UniProt ID | CL190_DROME | |
---|---|---|
UniProt AC | Q9VJE5 | |
Protein Name | Restin homolog | |
Gene Name | CLIP-190 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1690 | |
Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton . Golgi apparatus . Microtubule-associated. Lva-CLIP-190 complexes are found at the Golgi. | |
Protein Description | Together CLIP-190 and jar may coordinate the interaction between the actin and microtubule cytoskeleton. May link endocytic vesicles to microtubules. May play a role in formation of furrows during cellularization.. | |
Protein Sequence | MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYTDNSSAVLTANTEQFIIGQRVWLGGTRPGQIAFIGDTHFAAGEWAGVVLDEPNGKNDGCVSGKRYFQCEPKRGIFSRLTRLTTYPLAGAQTPTSPLAKSSPDRSRTVSPTASIRSSMLRSPGIGGKNGMAVGDRVIVSSGFGSRPGILRYLGETQFAPGNWCGVELDEPSGKNDGTVDDIRYFECKPKYGVFVPIAKVSLSPSSKKTRLSRTGSRESLTSIGTMNSIATTATSRMRMNAQQRKSSTPVKPILATPKSQFSMQDLLREKQQHVEKLMVERDLDREDAQNQALQLQKNINELKARIVELESALDNERKKTEELQCSIDEAQFCGDELNAQSQVYKEKIHDLESKITKLVSATPSLQSILPPDLPSDDGALQEEIAKLQEKMTIQQKEVESRIAEQLEEEQRLRENVKYLNEQIATLQSELVSKDEALEKFSLSECGIENLRRELELLKEENEKQAQEAQAEFTRKLAEKSVEVLRLSSELQNLKATSDSLESERVNKTDECEILQTEVRMRDEQIRELNQQLDEVTTQLNVQKADSSALDDMLRLQKEGTEEKSTLLEKTEKELVQSKEQAAKTLNDKEQLEKQISDLKQLAEQEKLVREMTENAINQIQLEKESIEQQLALKQNELEDFQKKQSESEVHLQEIKAQNTQKDFELVESGESLKKLQQQLEQKTLGHEKLQAALEELKKEKETIIKEKEQELQQLQSKSAESESALKVVQVQLEQLQQQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKSGHLLEQITKLKSEVGETQAALSSCHTDVESKTKQLEAANAALEKVNKEYAESRAEASDLQDKVKEITDTLHAELQAERSSSSALHTKLSKFSDEIATGHKELTSKADAWSQEMLQKEKELQELRQQLQDSQDSQTKLKAEGERKEKSFEESIKNLQEEVTKAKTENLELSTGTQTTIKDLQERLEITNAELQHKEKMASEDAQKIADLKTLVEAIQVANANISATNAELSTVLEVLQAEKSETNHIFELFEMEADMNSERLIEKVTGIKEELKETHLQLDERQKKFEELEEKLKQAQQSEQKLQQESQTSKEKLTEIQQSLQELQDSVKQKEELVQNLEEKVRESSSIIEAQNTKLNESNVQLENKTSCLKETQDQLLESQKKEKQLQEEAAKLSGELQQVQEANGDIKDSLVKVEELVKVLEEKLQAATSQLDAQQATNKELQELLVKSQENEGNLQGESLAVTEKLQQLEQANGELKEALCQKENGLKELQGKLDESNTVLESQKKSHNEIQDKLEQAQQKERTLQEETSKLAEQLSQLKQANEELQKSLQQKQLLLEKGNEFDTQLAEYQKVIDEMDDAASVKSALLEQLQNRVAELETALRQANDAQKTAYLETKELRRQLESLELEKSREVLSLKAQMNGASSRSGKGDEVESLDIETSLAKINFLNSIIADMQQKNDALKAKVQTLETLPMDFTKPHAFDALTKRKPAPRLFCDICDEFDQHDTEDCPIQGSEDQDYSTPSSESNNNEKERKLPAPRKYCDSCEVFGHDTSECADDETY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
38 | Phosphorylation | KLPGPIRSNIPTPAT CCCCCCCCCCCCCCC | 39.57 | 21082442 | |
45 | Phosphorylation | SNIPTPATSGTGIPQ CCCCCCCCCCCCCCC | 28.97 | 22817900 | |
48 | Phosphorylation | PTPATSGTGIPQPSK CCCCCCCCCCCCCCC | 31.53 | 21082442 | |
61 | Phosphorylation | SKMKAPSSFGSTGSV CCCCCCCCCCCCCCC | 32.35 | 29892262 | |
64 | Phosphorylation | KAPSSFGSTGSVSKI CCCCCCCCCCCCHHC | 27.82 | 21082442 | |
65 | Phosphorylation | APSSFGSTGSVSKIG CCCCCCCCCCCHHCC | 33.58 | 19429919 | |
67 | Phosphorylation | SSFGSTGSVSKIGRP CCCCCCCCCHHCCCC | 24.25 | 19429919 | |
69 | Phosphorylation | FGSTGSVSKIGRPCC CCCCCCCHHCCCCCC | 21.91 | 19429919 | |
70 (in isoform 3) | Phosphorylation | - | 47.20 | 28490779 | |
71 (in isoform 3) | Phosphorylation | - | 4.39 | 28490779 | |
74 (in isoform 3) | Phosphorylation | - | 23.07 | 28490779 | |
75 (in isoform 3) | Phosphorylation | - | 3.32 | 28490779 | |
82 (in isoform 3) | Phosphorylation | - | 66.99 | 28490779 | |
190 | Phosphorylation | FSRLTRLTTYPLAGA CHHHHHHCCCCCCCC | 22.46 | 19429919 | |
191 | Phosphorylation | SRLTRLTTYPLAGAQ HHHHHHCCCCCCCCC | 27.94 | 19429919 | |
192 | Phosphorylation | RLTRLTTYPLAGAQT HHHHHCCCCCCCCCC | 7.33 | 19429919 | |
199 | Phosphorylation | YPLAGAQTPTSPLAK CCCCCCCCCCCCCCC | 28.18 | 19429919 | |
201 | Phosphorylation | LAGAQTPTSPLAKSS CCCCCCCCCCCCCCC | 46.49 | 19429919 | |
202 | Phosphorylation | AGAQTPTSPLAKSSP CCCCCCCCCCCCCCC | 21.08 | 19429919 | |
207 | Phosphorylation | PTSPLAKSSPDRSRT CCCCCCCCCCCCCCC | 41.31 | 19429919 | |
208 | Phosphorylation | TSPLAKSSPDRSRTV CCCCCCCCCCCCCCC | 30.07 | 19429919 | |
212 | Phosphorylation | AKSSPDRSRTVSPTA CCCCCCCCCCCCCCH | 39.42 | 19429919 | |
214 | Phosphorylation | SSPDRSRTVSPTASI CCCCCCCCCCCCHHH | 26.95 | 27626673 | |
216 | Phosphorylation | PDRSRTVSPTASIRS CCCCCCCCCCHHHHH | 18.87 | 19429919 | |
218 | Phosphorylation | RSRTVSPTASIRSSM CCCCCCCCHHHHHHH | 26.07 | 19429919 | |
220 | Phosphorylation | RTVSPTASIRSSMLR CCCCCCHHHHHHHHC | 22.48 | 19429919 | |
228 | Phosphorylation | IRSSMLRSPGIGGKN HHHHHHCCCCCCCCC | 24.42 | 25749252 | |
309 | Phosphorylation | PIAKVSLSPSSKKTR EEEEEECCCCCCCCC | 18.41 | 19429919 | |
311 | Phosphorylation | AKVSLSPSSKKTRLS EEEECCCCCCCCCCC | 51.95 | 19429919 | |
312 | Phosphorylation | KVSLSPSSKKTRLSR EEECCCCCCCCCCCC | 41.37 | 19429919 | |
320 | Phosphorylation | KKTRLSRTGSRESLT CCCCCCCCCCCHHHH | 35.81 | 19429919 | |
322 | Phosphorylation | TRLSRTGSRESLTSI CCCCCCCCCHHHHCH | 32.06 | 19429919 | |
325 | Phosphorylation | SRTGSRESLTSIGTM CCCCCCHHHHCHHHH | 35.52 | 19429919 | |
327 | Phosphorylation | TGSRESLTSIGTMNS CCCCHHHHCHHHHHH | 27.81 | 19429919 | |
328 | Phosphorylation | GSRESLTSIGTMNSI CCCHHHHCHHHHHHH | 25.06 | 19429919 | |
331 | Phosphorylation | ESLTSIGTMNSIATT HHHHCHHHHHHHHHH | 16.12 | 29892262 | |
352 | Phosphorylation | MNAQQRKSSTPVKPI HCHHHHCCCCCCCCC | 41.45 | 19429919 | |
353 | Phosphorylation | NAQQRKSSTPVKPIL CHHHHCCCCCCCCCC | 39.50 | 19429919 | |
354 | Phosphorylation | AQQRKSSTPVKPILA HHHHCCCCCCCCCCC | 38.91 | 19429919 | |
362 | Phosphorylation | PVKPILATPKSQFSM CCCCCCCCCHHHCCH | 28.01 | 22817900 | |
365 | Phosphorylation | PILATPKSQFSMQDL CCCCCCHHHCCHHHH | 37.35 | 19429919 | |
368 | Phosphorylation | ATPKSQFSMQDLLRE CCCHHHCCHHHHHHH | 14.11 | 19429919 | |
605 | Phosphorylation | NLKATSDSLESERVN HHHHCCCCHHHHCCC | 33.53 | 25749252 | |
653 | Phosphorylation | NVQKADSSALDDMLR CHHHHCCCHHHHHHH | 33.14 | 25749252 | |
853 | Phosphorylation | AASGEEGSKTVAKLH HHCCCCHHHHHHHHH | 28.56 | 22817900 | |
1681 | Phosphorylation | CEVFGHDTSECADDE CCCCCCCCHHCCCCC | 22.28 | 18327897 | |
1682 | Phosphorylation | EVFGHDTSECADDET CCCCCCCHHCCCCCC | 36.41 | 12537569 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CL190_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CL190_DROME !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CL190_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MYS9_DROME | jar | physical | 9472041 | |
CLASP_DROME | chb | physical | 15710747 | |
LVA_DROME | lva | physical | 11076973 | |
HAIR_DROME | h | physical | 23918939 | |
MYS9_DROME | jar | physical | 25694447 | |
K10_DROME | fs(1)K10 | physical | 23918939 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; SER-216;SER-309; SER-322; SER-325; THR-327; SER-328; THR-362; THR-1681 ANDSER-1682, AND MASS SPECTROMETRY. |