECT and RLD domain containing E3 ubiquitin ligase 4, isoform C (LD13353p) (E8NHA2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASGKELYCWGSTSHGQLGLGGIEDEQILTPSQIPWTPDTAVQQVACGHRHTLFLTATGKVYACGSNDYSQLGHDLPTKRPRMSPFLLIPELQDYVIIQICCGSRHSLALSDWGQVLSWGDNDCGQLGHATDKEIVQLPKVVRQLVTKTVVQIACGNNHSLALTSCGELYSWGSNIYGQLGVNSPNDLTHCNYPLRLTTLLGIPLAAIACGGNHSFLISKSGAVFGWGRNNCGQLGLNDETNRSYPTQLKTLRTLGVRFVACGDEFSVFLTNEGGVFTCGAGAYGQLGHGFSSNEMLPRMVMELMGSTITQVACGNRHTLALVPSRGRVYAFGLGSSGQLGTRSTKSLMLPQVVIGPWVSPSGSALLQSNDSQVSLVIRQIFSGGDQSIVTTTLFVDKVPPEDFRNYNPKSQILTLTAEVTKQCAQCKQGLQSDMDLLSSIELIFRSQACWNGSFLLDHDRHFGCSVRNHGLDLKAAQLAFDNLRAVENESIRQVIWDNITKELVGSLVCSPADVESMRLYLLLPLYHEFVNSKHYKSLQVPFANAIFKLAENPRKVLNKWLAQTPAEYFEHLVQNFLHVVIHIISFKMGLAAASPSAERRQQLLPYNTELEIILKLMKTLCQINNERHDRLNYQIFYWPDLSDYADVQQEYVKWIMADTARDFNICNYSFIFDQSAKTALLQADQALQMHSAMANAATMAFSFFNYGMPISQFIVLNVTRENLVQDSLRELQHYSQSDLKKPLKIKFHGEEAEDAGGVRKEFFMLLLKDLLDPKYGMFKEYEQSRLLWFADLTFETENMYFLIGVLCGLAIYNFTIINLPFPLALFKKLLGKPVDLSDLRQLSPPEANSMQSLLDYQGDDFKEVFDLTFEISRDVFGEAETKCLKPNGNEIAVTLENRQEFVDLYVDFVFNKSVELHYNAFHKGFMKVCSGRVIHIFQPEELMAVVVGNEDYDWQALQDNCEYREGYTSVDDTIKWFWEVIHDMSEAEKKSFLLFLTGSDRIPIQGMKALKLTIQPTPDERFLPVAHTCFNLLDLPRYKTKERLKYKLLQAIQQTQGFSLV
Protein: Protein CIA1 (Cytosolic iron-sulfur protein assembly 1) (Protein EMBRYO DEFECTIVE 1345) (O80990)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:23104832}. Cytoplasm {ECO:0000269|PubMed:23104832}.
Interaction partners:
- MMS19 nucleotide excision repair protein homolog
- Protein AE7
- Protein NAR1
- Protein AE7-like 2
- Protein AE7-like 1
- General transcription and DNA repair factor IIH helicase subunit XPD
- Cytosolic Fe-S cluster assembly factor NBP35
- Defensin-like protein 87
- Anamorsin homolog
- Frataxin, mitochondrial
Sequence:
MDLMEKNLELVEIQKLEGHTDRVWSVAWNPVSSHADGVSPILASCSGDNTVRIWEQSSLSRSWTCKTVLEETHTRTVRSCAWSPSGQLLATASFDGTTGIWKNYGSEFECISTLEGHENEVKSVSWNASGSCLATCSRDKSVWIWEVLEGNEYDCAAVLTGHTQDVKMVQWHPTMDVLFSCSYDNTIKVWWSEDDDGEYQCVQTLGESNNGHSSTVWSISFNAAGDKMVTCSDDLTLKIWGTDIAKMQSGEEYAPWIHLCTLSGYHDRTIYSAHWSRDDIIASGAGDNAIRLFVDSKHDSVDGPSYNLLLKKNKAHENDVNSVQWSPGEGNRLLASASDDGMVKIWQLATKP
Protein: Phospholipase A I (AtPLA1) (EC 3.1.1.-) (F4HX15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidylserine (PS) and phosphatidylinositol (PI). Hydrolyzes phospholipids at both the sn-1 and sn-2 positions. Involved in basal jasmonic acid production and promotes resistance to the necrotrophic fungal pathogen Botrytis cinerea.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:12226489}.
Interaction partners:
- Phospholipase A
- Mediator of RNA polymerase II transcription subunit 14
- Patatin
- Phospholipase A2-alpha
- Galactolipase DONGLE, chloroplastic
- Patatin-like protein 7
- Phospholipase A2-beta
- Allene oxide cyclase 3, chloroplastic
- Cyclin-dependent kinase E-1
- Non-specific phospholipase C4
Sequence:
MSSTCSSPSAVEDPELGFRIDLDWTAGDSEDQVALRLESQLMVALPAPHDTVVVELKGIGDDDEGGLENVGLEMRVEKRREPLRAVTLMKAVGSGQQYDGVGVLTRLMRSDMMPAAIPAPAIDVASSCGVHWKTVTSLSLSGCGLLVMPVEVTELPLLEKLCLEHNKLSVLPPEIGKLKNLKILRVDNNMLISVPVELRQCVGLVELSLEHNKLVRPLLDFRAMAGLRILRLFGNPLEFLPEILPLHQLRHLSLVNIRIVSDENLRSVNVQIETENTSYFGASRHKLSAFSPLIFRSSSCHHPLLASTLVKIMQDEGNRSVIGKDENAVRQLISMITSDNQHVVEQACVALSSLARDVGVAMQLMKCDIMKPTETVLKSSSPDEVISVLQVVVTLAFVSDSVSQKMLTKDMLKALKSLCAHKNPEVQRQALLAVGNLAFCLENRRILITSESLRELLMRLIVTPEPRVNKAAARALAILGENEILRRSIKGRQVPKQGLRILTMDGGGMKGLATVQILKEIEKGSGKPIHELFDLICGTSTGGMLAIALGVKLMTLEQCEEIYKNLGKLVFAESVPKDNEAASWREKLDQLYKSSSQSFRVVIHGSKHSANEFERLLKEMCADEDGDLLIESAVKNVPKVFVVSTLVSVMPAQPFIFRNYQYPVGTPEMSYAFSDHSGGSTLTSSTASDQAGYYKQSAFMGSCKHQVWQAIRASSAAPYYLDDFSVDSYRWQDGAIVANNPTIFAIREAQLLWPDTKIDCLVSIGSGSVPTRVRKGGWRYLDTGQVLIESACSVERVEEALSTLLPMLPEIQYFRFNPVDDRCGMELDETDPAIWLKLEAAIEEFIQSNPQVFKNVCERLTLPFLNDEKWCDNLKPRFMNGKLPNSRVESSPSLGWRRNVLLMEAQHSPDSGRVKYHARALESFCSNNGIKLSSLHTTATPGCQKPSPGTAFPTPFTSPLITGSLPPSPLLFTPELGPQKFNRIDMVPPLSLDGGHVGKTVMSPPSSPPRQRQLYLPLRQMHEKLQNLPQVGILHLSLQNDSNGSILSWQNDVFVVAEPGDLADKFLQSVKVSILSVMQSNRRKAASVLSNICSISDLVRSKKCFQVGNIIHRYIGRQTLVMEDDQEIASFMFRRTVPSAHLTPDDIRWMVGAWRDRIIVFSGTFGPTQAVVKAFLDSGAKAVIGPSNEPQETPLITSQGSSEYNIGDQNGKFEIGEEEDEDEEVNEETEREEMEPPTPTSDWEDSDHEKTNRDGKYCGLWEDDEEEVSEFVCQLYDQLFRENSRVDVALQKALASHRKLRYTCHLPNV
Protein: ATP synthase F(0) complex subunit g, mitochondrial (ATPase subunit g) (ATP synthase membrane subunit g) (Q28852)
Organism: Bos taurus (Bovine)
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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase subunit e
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MAEFVRNLAEKAPALVNAAVTYSKPRLATFWYYAKVELVPPTPAEIPTAIQSLKKIINSAKTGSFKQLTVKEALLNGLVATEVWMWFYVGEIIGKRGIIGYDV
Protein: Metastasis associated 1 family, member 2 (Metastasis-associated protein MTA2) (Q7SXR7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAANMYRVGDYVYFENSSSNPYLIRRVEELNKTANGNVEAKVVCLFRRRDISASLNTLADSNARDFEEESKQPPTSEQQKHQLKHRELFLSRQFESLPATHIRGKCNVTLLNETDVLTGYLEREDCFFYSLVFDPVQKTLLADQGEIRVGSKYQAEIPDKLAEVEADSRVQEKLETKVWDPNNQLKDPQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQKNGYDLAKAMSTLVPQGGPVLCRDEMEEWSAPEAMLFEEALEKYGKDFNDIRQDFLPWKSLASVVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQITAPGNKPGMNGATGYQKGLSCESCHTAQSQQWYAWGPPNMQCRLCSSCWIYWKKYGGLKTPTQLEGATRASSEAAPRGHMTRQEVQGMSPFTSSAGRAKLLAKNRQTFILQTTKLTRIARRVCQDILQSRRAARRPYASINANAVKAECMIRLPKAAKSGVKNRPIPRPSLINIVKDLAIQAPLKLKAPRGAPTPINRNQVNQPRSASALLGKRPFDNAGGHLLSTNGRPFAMGMRAANQSVIKRQKVSQGDAPNPVVFVATKDTSPPGQSLDTPVVVFQAQVN
Protein: GDSL esterase/lipase At1g31550 (EC 3.1.1.-) (Extracellular lipase At1g31550) (Q9C857)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Uncharacterized protein At5g49220
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MASLDSHVLMKLGSLFLSTLFVSIVSSESQCRNFESIISFGDSIADTGNLLGLSDHNNLPMSAFPPYGETFFHHPTGRFSDGRLIIDFIAEFLGLPYVPPYFGSTNGNFEKGVNFAVASATALESSFLEEKGYHCPHNFSLGVQLKIFKQSLPNLCGLPSDCRDMIGNALILMGEIGANDYNFPFFQLRPLDEVKELVPLVISTISSAITELIGMGGRTFLVPGGFPLGCSVAFLTLHQTSNMEEYDPLTGCLKWLNKFGEYHSEQLQEELNRLRKLNPHVNIIYADYYNASLRLGREPSKYGFINRHLSACCGVGGPYNFNLSRSCGSVGVEACSDPSKYVAWDGLHMTEAAHKSMADGLVKGPYAIPPFDWSCLSSMIKKKEVVGNTIFFDE
Protein: DCN1-like protein 4 (DCNL4) (DCUN1 domain-containing protein 4) (Defective in cullin neddylation protein 1-like protein 4) (Squamous cell carcinoma-related oncogene 4) (Q9VWB1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:26792857}. Note=Exclusive nuclear localization in eye imaginal disk cells. {ECO:0000269|PubMed:26792857}.
Interaction partners:
- Nedd8-conjugating enzyme UbcE2M
- Cullin homolog 1
- Cullin 3, isoform F
- Ubiquitin-like protein NEDD8
- Cullin-4A
Sequence:
MPRGKRRAADTISDNMDHGQPKRARTSYTSIPTQQSSRRHIRLEDGFSQKRCMAWFQEYTTPDEPETLGPDGMEKFCEDIGVEPENIVMLVLAYKMGATQMGFFSQQEWLKGLTELDCDSAAKMVVKLDYLRSILNDPNSFKSIYRYAYDFAKDSDQRCMDILTAKAMLQLLLGKHWPLYPQFAQFLEQSKYKAINKDQWCNILEFSRTISIDLSNYDIDGAWPVMLDEFVEWLRLQRSQVTSTTGSS
Protein: Calmodulin-lysine N-methyltransferase (CLNMT) (CaM KMT) (EC 2.1.1.60) (F4JNX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the trimethylation of calmodulin. Regulates roots development probably by modulating auxin signaling responses. May be involved in gravitropism. Involved in abscisic acid (ABA)-mediated and abiotic stress responses, including salt (NaCl), cold, drought and heat stresses.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7Z624}. Nucleus {ECO:0000250|UniProtKB:Q7Z624}.
Interaction partners:
- Senescence/dehydration-associated protein At4g35985
- Histone-lysine N-methyltransferase EZA1
- Histone-lysine N-methyltransferase CLF
- Histone-lysine N-methyltransferase ATXR4
- Protein SET DOMAIN GROUP 41
- Histone-lysine N-methyltransferase ASHR1
- Histone-lysine N-methyltransferase ASHR2
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH5
- Histone-lysine N-methyltransferase family member SUVH9
- Histone-lysine N-methyltransferase SUVR3
Sequence:
MDPTSSSSSALRWKILRQALLRRSDSQSQTETKRISRKATQGFNLIPCQVVDSSPQSDKSREASVCYTLPITGSPKLYLTQRVDNCSDLNDFEISNRYNIDNTGLVCQWPSEEVLAYFCKSQPERFRGKRVIELGSGYGLAGLVIAAATEASEVVISDGNPQVVNYIKRNIETNSMAFGGTSVKAMELHWNQHQLSELTNTFDIIVASDCTFFKEFHKDLARTIKMLLKAKKASEALFFSPKRGDSLEKFMKEIKDIGLHYILTENYDAQVWKRHETLVKGDEAWPNYDKNHCYPLLIQITNQI
Protein: POU domain, class 6, transcription factor 1 (Octamer-binding transcription factor EMB) (Transcription regulatory protein MCP-1) (Q07916)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3').
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MPGISSQILTNAQGQVIGALPWVVNSASVATPAPAQSLQVQAVTPQLLLNAQGQVIATLASSPLPQPVAVRKPNTPESPAKSEVQPIQPTQAVPQPAVILTSPTPALKPSAATPIPITCSETPTVSQLVSKPHTPSLDEDGINLEEIREFAKNFKIRRLSLGLTQTQVGQALTATEGPAYSQSAICRFEKLDITPKSAQKLKPVLEKWLMEAELRNQEGQQNLMEFVGGEPSKKRKRRTSFTPQAIEALNAYFEKNPLPTGQEITEIAKELNYDREVVRVWFCNRRQTLKNTSKLNVFQIP
Protein: Tubulin beta-3 chain (Q9ERD7)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (By similarity). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (By similarity). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (By similarity). TUBB3 plays a critical role in proper axon guidance and maintenance. Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Plays a role in dorsal root ganglion axon projection towards the spinal cord (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20074521}. Cell projection, growth cone {ECO:0000269|PubMed:28483977}. Cell projection, lamellipodium {ECO:0000269|PubMed:28483977}. Cell projection, filopodium {ECO:0000269|PubMed:28483977}.
Interaction partners:
- Tubulin alpha-1B chain
- Microtubule-associated protein
- Gap junction alpha-1 protein
- Tubulin alpha-1A chain
- Tubulin alpha-4A chain
- Tubulin alpha-3 chain
- Tubulin alpha-1C chain
- Tubulin alpha-8 chain
- Tubulin alpha chain-like 3
- Microtubule-associated protein 2
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDDEESEAQGPK
Protein: Cytochrome P450 3A11 (EC 1.14.14.1) (CYPIIIA11) (Cytochrome P-450IIIAM1) (Cytochrome P-450UT) (Q64459)
Organism: Mus musculus (Mouse)
Function: Catalyzes erythromycin N-demethylation, nifedipine oxidation and testosterone 6 beta-hydroxylation.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- UDP-glucuronosyltransferase 2A3
- UDP-glucuronosyltransferase
- Cytochrome P450 3A25
- UDP-glucuronosyltransferase 2B17
- Cytochrome P450 1A2
- Cytochrome P450 2C29
- NADPH--cytochrome P450 reductase
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- UDP-glucuronosyltransferase
Sequence:
MDLVSALSLETWVLLAISLVLLYRYGTRKHELFKKQGIPGPKPLPFLGTVLNYYKGLWKFDMECYKKYGKTWGLFDGQTPLLAVTDPETIKNVLVKECFSVFTNRRDFGPVGIMSKAISISKDDEWKRYRALLSPTFTSGKLKEMFPVIEQYGDILVKYLRQKAKKGKPVTMKDVLGAYSMDVITSTSFGVNVDSLNNPEDPFVEKAKKLLRFDFFDPLLFSVVLFPFLTPVYEMLNICMFPKDSIEFFKKFVDRMKESRLDSKQKHRVDFLQLMMNSHNNSKDKVSHKALSDMEITAQSIIFIFAGYETTSSTLSFTLHSLATHPDIQKKLQDEIDEALPNKAPPTYDTVMEMEYLDMVLNETLRLYPIANRLERVCKKDVELNGVYIPKGSTVMIPSYALHHDPQHWSEPEEFQPERFSKENKGSIDPYVYLPFGNGPRNCLGMRFALMNMKLALTKIMQNFSFQPCKETQIPLKLSRQGLLQPEKPIVLKVVPRDAVITGA
Protein: Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Liver regeneration-related protein LRRG03) (Siderophilin) (P12346)
Organism: Rattus norvegicus (Rat)
Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Subcellular location: Secreted.
Interaction partners:
- Transferrin receptor protein 1
- Transferrin receptor protein 2
- Beta-2-microglobulin
- Ceruloplasmin
- Albumin
- Hereditary hemochromatosis protein homolog
- Transthyretin
- Alpha-2-HS-glycoprotein
- Alpha-2-macroglobulin
- Haptoglobin
Sequence:
MRFAVGALLACAALGLCLAVPDKTVKWCAVSEHENTKCISFRDHMKTVLPADGPRLACVKKTSYQDCIKAISGGEADAITLDGGWVYDAGLTPNNLKPVAAEFYGSLEHPQTHYLAVAVVKKGTDFQLNQLQGKKSCHTGLGRSAGWIIPIGLLFCNLPEPRKPLEKAVASFFSGSCVPCADPVAFPQLCQLCPGCGCSPTQPFFGYVGAFKCLRDGGGDVAFVKHTTIFEVLPQKADRDQYELLCLDNTRKPVDQYEDCYLARIPSHAVVARNGDGKEDLIWEILKVAQEHFGKGKSKDFQLFGSPLGKDLLFKDSAFGLLRVPPRMDYRLYLGHSYVTAIRNQREGVCPEGSIDSAPVKWCALSHQERAKCDEWSVSSNGQIECESAESTEDCIDKIVNGEADAMSLDGGHAYIAGQCGLVPVMAENYDISSCTNPQSDVFPKGYYAVAVVKASDSSINWNNLKGKKSCHTGVDRTAGWNIPMGLLFSRINHCKFDEFFSQGCAPGYKKNSTLCDLCIGPAKCAPNNREGYNGYTGAFQCLVEKGDVAFVKHQTVLENTNGKNTAAWAKDLKQEDFQLLCPDGTKKPVTEFATCHLAQAPNHVVVSRKEKAARVSTVLTAQKDLFWKGDKDCTGNFCLFRSSTKDLLFRDDTKCLTKLPEGTTYEEYLGAEYLQAVGNIRKCSTSRLLEACTFHKS
Protein: Inositol polyphosphate multikinase beta (EC 2.7.1.140) (EC 2.7.1.151) (Inositol polyphosphate 6-/3-/5-kinase beta) (AtIpk2-beta) (AtIpk2beta) (Q9FLT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentakisphosphate (Ins(1,2,3,4,6)P5) but not inositol 1,4-bisphosphate (Ins(1,4)P2), inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), inositol 1,2,6-trisphosphate (Ins(1,2,6)P3), inositol 3,4,5,6-tetrakisphosphate (Ins(3,4,5,6)P4), inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5), inositol 1,2,4,5,6-pentakisphosphate (Ins(1,2,4,5,6)P5) or inositol hexakisphosphate (InsP6). Involved in the auxin signaling pathway. Regulates axillary shoot branching and is required for phytate synthesis in seeds.
Subcellular location: Nucleus {ECO:0000269|PubMed:12566584}.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-tetrakisphosphate 1-kinase 1
- Inositol-pentakisphosphate 2-kinase
- Inositol 1,3,4-trisphosphate 5/6-kinase 4
- Inositol-pentakisphosphate 2-kinase
- Inositol-tetrakisphosphate 1-kinase 2
- Inositol-tetrakisphosphate 1-kinase 3
- Phosphoinositide phospholipase C 1
- Phosphoinositide phospholipase C 4
- Phosphoinositide phospholipase C 2
Sequence:
MLKVPEHQVAGHIASDGKLGPLVDDQGRFFKPLQGDSRGEHEAKFYESFTSNMKVPDHIHRYFPVYHGTQLVEASDGSGKLPHLVLDDVVSGYANPSVMDVKIGSRTWYPDVSEEYFKKCIKKDRQTTTVSLGFRVSGFKIFDHQESSFWRAEKKLVLGYNADGARLALRKFVSSNSPADSNLTPNCAFASEVYGGCNGILAQLLELKDWFETQTLYHFNSCSILMIYENESILMQGGDDAPAPRAQVKLVDFAHVLDGNGVIDHNFLGGLCSFIKFIKDILQSVEKHDETDTSLLENGR
Protein: IQ calmodulin-binding motif containing protein (Q389I6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDNQRNTERQPQSEEENAKSDVNVLENSCSGVVRSFPLPFIRREGATAAGSTSFSHALLVSGSKNRSQSETCSSDSSGAERTSGQITLLQTGDIGSDCSLSEDFQTSTTGHTERLRLCAPLRKRDSETTKDPRITRKCLLNAFPVSLKHIAVDEVAAAGMKPGDTVIAATSGYHHQFTEQTLLEIHGLLLRTAAAAEARKQYLMAGAHMEATSVGRRVTEGLIEGESARDLTVWSEGWYRHHPSVRGGVLTAVTVRPPQFKAGMLWNGEDKFLLGGTAFVEEARILQVKVPHSQNFLQMVSNSTTLCTEGSRVTKDQWTESCDGSDARSEPKKVAHLLVREYSSISKVRGGTMVQTFSLIPDHVQGNTQRSLILQRGQITKVLSECAPGAVTRGFSLQLLLPSSLRSELGSMAYENPFSTRDTDSNILDDGGGECGTFCANESTFANTMNSDFMSSTATLMMNRTSKVRTTVRQPLGDETYLRFANPKLYAFVMQQSPAILTAHTNAIREYILYHHRFRIRRKIAEVMQAIRALQGFFRHCLGRKKRAIKRMLRQWRRLEYQCRARLKKQTFEAPNVSRISYVVGSVLWEHVVTTDEYKLNMLEEQMKARRAGYLRWCAQRREENRMMPKVNESSESTEVRGIGDPRGASTVLSPKELSTGTMLVSREQPRLDSTLNKSHHRWIAKWRDVVHARFGWYIEPEVLLRESHRRLLHSLRNTILTMADVQAALKKRGEEDEFTLM
Protein: Synaptic vesicle 2-related protein (SV2-related protein) (Q9Z2I7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:9801366}; Multi-pass membrane protein {ECO:0000269|PubMed:9801366}.
Interaction partners:
- Major facilitator superfamily domain containing 9
- Protein spinster homolog 1
- Protein unc-93 homolog A
- Major facilitator superfamily domain-containing protein 10
Sequence:
MEEDLFQLRQLPVVKFRRTGESARSEDDAASGEHDVQIEGVRVGLEAVELDDGAAVPKEFANPTDDTFMVEDAVEAIGFGRFQWKLSVLTGLAWMADAMEMMILSILAPQLHCEWRLPSWQVALLTSVVFIGMMSSSTLWGNISDQYGRKTGLKISVFWTLYYGILSAFAPVYSWILVLRGLVGFGIGGVPQSVTLYAEFLPMKARAKCILLIEVFWAIGTVFEVLLAVFVMPSLGWRWLLLLSAAPLLVFAVLCFWLPESARYDVLSGNQEKAIATLKRIATENGAPMPLGKLIISRQEDRGKMRDLFTPHFRWTTLLLWFIWFSNAFSYYGLVLLTTELFQAGDVCSISSRKKAVEAKCSLACEYLSKEDYMDLLWTTLSEFPGVLVTLWVIDRLGRKKTMALCFVIFSLCSLLLFICIGRNVLTLLLFIARAFISGGFQAAYVYTPEVYPTATRALGLGTCSGMARVGALITPFIAQVMLESSVYLTLAVYSGCCLLAALASCFLPIETKGRALQESSHREWGQEMVGRGTNSTGVPRSNSGSQE
Protein: Calmodulin-4 (Calcium-binding protein Dd112) (Q9JM83)
Organism: Mus musculus (Mouse)
Function: Implicated in the early stage of ectopic ossification.
Interaction partners:
- Ryanodine receptor 2
- Nitric oxide synthase 1
- Protein phosphatase 3 catalytic subunit alpha
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Ryanodine receptor 1
- Nitric oxide synthase, inducible
- Calmodulin-1
- GTPase KRas
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- Transient receptor potential cation channel subfamily V member 1
Sequence:
MSHGFTKEEVAEFQAAFNRFDKNKDGHISVEELGDVMKQLGKNLPEKDLKALISKLDTDGDGKISFEEFLTAIEKYKKGHRAGELRAVFNVLDQNGDGYITVDELKESLSKLGESLSQEELEDMIRVADVDQDGKVKYEEFVRLHVEN
Protein: Fructose-bisphosphate aldolase (ALDO) (EC 4.1.2.13) (Q86A67)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Fructose-1,6-bisphosphatase
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Transketolase
- Glucose-6-phosphate isomerase
- Probable transaldolase
- Uncharacterized protein
- Phosphoglycerate kinase
- Enolase A
Sequence:
MNSKFADELIATAKAIVAPGKGILAADESTNTIGARFKKINLENNEENRRAYRELLIGTGNGVNEFIGGIILYEETLYQKMADGRLFTDVLREQKIHIGIKVDKGVVPIPGTDGETSTQGLDGLAERCKKYYEAGARFAKWRAVLKIDLAKNCPSQLSITENAHTLARYAAICQENGLVPIVEPEILMDGNHTVEQSAEVTEKVLAAVFKALNDHHILLEGALLKPNMVVNGTDCPIKATSEQIGKFTVRTLQRTVPPALTGVVFLSGGQTEIEATANLNAMNVLPNRPWALSFSYGRALQASVISTWKGESANVEAARKVYLHRAKCNSLAQLGKYTGEESTGSASESLYVKDYKY
Protein: Glycerophosphocholine phosphodiesterase GDE1 (EC 3.1.4.2) (Glycerophosphodiester phosphodiesterase GDE1) (Q02979)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline. The choline is used for phosphatidyl-choline synthesis. Required for utilization of glycerophosphocholine as phosphate source. May also use glycerophosphoinositol as substrate in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Lysophospholipase NTE1
- Vacuolar transporter chaperone 3 complex subunit 3
- Lysophospholipase 2
- Lysophospholipase 3
- Choline kinase
- Ethanolamine kinase
- Vacuolar transporter chaperone complex subunit 2
- Lysophospholipase 1
- Vacuolar transporter chaperone complex subunit 4
- Glycerophosphoinositol transporter 1
Sequence:
MKFGKTFANHRIPEWSSQYVGYKSLKKMIKEITRLQEDIYRAHNKNSYDEGRPPTKMRDSSNSAQNYLDSPKIQKLLASFFFAVDRDIEKVDTFYNSQYAEYKKRFERLLSSNQFNEIKSTLVVDANKEDAVAQTLLTKDTREMNMLLKGTSQASRLSYHKDDLIEIQSILAELRKQFRNLKWYAELNKRAFGKILKKLDKKVGTNQQMSTMKTRILPLQFANDSLITKDLSLLKTIWEQVTFRINSYERVMRSTSPNANANDNTEFFKIICVFIEEDDSKGLIRELTNLYSELSLIPTRIMISVLNKAALSKSLACIDAILKVIPSLNDSEDINRRNFFHHHIIAIGKLIRKQEILSRKKKSQPSKYTNSEGEIVTDLRTLHTTLSAPAESDSITEEEKSSACTLSYILEELPIHLRPCLFQHDNYKRTPLHYSCQYGLSEVTKLIIKLMKEWNIWNEIPIDDVSAFGDAESLTPLHLCVLGAHPKTTEVLLQSLDPNVKLKSSSLLHLATEWNNYPLLHVLLSSKRFDINYQDNELHETPLYLACRLNFFEAAVCLLYNGADLEIREKLFGWTAIFVAAAEGFTDIVKLLIANNANFDIEDEGGWTPMEHAVLRGHLHIADMVQIRDELVTHPHSQLNSGSEEKEPLNEISAGELNERNENGNGGNKGSLGKLAGPIKSYGHRFLDNNESLILITLGSNDTRNKSPSISLSSEALAKVIGLETDCALSLVISCNDSIDKSSVILDLPLDDNVDAVDFKVPFKVDYSHTLYFDIVPTYGTRSLETHNRIDCQKNNNNYVMARGVSMLNKSYSSVGVNRSILNGSVTVPIIANHTLEILGTLKFEYIIITPFEHPQLPLERTETYWKSLVSTRVIGHRGLGKNNPNKSLQIGENTVESFIMAASLGASYVEFDVQLTKDNVPVVYHDFLVAETGVDIPMHELTLEQFLDLNNADKEHIQRGAGHSPHHVNGADTALQKYRGRSVDDSDVSTLRRAWDLHDNDPNGKSNNAHWSDNRMRLTKTFKKNNFKGNARGHSIASSFVTLKELFKKIPANVGFNIECKFPMLDEAEEEELGQIMMEMNHWVDTVLKVVFDNANGRDIIFSSFHPDICIMLSLKQPVIPILFLTEGGSEQMADLRASSLQNGIRFAKKWNLLGIVSAAAPILKAPRLVQVVKSNGLVCVTYGVDNNDPENASIQIEAGVDAVIVDSVLAIRRGLTKKNEK
Protein: MAP kinase-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 1) (MAPK signal-integrating kinase 1) (Mnk1) (O08605)
Organism: Mus musculus (Mouse)
Function: May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Eukaryotic translation initiation factor 4E type 1B
- MAP kinase-interacting serine/threonine-protein kinase 2
- Cyclic AMP-dependent transcription factor ATF-4
- Eukaryotic translation initiation factor 4E type 2
- Mitogen-activated protein kinase 14
- Neuronal migration protein doublecortin
Sequence:
MVSSQKLEKPIEMGSSEPLPIVDSDKRRKKKRKTRATDSLPGKFEDVYQLTSELLGEGAYAKVQGAVNLQSGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNRNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKRKHFNEREASRVVRDVATALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGVKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFRDEATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRMCQNKLFESIQEGKYEFPDKDWAHISNEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPERGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEQEALAEGLCSMKLSPPSKSRLARRRALAQAGRSRDANPCLTPAGL