wanglab/gogpt-training-data huggingface dataset:
Protein: Claspin (Q8IRB5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for checkpoint signaling in response to DNA replication stress; either resulting from normal embryogenesis or induced by the DNA synthesis inhibitor hydroxyurea (HU). It is not required for the G2 arrest resulting from DNA double strand breaks induced by ionizing irradiation (IR). Necessary for the timely phosphorylation of Cdk1 at the mid-blastula transition. May have a minor role in maintaining genomic stability in mitotic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:22796626}.
Interaction partners:
- Timeout
- Protein timeless
- CDC45L
- Serine/threonine-protein kinase grp
- DNA replication licensing factor Mcm2
- Replication protein A 70 kDa DNA-binding subunit
- Mutagen-sensitive 101
- GEO08380p1
- Chromosome transmission fidelity 4
- DNA polymerase epsilon catalytic subunit 1
Sequence:
MSESLAETAAAAENEEQADDSMEKLVFDEEDEQMVSGEDLLGGKSLIMSDDSEAEDGSQEKPLSPKDRRRRMMDSDQEEDAMDQGNGDSIKNSEDVEEEMVSRPKKKVSAIIDSDNDDEQQAEKKTQKEEGKQPVKSKKKRSQVNQEDQEKPVKSNKTKKAVKNKTQANKAEDDQDNPSKEDKPKKVVKNKKQTNKDGKPQTNEEYDHHQQHEKPAKTQKSKKLAKKQKQQEDDKEDNGTEQEKKKPSPKSKAKKSDKSKIDSLMDNEEDAGEDLKMYQEDQEPQKQKTKKSAKKTNKDSKEESGEDQEHQEQKKPLKKIKLDNIDTKEDKEQIVKPKKMAKKNKQKVLSDDESEENQNEKVDQDHDLKKMSSENELEMGSDKEDQEMQEPPKKAKKNKQRMDSESEDEIPKTESEKITSSPKNKLKGLVDSESEPEETAEEVSPVKNKLKGLVDSESEPELDNPEESAGEQEAPMESALSREKPKKAKVVRESAKKALEGMQAIQSEQQRLHREAHINVPYHQPKPRTLKEFLSRRTINAPLATALAGGSPMPSRQPRKSVGLRMTREELEAYAKLMEDRAKEATEFFKSESESDEEDDSENEEPMELKDNPGVMDEMLDNPKTPEQPKNDTEDMTSQAVIEVPVLGEDKTDDTVGDEAMVADSITEEEPIASTSTAAALKLADNFEIQQETNAKSPSKVCLVTEVVELPKLDLSTINITPSSKPATPKISEVIRQLKIEKSLDESPSLKGDPNMVIDLETGDMFAKKPTGVDDLLNRLMKTREAKKHKTTETVNILTTEHGKLEMSKVSIHLHEEEIAKEPKPGAGYMKMQEHLKTLITKKRMEDLRKKQAEEQEKMAEDEEEGMDVDEEYEPEDKPGYAEVTINEDEEIIDKVDSTAEDDGDAEENKNDADEDPEDNPVEDSEDEKNDSESEQECEANPEPETQTRKKNRIIKAFEDDNSDEDDLDLLQTPKPSNVAPITATQLQLSAHKLFDVETRRTASDEENELLDLCSGQFPQTQMLSSDAPSVDTAVISQIPMTQFGGSSQAADELEGLCSGTFATQLPSQAPTQQPEQQEESEVPAAVANRIVSSDEEAQEDALEVDKPRNKKLTKKRPKKKAKLGFSDDEDSDDEVEEFDEESDAEPVEEIPETFVDYDSEENEIVVEMTKKDRKIRAANFVDKEAELSESEWGSADEDEKNMDEYDIELGDEDQFDRDKLRHELGQIHARKMMDQDIREVRKIKELLFEEEEEGANRQRQFRWKNVEAGFSLDDNRTDNGEGNDGSGDEENEHLWRKIRYEREQLLLEKGLKPEVASPLSTSVINTSNNGNSPAIRRLNIISSKKTTVEVKKNSPFLISKTIAGKQQKSAVRGSFLIRDQQTLSKLAGLTKGTSGDVDAAEGTISVKSAKAKNFVFATLTEEEHENRKRKAADILNSSTETGVNFIKKPKLEPRRDKCLIDQLL
Protein: Peptidyl-lysine N-acetyltransferase YjaB (EC 2.3.1.-) (KAT) (P09163)
Organism: Escherichia coli (strain K12)
Function: N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Binds acetyl-CoA.
Interaction partners:
- [Ribosomal protein bS18]-alanine N-acetyltransferase
- Aminoalkylphosphonate N-acetyltransferase
- Peptidyl-lysine N-acetyltransferase PatZ
- Uncharacterized N-acetyltransferase YhbS
- Uncharacterized N-acetyltransferase YafP
- Protein ElaA
- Uncharacterized N-acetyltransferase YjgM
- Probable acyltransferase FabY
- L-amino acid N-acyltransferase MnaT
- Acetyltransferase YpeA
Sequence:
MVISIRRSRHEEGEELVAIWCRSVDATHDFLSAEYRTELEDLVRSFLPEAPLWVAVNERDQPVGFMLLSGQHMDALFIDPDVRGCGVGRVLVEHALSMAPELTTNVNEQNEQAVGFYKKVGFKVTGRSEVDDLGKPYPLLNLAYVGA
Protein: TOM1-like protein 4 (Q6NQK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might contribute to the loading of the ESCRT machinery.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22639582}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Protein ELC-like
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Auxilin-related protein 1
- Protein ELC
Sequence:
MANDAAACAERATNDMLIGPDWAINIELCDLINMDPSQAKEAVKVLKKRLGSKNSKVQILALYALETLSKNCGENVYQLIIDRGLLNDMVKIVKKKPELNVREKILTLLDTWQEAFGGRGGRYPQYYNAYNDLRSAGIEFPPRTESSLSFFTPPQTQPDEDAAIQASLQGDDASSLSLEEIQSAEGSVDVLMDMLGAHDPGNPESLKEEVIVDLVEQCRTYQRRVMTLVNTTTDEELLCQGLALNDNLQHVLQRHDDIANVGSVPSNGRNTRAPPPVQIVDINHDDEDDESDDEFARLAHRSSTPTRRPVHGSDSGMVDILSGDVYKPQGNSSSQGVKKPPPPPPHTSSSSSSPVFDDASPQQSKSSEVIRNLPPPPSRHNQRQQFFEHHHSSSGSDSSYEGQTRNLSLTSSEPQKEEKPEDLLFKDLVEFAKTRSSKANNNNRSL
Protein: Osteomodulin (Keratan sulfate proteoglycan osteomodulin) (KSPG osteomodulin) (Osteoadherin) (OSAD) (Q99983)
Organism: Homo sapiens (Human)
Function: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Mimecan
- Asporin
- Prolargin
- Fibromodulin
- Lumican
- Aggrecan core protein
- Extracellular matrix protein 2
Sequence:
MGFLSPIYVIFFFFGVKVHCQYETYQWDEDYDQEPDDDYQTGFPFRQNVDYGVPFHQYTLGCVSECFCPTNFPSSMYCDNRKLKTIPNIPMHIQQLYLQFNEIEAVTANSFINATHLKEINLSHNKIKSQKIDYGVFAKLPNLLQLHLEHNNLEEFPFPLPKSLERLLLGYNEISKLQTNAMDGLVNLTMLDLCYNYLHDSLLKDKIFAKMEKLMQLNLCSNRLESMPPGLPSSLMYLSLENNSISSIPEKYFDKLPKLHTLRMSHNKLQDIPYNIFNLPNIVELSVGHNKLKQAFYIPRNLEHLYLQNNEIEKMNLTVMCPSIDPLHYHHLTYIRVDQNKLKEPISSYIFFCFPHIHTIYYGEQRSTNGQTIQLKTQVFRRFPDDDDESEDHDDPDNAHESPEQEGAEGHFDLHYYENQE
Protein: Mitochondrial potassium channel ATP-binding subunit (ATP-binding cassette sub-family B member 8, mitochondrial) (Mitochondrial sulfonylurea-receptor) (Q9BL17)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Iron-sulfur clusters transporter ABCB7, mitochondrial
Sequence:
MSILSKLSQISIKSAVQSSKHCFSSYPWLHKPISRTTILKTWRICGFGAGLGAVTLRKAACAPKLSKRIDHLRTTEDQNASMTAGELWNLIKPFFGWFFAAVVCAILSAYINIQIPLCLGDLVNGIVKIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVLQFSRLEPSIPMDTGVCIPYHSLWGDIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEAHNVDS
Protein: Recombination initiation defects 3 (F4HU48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKMNINKACDLKSISVFPPNLRRRSAEPQASQQLRSQQSQQSFSQGPSSSQRGCGGFSQMTQSSIDELLINDQRFSSQERDLSLKKVSSCLPPINHKREDSQLVASRSSSGLSRRWSSASIGESKLAQISEELEQRFGMMETSLSRFGMMLDSIQSDIMQANRGTKEVFLETERIQQKLTLQDTSLQQLRKEQADSKASLDGGVKFILEEFSKDPNQEKLQKILQMLTTIPEQVETALQKIQREICHTFTREIQVLASLRTPEPRVRVPTAPQVKAKENLPEQRGQAAKVLTSLKMPEPRVQVPAAPQAKENFPEQRGPVAKSNSFCNTTLKTKQPQFPRNPNDASARAVKPYLSPKIQVGCWKTVKPEKSNFKKRATRKPVKSESTRTQFEQCSVVIDSDEEDIDGGFSCLINENTRGTNFEWDAEKETERILRTARRTKRKFGNPIIIN
Protein: Fibrinogen C-terminal domain-containing protein (Q18705)
Organism: Caenorhabditis elegans
Interaction partners:
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- F-box domain-containing protein
- F-box domain-containing protein
- VWFA domain-containing protein
- CUB_2 domain-containing protein
- VWFA domain-containing protein
- C-type lectin domain-containing protein
- Uncharacterized protein T25D10.1
- F-box domain-containing protein
Sequence:
MSKETVSLLLTFACGILVSADTSQYFQVLIREIDNPSGNIFDGTSCSPFRFTGYGCNTYLTGGVAAGPTLNNSFTNTQLNFHGETKIDNLNLIVNDIYAKDVSEFTGFSVSFILKTADGGIIDEYSFRVNTTENQGVYVYNSVRPGTLSTTISIAWATNIPPPSETTTTEITGTTPTPGPTEPPTTTAKLPSDCDEVESTSSGLQTIYPDGSTPVSVYCDRKNSAGAYTIIQSRGREGSNITFDIPFANYSDWFGESGVGKNFWLGLDNMNNLSTNGKTYSLQIDLCCGTQLMAKQLYTNFKVATKAEQYALTASADLPGIGLDYSSSAKDLGAPFSTQLTYSLPKGKAECDQFEFYDDDNGGAGPSKGYGGWWYGSCGNNLNGFLYPNNNGDCSVTKFDSTLLLGINMRTTTGTATGGYDVDLISYDRVRMALFTFDTTLIDRTDSSFCN
Protein: Cholesterol 7-desaturase (EC 1.14.19.21) (Cholesterol desaturase daf-36) (Rieske oxygenase DAF-36/Neverland) (DAF-36/NVD) (Q17938)
Organism: Caenorhabditis elegans
Function: Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. This reaction is the first step in the synthesis of the steroid hormone Delta(7)-dafachronic acid (one of the principal steroid hormones in nematodes). Dafachronic acids bind directly to the nuclear hormone receptor (NHR) daf-12, suppressing dauer formation and inducing reproductive growth.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- 2Fe-2S ferredoxin-type domain-containing protein
- 3-ketosteroid oxygenase
- 3beta-hydroxysteroid dehydrogenase dhs-16
- 3beta-hydroxysteroid dehydrogenase/Delta
- Nuclear hormone receptor family member daf-12
- Cytochrome-b5 reductase
- NADH-cytochrome b5 reductase
- NADH-cytochrome b5 reductase
- fumarate reductase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MLLEQIWGFLTAHPISVVTTILIVYLIHITLKPLNRVRRLGDVGLFFGKPELKGFYRERQLERLKLLRRVGDMPPVFPNGWYCVCESEKLANNQIMEITVLGQFLSLIRSESGAVYITDSYCPHIGANFNIGGRVVRDNCIQCPFHGWIFSAETGKCVEVPYDEGRIPEQAKVTTWPCIERNNNIYLWYHCDGAEPEWEIPEITEITDGFWHLGGRTEHEVMCHIQEIPENGADIAHLNYLHKSAPPVTKGSDIIKTDLSDPQPAVQHVWDGKWEVKSEEDRHCGVMHLNQFMTFWGYKVPLTSSKLVAEQHGPGIVHMLFDFGIWGKGVVFQTVTPEEALLQRVRFRIFSNIPWFFVKFFMTVEAMQFERDVFIWSNKKYIKSPLLVKNDGPIQKHRRWFSQFYTENSPKMLKDGSLSNQAKSIFDW
Protein: Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin-like domain-containing leucine-rich transmembrane protein 3) (Q70AK3)
Organism: Xenopus laevis (African clawed frog)
Function: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (By similarity). Modulates cadherin-dependent cell-cell adhesion and cell sorting. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development. Plays a role in cell-cell adhesion via its interaction with latrophilins that are expressed at the surface of adjacent cells. Mediates axon attraction towards cells expressing ntn1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with unc-5 family members. Plays a role in the regulation of the density of glutamaergic synapses (By similarity). Plays a role in signaling cascades downstream of fgfr1, and possibly also other fgfr family members. Plays a role in embryonic morphogenesis, but not in embryonic patterning.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14688794, ECO:0000305|PubMed:19492039}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1}.
Interaction partners:
Sequence:
MSTETWNLFVAWAQFLLLLRMLPQCDSAKPCPSVCRCDAGFIYCNDRDLTSIPSGIPDDATTLYLQNNQINNAGIPSDLKGLDKVERIYLYRNSLDEFPINLPKNVKELHLQENNIRTITYDALLQIPFIEELHLDDNSVSAVSIEDGAFRDNIFLRLLFLSRNHLSTIPWGLPKTIEELRLDDNRISTISEISLQDLTNLKRLVLDGNLLNNNGLGERVFMNLINLTELSLVRNSLTSPPANLPGTSLRKLYLQENHMNYVPPNSFADLTQLYRLDMSNNNLTALPQGIFDDLDNLTQLFLRNNPWYCGCKMKWVRDWLQSLPSKVNVRGLMCQAPERVRGMTIKDLNKELFDCKDRIGSNTIHVTTTMLNSLLPAQGQWPVPVTKQPEIRPPDINKIFRTTPIPVKKIITIQVKSITTETIYISWKVALPMTALRLSWQLGHSPVFGSITETIVTGDRAEYLLTALEPESPYRICMVPMETGNIYLSDETPVCIETETAPLKMYNPTTTLNREQEKEPYKNSSLPLAAIIGGAVALVAITLLALVCWYVHRNGSLFSRNCAYNKGRRRKDDYAEAGTKKDNSILEIRETSFPMIPINSDPLSKEEFIIHTIFPPNGVSLYKNSHSESSSNRSYRDSGIPDSDHSHS
Protein: Covalently-linked cell wall protein 14 (Inner cell wall protein) (O13547)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the inner layer of the cell wall.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Covalently-linked cell wall protein 12
- Cell wall protein CWP1
- Glucan 1,3-beta-glucosidase
- Cell wall mannoprotein PST1
- Protein YGP1
- Cell wall mannoprotein HSP150
Sequence:
MRATTLLSSVVSLALLSKEVLATPPACLLACVAQVGKSSSTCDSLNQVTCYCEHENSAVKKCLDSICPNNDADAAYSAFKSSCSEQNASLGDSSSSASSSASSSSKASSSTKASSSSASSSTKASSSSASSSTKASSSSAAPSSSKASSTESSSSSSSSTKAPSSEESSSTYVSSSKQASSTSEAHSSSAASSTVSQETVSSALPTSTAVISTFSEGSGNVLEAGKSVFIAAVAAMLI
Protein: N-terminal acetyltransferase A complex catalytic subunit ARD1 (NatA complex subunit ARD1) (EC 2.3.1.255) (Arrest-defective protein 1) (P07347)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- N-alpha-acetyltransferase NAT5
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase A complex subunit NAT1
- N-terminal acetyltransferase B complex subunit MDM20
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-terminal acetyltransferase B complex catalytic subunit NAT3
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL31A
- Large ribosomal subunit protein uL3
Sequence:
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQDENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV
Protein: C-C motif chemokine 8 (HC14) (Monocyte chemoattractant protein 2) (Monocyte chemotactic protein 2) (MCP-2) (Small-inducible cytokine A8) [Cleaved into: MCP-2(6-76)] (P80075)
Organism: Homo sapiens (Human)
Function: Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils. May play a role in neoplasia and inflammatory host responses. This protein can bind heparin. The processed form MCP-2(6-76) does not show monocyte chemotactic activity, but inhibits the chemotactic effect most predominantly of CCL7, and also of CCL2 and CCL5 and CCL8.
Subcellular location: Secreted.
Interaction partners:
- C-X-C motif chemokine 10
- C-C motif chemokine 2
- C-X-C motif chemokine 11
- C-C chemokine receptor type 1
- C-C chemokine receptor type 5
- C-C chemokine receptor type 2
- C-X-C motif chemokine 2
- C-C motif chemokine 13
- Interleukin-8
- Platelet basic protein
Sequence:
MKVSAALLCLLLMAATFSPQGLAQPDSVSIPITCCFNVINRKIPIQRLESYTRITNIQCPKEAVIFKTKRGKEVCADPKERWVRDSMKHLDQIFQNLKP
Protein: Small ribosomal subunit protein eS27y (40S ribosomal protein S27-2) (Q9M2F1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the elimination of damaged mRNA after UV irradiation.
Interaction partners:
- Small ribosomal subunit protein uS15y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS21y
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS28z/eS28y
- Large ribosomal subunit protein uL18z
- Small ribosomal subunit protein eS7y
- Large ribosomal subunit protein uL3z
Sequence:
MVLQNDIDLLNPPAELEKRKHKLKRLVQSPNSFFMDVKCQGCFNITTVFSHSQTVVVCGNCQTILCQPTGGKAKLTEGCSFRRKGD
Protein: Cilia- and flagella-associated protein 52 (WD repeat-containing protein 16) (F1SS88)
Organism: Sus scrofa (Pig)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). Important for proper ciliary and flagellar beating. May act in cooperation with CFAP45 and axonemal dynein subunit DNAH11. May play a role in cell growth and/or survival (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N1V2}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8N1V2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q5F201}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q8N1V2}.
Interaction partners:
- EF-hand domain containing 1
- Parkin coregulated
- Tektin
- Tektin
- Methyl-CpG binding domain protein 1.
- Tektin
- Protein Flattop
- EF-hand domain-containing family member C2
- Coiled-coil domain-containing protein 114 isoform X2
- Ankyrin repeat domain containing 50
Sequence:
MENQIQPKAEVAKLELEAVIGFNGHVPTGLKCHPDQEHLIYPLGCTILIQAIKTQEQNFLHGHSNNVSCVTISKSGVYIASGQVTFMGFKADIILWDYKKRELMARLSLHKGKIEALAFSPNDLYLVSLGGPDDGSVVVWSIAKTEAICGSPAAGLNVGNATSVVFSQCHDEMFVTAGNGTIRVWELDLPNRKIWPTECQTGQMKRIVMSISMASDDSFFYLGTTTGDILKMNPRTKLLADTGPAKDKFSLGVSAIKCLKTGGLLVGSGAGLLVFCRSPSYKPIKKIQLQGGITSISLRGEGHQFFVGTEESHIYRVNFTDFKETLVTTCHFEAVEDVVFPFGTAELFATCAKKDIRVWHTLSNRELLRITVPNMTCHGIDFMRDGKSLISAWDDGKIRAFAPETGRLMYVISNAHRIGVTAVATTSDCTRVISGGGEGEVRVWQIGHQTQKLEEALKEHKSSVSCIRVKKNNEECVTASTDGTCIIWDLVRLRRNQMILANTLFQCVCYHPEEFQIITSGTDRKIAYWEVFDGSGIRELDGSLSGSINGMDITPEGVHFVTGGNDHLVKVWDYNEGEVTHVGVGHSGNITRVRISPGNEYIVSVSADGAILRWKYPFPS
Protein: Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease mppa-1) (Q95XN2)
Organism: Caenorhabditis elegans
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P20069}.
Interaction partners:
- Mitochondrial-processing peptidase subunit beta
- Cytochrome c domain-containing protein
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 7
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 4
Sequence:
MLLRKSIPYIKICRDISASVRNNKEIAQKLPLSVPLPMENNSKSIEKGCPPMGRNSRVTRLPNGLKVCTEDTYGDFVTVGVAIESGCRYENGFPFGISRIVEKLAYNSSESFSSRDEVFAKLEENSGIVDCQSTRDTMMYAASCHRDGVDSVIHVLSDTIWKPIFDEQSLEQAKLTVSYENQDLPNRIEAIEILLTDWIHQAAFQNNTIGYPKFGNNSMDKIRVSDVYGFLSRAHTPQRMVVGGVGVGHDEFVSIISRHFDLNKSTWTTQPTVLPAKIPEIDESRAQYTGGELRLDTDLTKLTIGKPYPLLSHVVLGLEGCSYKDEDFVAFCVLQSLLGGGGAFSAGGPGKGMYARMYTELMNRHHWIYSAIAHNHSYSDSGVFTVTASSPPENINDALILLVHQILQLQQGVEPTELARARTQLRSHLMMNLEVRPVLFEDMVRQVLGHGDRKQPEEYAEKIEKVTNSDIIRVTERLLASKPSLVGYGDIKKLKDLRSLDQAVAKRDLKYLFN
Protein: Guanine nucleotide-binding protein subunit beta-1 (P26308)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Interaction partners:
- G protein alpha o subunit subunit alpha 47A)
- Guanine nucleotide-binding protein subunit gamma-1
- G protein alpha i subunit subunit alpha 65A)
- G protein alpha s subunit subunit alpha)
- Latrophilin Cirl
- Guanine nucleotide-binding protein subunit gamma-e
- Guanine nucleotide-binding protein subunit alpha homolog
- Phosducin-like protein 1
- Guanine nucleotide-binding protein subunit alpha
- G protein alpha q subunit subunit alpha)
Sequence:
MNELDSLRQEAESLKNAIRDARKAACDTSLLQAATSLEPIGRIQMRTRRTLRGHLAKIYAMHWGNDSRNLVSASQDGKLIVWDSHTTNKVHAIPLRSSWVMTCAYAPSGSYVACGGLDNMCSIYNLKTREGNVRVSRELPGHGGYLSCCRFLDDNQIVTSSGDMSCGLWDIETGLQVTSFLGHTGDVMALSLAPQCKTFVSGACDASAKLWDIREGVCKQTFPGHESDINAVTFFPNGQAFATGSDDATCRLFDIRADQELAMYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTMKAERSGILAGHDNRVSCLGVTENGMAVATGSWDSFLRVWN
Protein: Antimicrobial protein 1 (A1YV58)
Organism: Scylla serrata (Mud crab)
Function: Has antibacterial activity against the Gram-positive bacteria E.coli (MIC<50 ug/ml) and P.aeruginosa (MIC<25 ug/ml), and the Gram-negative bacteria S.aureus (MIC<100 ug/ml) and S.pyogenes (MIC<50 ug/ml).
Subcellular location: Secreted {ECO:0000269|PubMed:19219229}.
Interaction partners:
Sequence:
MRSSLLLGLTVVLLLGVTVPPCMAGQALNKLMPKIVSAIIYMIGQPNAGVTFLGHQCLVESTRQPDGFYTAKMWCTSWTSDNPIVGEGRSRVELEALKGSIRNFVQTASDYKKFTIEEVEDWIASY
Protein: Auxin-responsive protein IAA12 (Indoleacetic acid-induced protein 12) (Protein BODENLOS) (Q38830)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Auxin response factor 5
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Protein TOPLESS
- Auxin response factor 7
- Auxin transporter protein 1
- Corepressor
- Auxin response factor 18
- Auxin response factor 3
- Auxin response factor 9
- Auxin response factor 1
Sequence:
MRGVSELEVGKSNLPAESELELGLGLSLGGGAWKERGRILTAKDFPSVGSKRSAESSSHQGASPPRSSQVVGWPPIGLHRMNSLVNNQAMKAARAEEGDGEKKVVKNDELKDVSMKVNPKVQGLGFVKVNMDGVGIGRKVDMRAHSSYENLAQTLEEMFFGMTGTTCREKVKPLRLLDGSSDFVLTYEDKEGDWMLVGDVPWRMFINSVKRLRIMGTSEASGLAPRRQEQKDRQRNNPV
Protein: Dolichol-phosphate mannosyltransferase (EC 2.4.1.83) (Dolichol-phosphate mannose synthase) (DPM synthase) (Dolichyl-phosphate beta-D-mannosyltransferase) (Mannose-P-dolichol synthase) (MPD synthase) (P14020)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15657391}; Cytoplasmic side {ECO:0000269|PubMed:15657391}.
Interaction partners:
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichol kinase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Mannose-1-phosphate guanyltransferase
- Dolichyldiphosphatase
- Dehydrodolichyl diphosphate synthase complex subunit RER2
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
- Dehydrodolichyl diphosphate synthase complex subunit SRT1-farnesyl diphosphate specific))
- Phosphomannomutase
Sequence:
MSIEYSVIVPAYHEKLNIKPLTTRLFAGMSPEMAKKTELIFVDDNSQDGSVEEVDALAHQGYNVRIIVRTNERGLSSAVLKGFYEAKGQYLVCMDADLQHPPETVPKLFESLHDHAFTLGTRYAPGVGIDKDWPMYRRVISSTARMMARPLTIASDPMSGFFGLQKKYLENCNPRDINSQGFKIALELLAKLPLPRDPRVAIGEVPFTFGVRTEGESKLSGKVIIQYLQQLKELYVFKFGANNLILFITFWSILFFYVCYQLYHLVF