wanglab/gogpt-training-data huggingface dataset:
Protein: RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein) (Q9R1K8)
Organism: Rattus norvegicus (Rat)
Function: Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (By similarity). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses. May also function in differentiation of other cell types. Proto-oncogene, which promotes T-cell lymphomagenesis when its expression is deregulated (By similarity).
Subcellular location: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Found both in the cytosol and associated with membranes. Relocalization to the cell membrane upon activation is F-actin-dependent (By similarity). Translocates to the Golgi in response to phorbol ester or nerve growth factor (By similarity). Localizes to somata and dendrites but not to axons of hippocampal pyramidal cells. {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Ras-related protein Rap-1A
- GTPase NRas
- GTPase HRas
- RAS related 2
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- SOS Ras/Rho guanine nucleotide exchange factor 2
- SOS Ras/Rac guanine nucleotide exchange factor 1
Sequence:
MGTLGKAREAPRKPCHGSRAGPKGRLEAKSTNSPLPAQPSLAQITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIIISSAELLQKLMNLYKDALEKNSPGICLKICYFVRYWITEFWIMFKMDASLTSTMEEFQDLVKANGEESHCHLIDTTQINSRDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIHVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSCRNYDNYRRAYGECTHFKIPILGVHLKDLISLYEAMPDYLEDGKVNVQKLLALYNHINELVQLQDVAPPLDANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDLDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRSKSPAVSTENISSVVPMSTLCPLGTKDLLHAPEEGSFIFQNGEVVDHSEESKDRTIMLLGVSSQKISVRLKRTVAHKTTQTESFPWVGGEMPPGHFVLTSPRKSAQGALYVHSPASPCPSPALVRKRAFVKWENKESLIKPKPELHLRLRTYQELEQEVNTLRADNDALKIQLKYAQKQIESLQLGKSNHVLAQMDHGDGT
Protein: Ethylene-responsive transcription factor ERF084 (Q9M8M5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MENSYTVDGHRLQYSVPLSSMHETSQNSETYGLSKESPLVCMPLFETNTTSFDISSLFSFNPKPEPENTHRVMDDSIAAVVGENVLFGDKNKVSDHLTKEGGVKRGRKMPQKTGGFMGVRKRPWGRWSAEIRDRIGRCRHWLGTFDTAEEAARAYDAAARRLRGTKAKTNFVIPPLFPKEIAQAQEDNRMRQKQKKKKKKKVSVRKCVKVTSVAQLFDDANFINSSSIKGNVISSIDNLEKMGLELDLSLGLLSRK
Protein: Subtilisin-like protease SBT3.1 (EC 3.4.21.-) (Subtilase subfamily 3 member 1) (AtSBT3.1) (F4JJH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
Interaction partners:
- Lysine-specific demethylase JMJ28
- Transcription factor bHLH103
- Pentatricopeptide repeat-containing protein At4g21170
- Cysteine-rich receptor-like protein kinase 27
- Protein KINESIN LIGHT CHAIN-RELATED 2
- AT4g21620/F17L22_80
- Sugar transport protein 12
- Protein DETOXIFICATION 35
- B3 domain-containing transcription factor VAL3
- Receptor-like protein 12
Sequence:
MIQTLKTDSSFRLCFAAIAFGFVFIMNGKLSSGTTPHEFPVYIFYLGERKHDDPNLVTQSHLEILKSVLGSEEATNKSMVYSYHHGFSGFAAKLKPAEAEKLKKHPEVIILLENRKLGLQTTRTWDYLGQFSTPTSSKSLLHETNMGSGAIIGVIDSGIWSESGSFDDDGYGPIPKHWKGQCVSADQFSPADCNKKLIGAKYYIDGLNADLETSINSTTEYLSPRDHNGHGTQVSSTAAGSFVSNMTLLGLSSGSIMRGGAPKAHIAMYKACWDVEGGMCSVADVWKAFDEAIHDGVDVLSVSVGGSALKTLDVEIDIAIPALHAVNKGIPVVSPAGNEGSRSSSVINVSPWILTVAATTLDRSFSTLITLENNKTYLGQSLYTGPEISFTDVICTGDHSNVDQITKGKVIMHFSMGPVRPLTPDVVQKNGGIGLIYVRNPGDSRVECPVNFPCIYLDMEVGSELYTYIQTRSSMKIKISPYKTIIGESVASKVAKSSARGPSSFSPAILKPDIAAPGLTLLTPRIPTDEDTREFVYSGTSMATPVIAGIVALLKISHPNWSPAVIKSALVTTAMKTDPYGERLTVDGGNYKVADAFDYGGGLVNLEKATDPGLVYDMDINDYTHYLCSQTLYTDKKVSALTGNVNNKCPSSSSSILDLNVPSITIPDLKGTVNVTRTVTNVGRVKSVYKPVIEAPFGFNVVVSPKKLKFNKTRNKLAFTVTVSPGSHRVNTAFYFGSLTWSDKVHNVTIPISLRTRFIDNFFL
Protein: Monoglyceride lipase (H7C4E0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLQGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKDYSRILKHLMEKASRMLKFWIPRPFWVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP
Protein: Fibulin-5 (FIBL-5) (Developmental arteries and neural crest EGF-like protein) (Dance) (Embryonic vascular EGF repeat-containing protein) (EVEC) (Q9WVH8)
Organism: Rattus norvegicus (Rat)
Function: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN. Stabilizes and organizes elastic fibers in the skin, lung and vasculature. Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling. May act as an adapter that mediates the interaction between FBN1 and ELN.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9UBX5}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9UBX5}. Note=co-localizes with ELN in elastic fibers. {ECO:0000250|UniProtKB:Q9UBX5}.
Interaction partners:
- protein-lysine 6-oxidase
- Protein-lysine 6-oxidase
- Lysyl oxidase homolog 2
- Elastin
- Periostin
Sequence:
MPGLKRILTVTILALWLPHPGNAQQQCTNGFDLDRQTGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTSYSGPYPAAAPPVPASNYPTISRPLVCRFGYQMDEGNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNDDGRSCQDVNECETENPCVQTCVNTYGSFICRCDPGYELEEDGIHCSDMDECSFSEFLCQHECVNQPGSYFCSCPPGYVLLEDNRSCQDINECEHRNHTCTPLQTCYNLQGGFKCIDPIVCEEPYLLIGDNRCMCPAENTGCRDQPFTILFRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPRDIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF
Protein: ER membrane protein complex subunit 7 homolog (Q8VY97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 1
- Membrane magnesium transporter
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 8/9 homolog
- Uncharacterized protein family
Sequence:
MAPIFRSTSLIAFSLFFFFFASTLPISSGSEDSYTITGRVRVPASTVIGHAAKFSNIKVILNGGQHVTFLRPDGYFTFHKVPAGTHLIEVYALGYFFSPVRVDVSARHRGKVQATLTETRRSLTELVLEPLRAEQYYEMREPFSVMSIVKSPMGLMVGFMVVVVFLMPKLMENIDPEEMKSAQEQMRSQGVPSLTSLLPASR
Protein: Transposon Ty1-PL Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12414)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Cytochrome b6 (P0C315)
Organism: Oryza sativa (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00633}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00633}.
Interaction partners:
Sequence:
MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
Protein: Jonah 25Biii (EC 3.4.21.-) (RE34302p) (RH42519p) (Q9VMX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peptidase S1 domain-containing protein
- Jonah 99Fii
- Jonah 25Bi
- Jonah 44E, isoform A
- Venom allergen-1
- trypsin
- Zinc carboxypeptidase A 1
- Jonah 25Bii, isoform A
- trypsin
- Serine protease 3
Sequence:
MKVFLAILALAVASASAFDEKVFVKDLPKATKIEGRITNGYAAPEGKAPYTVGLGFSGGWWCGGSIIAHDWVLTAEHCIGDAASVIVYFGATWRTNAQFTHTVGNGNFIKHSNADIALIRIPHVDFWHMVNKVELPSYNDRYNNYNEWWAVACGWGGTYDGSPLPDWLQCVDLQIVHNEECGWTYGSVGDNVICTRTVDGKSICGGDSGGPLVTHDGSKLVGVSNFVSSNGCQSGAPAGFQRVTYHLDWIRDHTGISY
Protein: Neuron-specific vesicular protein calcyon (Q9NYX4)
Organism: Homo sapiens (Human)
Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
Subcellular location: Cytoplasmic vesicle membrane; Single-pass membrane protein. Cell membrane; Single-pass membrane protein.
Interaction partners:
- D
Sequence:
MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ
Protein: Interleukin-8 (Putative cxc chemokine) (Putative interleukin 8) (Q98TQ2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSIRMSASLVVVLLALLTITEGMSLRGMGADLRCRCIETESRRIGKLIKKVEMFPPSSHCRDTEIIATLSKSGQEICLDVSAPWVKRVIEKMLANNK
Protein: Epididymal-specific lipocalin-12 (Q6JVE5)
Organism: Homo sapiens (Human)
Function: Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Epididymal-specific lipocalin-9
Sequence:
MRLLCGLWLWLSLLKVLQAQTPTPLPLPPPMQSFQGNQFQGEWFVLGLAGNSFRPEHRALLNAFTATFELSDDGRFEVWNAMTRGQHCDTWSYVLIPAAQPGQFTVDHGVEPGADREETRVVDSDYTQFALMLSRRHTSRLAVLRISLLGRSWLLPPGTLDQFICLGRAQGLSDDNIVFPDVTGWSPQASVC
Protein: Germacrene A hydroxylase (EC 1.14.14.95) (Germacrene A oxidase) (TpGAO) (X2JI34)
Organism: Tanacetum parthenium (Feverfew) (Matricaria parthenium)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti-cancer drugs highly active against colon cancer cells. Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:D5JBW8}.
Interaction partners:
Sequence:
MALSLTTSIALATILFFVYKFATRSKSTKNSLPEPWRLPIIGHMHHLIGTIPHRGVMDLARKYGSLMHLQLGEVSTIVVSSPKWAKEILTTYDITFANRPETLTGEIVAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSLREEECWNLVQEIKASGSGRPVNLSENIFKLIATILSRAAFGKGIKDQKEFTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSIHQKLDNLINNLVAEHTVKTSSKTNETLLDVLLRLKDSAEFPLTADNVKAIILDMFGAGTDTSSATIEWAISELIKCPRAMEKVQVELRKALNGKERIHEEDIQELSYLNLVIKETLRLHPPLPLVMPRECRQPVNLAGYDIPNKTKLIVNVFAINRDPEYWKDAETFIPERFENSSTTVMGAEYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGASYDQIDMTESFGATVQRKTELLLVPSF
Protein: Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) (B7QK46)
Organism: Ixodes scapularis (Black-legged tick) (Deer tick)
Function: Responsible for the biosynthesis of pyroglutamyl peptides. Seems to have a preference for substrates with neutral or hydrophobic amino-acid residues at the second and third positions. Shows activity towards the peptides [Gln-1]-corazonin, [Gln-1]-periviscerokinin and [Gln-1]-sulfakinin.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MLFPVLLLLKLVIGALIIDASALSWHDLKWPRDLRPLAHHDLLYMGQISEEDRGDFNATLRNFLVPRVVGSQKHREVREFIVRSLKDLDWDVEEDCFDGQTPHGIKPFCNVIATLNPSACHRLVLACHYDSLLHKEGTFIGATDSAVPCAQLLYLARSLNGKLQNQKTRGDGLTLQLVFFDGEEAFERWSSHDSLYGSRHLAQKWHEDRTSAERLESCLERSEIANQIDRMEVMVLLDLLGAENPRFYSYFGETQPVYRRLVNIESRLNDAGLMELPRRRRRTNYFSNSSTVGFIEDDHIPFLKRSVPIVHIIPSPFPDVWHTLDDNEQNLHHPTISNLNKIFKAFVSEYLQL
Protein: Acid-sensing ion channel 4-A (ASIC4-A) (Acid-sensing ion channel 4.1) (Amiloride-sensitive cation channel 4-A) (ZASIC4.1) (Q708S4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14970195, ECO:0000269|PubMed:17686779}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPIEFVCKIKFAEEDEKQKGNQDGDKESLIEESCSPPTKDLAGFASASSLHGINHIFVSGRLGVRQTLWALAFLVSLALFLYQAAKCAISYLEHPHVTALNEEATPEMVFPAVTICNINRFRFSALTDADIYHLANLTGLPPKNKDGHKPTDLEYPAPDMQDIFNRTGHQLEEMLKSCNFSGQNCSAEDFTVVYTRYGKCYTFNGNKTTSRKTKQGGMGNGLEIMLDIQQDDYLPIWKETNETSLEAGIRVQIHSQDEPPYIHQLGFGVSPGFQTFVSCQEQRLTYLPQPWGNCRSTSEQMIPGYDTYSISACRLRCETLEVLRECKCRMVHMPGDANICTPSDIKCVDKALALLQKSSGDTCFCETPCNLTRYGKELSMVKIPSKGSARYLSRKYDKSEDYIRDNFLVLDIFFEALNYETIEQKKAYDVAGLLGDIGGQMGLFIGASVLTILEILDYVYEVIKHRLERLLRPQRDDKKQTQQQQQASTVATVNLEEMKAKDSSEMSRSHSEGAYANTILPNHHHHHRTHHRVSEDFAC
Protein: C2 domain-containing protein 2 (Transmembrane protein 24-like) (Q9Y426)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Rho GTPase-activating protein 10
- Rho GTPase-activating protein 26
Sequence:
MAMARLGSWLGEAQWLALVSLFVAALATVGLYLAQWALARARPQPQRRAVEPGEGPRPGSDALLSWILTLGSWRSQWQAAWVTALNEEAERKGGPPFLSFEEDPRQQALELVVQEVSSVLRSAEEKVVVCHVVGQAIQFLVSETPALGAGCRLYDMRLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEDQVAETSAMSDVLKDILKHLAGSASPSVVLITKPTTVKEAQNLQCAASTAQESCPPKPPRAHELKLLVRNIHVLLLSEPGASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFELNAKSKELHLQISEAGRSSEGLLATATVPLDLFKKQPSGPQSFTLTSGSACGSSVLGSVTAEFSYMEPGELKSWPIPPPVPAAKIEKDRTVMPCGTVVTTVTAVKTKPRVDVGRASPLSSDSPVKTPIKVKVIEKDISVQAIACRSAPVSKTLSSSDTELLVLNGSDPVAEVAIRQLSESSKLKLKSPRKKSTIIISGISKTSLSQDHDAALMQGYTASVDSTHQEDAPSHPERAAASAPPEEAESAQASLAPKPQEDELDSWDLEKEPQAAAWSSQVLLDPDGDELSESSMSVLEPGTAKKHKGGILRKGAKLFFRRRHQQKDPGMSQSHNDLVFLEQPEGSRRKGITLTRILNKKLLSRHRNKNTMNGAPVEPCT
Protein: Terminal uridylyl transferase 4 (E9PKX1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKNDESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDVNIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSAGNDMACLTTDLLTALGKIEPVFIPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWECNSSSATEKNSIAEENKAKADQPKDDTKKTETDNQSNAMKEKHGKSPLALETPNRVSLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKSTVDFKKREKGKISNKKPVKSNNMATNGCILLGETTEKINAEREQPVQCDEMDCTSQRCIIDNNNLLVNELDFADHGQDSSSLSTSKSSEIEPKLDKKQDDLAPSETCLKKELSQCNCIDLSKSPDPDKSTGTDCRSNLETESSHQSVCTDTSATSCNCKATEDASDLNDDDNLPTQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESL
Protein: Guanine nucleotide exchange factor subunit RIC1 (Connexin-43-interacting protein of 150 kDa) (Protein RIC1 homolog) (RAB6A-GEF complex partner protein 1) (Q4ADV7)
Organism: Homo sapiens (Human)
Function: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP, and may thereby be required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. Required for phosphorylation and localization of GJA1. Is a regulator of procollagen transport and secretion, and is required for correct cartilage morphogenesis and development of the craniofacial skeleton.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23091056}. Membrane {ECO:0000269|PubMed:23091056}.
Interaction partners:
- RAB6A-GEF complex partner protein 2
- Conserved oligomeric Golgi complex subunit 8
- Ras-related protein Rab-33B
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR5
- Ragulator complex protein LAMTOR4
- Ragulator complex protein LAMTOR2
- Ras-related protein Rab-6A
- Conserved oligomeric Golgi complex subunit 3
Sequence:
MYFLSGWPKRLLCPLGSPAEAPFHVQSDPQRAFFAVLAAARLSIWYSRPSVLIVTYKEPAKSSTQFGSYKQAEWRPDSTMIAVSTANGYILFFHITSTRGDKYLYEPVYPKGSPQMKGTPHFKEEQCAPALNLEMRKILDLQAPIMSLQSVLEDLLVATSDGLLHLIHWEGMTNGRKAINLCTVPFSVDLQSSRVGSFLGFTDVHIRDMEYCATLDGFAVVFNDGKVGFITPVSSRFTAEQLHGVWPQDVVDGTCVAVNNKYRLMAFGCVSGSVQVYTIDNSTGAMLLSHKLELTAKQYPDIWNKTGAVKLMRWSPDNSVVIVTWEYGGLSLWSVFGAQLICTLGGDFAYRSDGTKKDPLKINSMSWGAEGYHLWVISGFGSQNTEIESDLRSVVKQPSILLFQFIKSVLTVNPCMSNQEQVLLQGEDRLYLNCGEASQTQNPRSSSTHSEHKPSREKSPFADGGLESQGLSTLLGHRHWHVVQISSTYLESNWPIRFSAIDKLGQNIAVVGKFGFAHYSLLTKKWKLFGNITQEQNMIVTGGLAWWNDFMVLACYNINDRQEELRVYLRTSNLDNAFAHVTKAQAETLLLSVFQDMVIVFRADCSICLYSIERKSDGPNTTAGIQVLQEVSMSRYIPHPFLVVSVTLTSVSTENGITLKMPQQARGAESIMLNLAGQLIMMQRDRSGPQIREKDSNPNNQRKLLPFCPPVVLAQSVENVWTTCRANKQKRHLLEALWLSCGGAGMKVWLPLFPRDHRKPHSFLSQRIMLPFHINIYPLAVLFEDALVLGAVNDTLLYDSLYTRNNAREQLEVLFPFCVVERTSQIYLHHILRQLLVRNLGEQALLLAQSCATLPYFPHVLELMLHEVLEEEATSREPIPDPLLPTVAKFITEFPLFLQTVVHCARKTEYALWNYLFAAVGNPKDLFEECLMAQDLDTAASYLIILQNMEVPAVSRQHATLLFNTALEQGKWDLCRHMIRFLKAIGSGESETPPSTPTAQEPSSSGGFEFFRNRSISLSQSAENVPASKFSLQKTLSMPSGPSGKRWSKDSDCAENMYIDMMLWRHARRLLEDVRLKDLGCFAAQLGFELISWLCKERTRAARVDNFVIALKRLHKDFLWPLPIIPASSISSPFKNGKYRTVGEQLLKSQSADPFLNLEMDAGISNIQRSQSWLSNIGPTHHEIDTASSHGPQMQDAFLSPLSNKGDECSIGSATDLTESSSMVDGDWTMVDENFSTLSLTQSELEHISMELASKGPHKSQVQLRYLLHIFMEAGCLDWCIVIGLILRESSIINQILVITQSSEVDGEMLQNIKTGLHAVDRWASTDCPGYKPFLNIIKPQLQKLSEITEEQVQPDAFQPITMGKTPEQTSPRAEESRGSSSHGSIPQGEVGSSNMVSRKEEDTAQAEEEEPFQDGTYDCSVS
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI) (O95450)
Organism: Homo sapiens (Human)
Function: Cleaves the propeptides of type I and II collagen prior to fibril assembly (By similarity). Does not act on type III collagen (By similarity). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form with reduced collagen-binding activity.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen and calcium-binding EGF domain-containing protein 1
- EGF-containing fibulin-like extracellular matrix protein 2
- Collagen alpha-1
- Collagen alpha-2
- Fibulin-5
- V-type proton ATPase 116 kDa subunit a 2
- Protein-lysine 6-oxidase
Sequence:
MDPPAGAARRLLCPALLLLLLLLPPPLLPPPPPPANARLAAAADPPGGPLGHGAERILAVPVRTDAQGRLVSHVVSAATSRAGVRARRAAPVRTPSFPGGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLGSCLYVGDVAGLAEASSVALSNCDGLAGLIRMEEEEFFIEPLEKGLAAQEAEQGRVHVVYRRPPTSPPLGGPQALDTGASLDSLDSLSRALGVLEEHANSSRRRARRHAADDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIEIGNPSQSLENVCRWAYLQQKPDTGHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLLDDPFAHDWPALPQLPGLHYSMNEQCRFDFGLGYMMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTMCAPGKHCFKGHCIWLTPDILKRDGSWGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCPDSLADFREEQCRQWDLYFEHGDAQHHWLPHEHRDAKERCHLYCESRETGEVVSMKRMVHDGTRCSYKDAFSLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHCKVVKGTFTRSPKKHGYIKMFEIPAGARHLLIQEVDATSHHLAVKNLETGKFILNEENDVDASSKTFIAMGVEWEYRDEDGRETLQTMGPLHGTITVLVIPVGDTRVSLTYKYMIHEDSLNVDDNNVLEEDSVVYEWALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKAIRRACNPQECSQPVWVTGEWEPCSQTCGRTGMQVRSVRCIQPLHDNTTRSVHAKHCNDARPESRRACSRELCPGRWRAGPWSQCSVTCGNGTQERPVLCRTADDSFGICQEERPETARTCRLGPCPRNISDPSKKSYVVQWLSRPDPDSPIRKISSKGHCQGDKSIFCRMEVLSRYCSIPGYNKLCCKSCNLYNNLTNVEGRIEPPPGKHNDIDVFMPTLPVPTVAMEVRPSPSTPLEVPLNASSTNATEDHPETNAVDEPYKIHGLEDEVQPPNLIPRRPSPYEKTRNQRIQELIDEMRKKEMLGKF