CROCC_HUMAN - dbPTM
CROCC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CROCC_HUMAN
UniProt AC Q5TZA2
Protein Name Rootletin
Gene Name CROCC {ECO:0000312|EMBL:CAH70055.1}
Organism Homo sapiens (Human).
Sequence Length 2017
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . In ciliated cells, associated with ciliary rootlets. In
Protein Description Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus (By similarity). Furthermore, is required for the correct positioning of the cilium basal body relative to the cell nucleus, to allow for ciliogenesis. [PubMed: 27623382 Contributes to centrosome cohesion before mitosis]
Protein Sequence MSLGLARAQEVELTLETVIQTLESSVLCQEKGLGARDLAQDAQITSLPALIREIVTRNLSQPESPVLLPATEMASLLSLQEENQLLQQELSRVEDLLAQSRAERDELAIKYNAVSERLEQALRLEPGELETQEPRGLVRQSVELRRQLQEEQASYRRKLQAYQEGQQRQAQLVQRLQGKILQYKKRCSELEQQLLERSGELEQQRLRDTEHSQDLESALIRLEEEQQRSASLAQVNAMLREQLDQAGSANQALSEDIRKVTNDWTRCRKELEHREAAWRREEESFNAYFSNEHSRLLLLWRQVVGFRRLVSEVKMFTERDLLQLGGELARTSRAVQEAGLGLSTGLRLAESRAEAALEKQALLQAQLEEQLRDKVLREKDLAQQQMQSDLDKADLSARVTELGLAVKRLEKQNLEKDQVNKDLTEKLEALESLRLQEQAALETEDGEGLQQTLRDLAQAVLSDSESGVQLSGSERTADASNGSLRGLSGQRTPSPPRRSSPGRGRSPRRGPSPACSDSSTLALIHSALHKRQLQVQDMRGRYEASQDLLGTLRKQLSDSESERRALEEQLQRLRDKTDGAMQAHEDAQREVQRLRSANELLSREKSNLAHSLQVAQQQAEELRQEREKLQAAQEELRRQRDRLEEEQEDAVQDGARVRRELERSHRQLEQLEGKRSVLAKELVEVREALSRATLQRDMLQAEKAEVAEALTKAEAGRVELELSMTKLRAEEASLQDSLSKLSALNESLAQDKLDLNRLVAQLEEEKSALQGRQRQAEQEATVAREEQERLEELRLEQEVARQGLEGSLRVAEQAQEALEQQLPTLRHERSQLQEQLAQLSRQLSGREQELEQARREAQRQVEALERAAREKEALAKEHAGLAVQLVAAEREGRTLSEEATRLRLEKEALEGSLFEVQRQLAQLEARREQLEAEGQALLLAKETLTGELAGLRQQIIATQEKASLDKELMAQKLVQAEREAQASLREQRAAHEEDLQRLQREKEAAWRELEAERAQLQSQLQREQEELLARLEAEKEELSEEIAALQQERDEGLLLAESEKQQALSLKESEKTALSEKLMGTRHSLATISLEMERQKRDAQSRQEQDRSTVNALTSELRDLRAQREEAAAAHAQEVRRLQEQARDLGKQRDSCLREAEELRTQLRLLEDARDGLRRELLEAQRKLRESQEGREVQRQEAGELRRSLGEGAKEREALRRSNEELRSAVKKAESERISLKLANEDKEQKLALLEEARTAVGKEAGELRTGLQEVERSRLEARRELQELRRQMKMLDSENTRLGRELAELQGRLALGERAEKESRRETLGLRQRLLKGEASLEVMRQELQVAQRKLQEQEGEFRTRERRLLGSLEEARGTEKQQLDHARGLELKLEAARAEAAELGLRLSAAEGRAQGLEAELARVEVQRRAAEAQLGGLRSALRRGLGLGRAPSPAPRPVPGSPARDAPAEGSGEGLNSPSTLECSPGSQPPSPGPATSPASPDLDPEAVRGALREFLQELRSAQRERDELRTQTSALNRQLAEMEAERDSATSRARQLQKAVAESEEARRSVDGRLSGVQAELALQEESVRRSERERRATLDQVATLERSLQATESELRASQEKISKMKANETKLEGDKRRLKEVLDASESRTVKLELQRRSLEGELQRSRLGLSDREAQAQALQDRVDSLQRQVADSEVKAGTLQLTVERLNGALAKVEESEGALRDKVRGLTEALAQSSASLNSTRDKNLHLQKALTACEHDRQVLQERLDAARQALSEARKQSSSLGEQVQTLRGEVADLELQRVEAEGQLQQLREVLRQRQEGEAAALNTVQKLQDERRLLQERLGSLQRALAQLEAEKREVERSALRLEKDRVALRRTLDKVEREKLRSHEDTVRLSAEKGRLDRTLTGAELELAEAQRQIQQLEAQVVVLEQSHSPAQLEVDAQQQQLELQQEVERLRSAQAQTERTLEARERAHRQRVRGLEEQVSTLKGQLQQELRRSSAPFSPPSGPPEK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
100PhosphorylationVEDLLAQSRAERDEL
HHHHHHHCHHHHHHH
28.0525599653
154PhosphorylationQLQEEQASYRRKLQA
HHHHHHHHHHHHHHH
20.9024719451
155PhosphorylationLQEEQASYRRKLQAY
HHHHHHHHHHHHHHH
19.9024719451
229PhosphorylationLEEEQQRSASLAQVN
HHHHHHHCHHHHHHH
20.1930576742
284PhosphorylationAWRREEESFNAYFSN
HHHHHHHHHHHHCCC
27.3828555341
288PhosphorylationEEESFNAYFSNEHSR
HHHHHHHHCCCHHHH
14.51-
320UbiquitinationVKMFTERDLLQLGGE
HHHCCHHHHHHHHHH
45.5624816145
379UbiquitinationRDKVLREKDLAQQQM
HHHHHHHHHHHHHHH
52.1629967540
392UbiquitinationQMQSDLDKADLSARV
HHHHHHHHHHHHHHH
51.6124816145
394UbiquitinationQSDLDKADLSARVTE
HHHHHHHHHHHHHHH
47.0724816145
400PhosphorylationADLSARVTELGLAVK
HHHHHHHHHHHHHHH
21.6821406692
426UbiquitinationVNKDLTEKLEALESL
CCHHHHHHHHHHHHH
46.5229967540
432PhosphorylationEKLEALESLRLQEQA
HHHHHHHHHHHHHHH
21.4619413330
462PhosphorylationDLAQAVLSDSESGVQ
HHHHHHHCCCCCCCC
32.2730266825
464PhosphorylationAQAVLSDSESGVQLS
HHHHHCCCCCCCCCC
30.2230266825
466PhosphorylationAVLSDSESGVQLSGS
HHHCCCCCCCCCCCC
48.4930266825
471PhosphorylationSESGVQLSGSERTAD
CCCCCCCCCCCCEEC
24.1530266825
473PhosphorylationSGVQLSGSERTADAS
CCCCCCCCCCEECCC
22.1121406692
480PhosphorylationSERTADASNGSLRGL
CCCEECCCCCCCCCC
42.1229802988
483PhosphorylationTADASNGSLRGLSGQ
EECCCCCCCCCCCCC
21.1025850435
488PhosphorylationNGSLRGLSGQRTPSP
CCCCCCCCCCCCCCC
35.3930266825
492PhosphorylationRGLSGQRTPSPPRRS
CCCCCCCCCCCCCCC
21.8930266825
494PhosphorylationLSGQRTPSPPRRSSP
CCCCCCCCCCCCCCC
47.0930266825
499PhosphorylationTPSPPRRSSPGRGRS
CCCCCCCCCCCCCCC
42.0121406692
500PhosphorylationPSPPRRSSPGRGRSP
CCCCCCCCCCCCCCC
29.5730576142
506PhosphorylationSSPGRGRSPRRGPSP
CCCCCCCCCCCCCCC
26.11-
512PhosphorylationRSPRRGPSPACSDSS
CCCCCCCCCCCCCHH
28.1423401153
516PhosphorylationRGPSPACSDSSTLAL
CCCCCCCCCHHHHHH
42.5125850435
518PhosphorylationPSPACSDSSTLALIH
CCCCCCCHHHHHHHH
14.6625850435
519PhosphorylationSPACSDSSTLALIHS
CCCCCCHHHHHHHHH
32.2225850435
520PhosphorylationPACSDSSTLALIHSA
CCCCCHHHHHHHHHH
21.7225850435
526PhosphorylationSTLALIHSALHKRQL
HHHHHHHHHHHHCCC
26.0727251275
602PhosphorylationRSANELLSREKSNLA
HHHHHHHHHHHHHHH
51.5224719451
712AcetylationEVAEALTKAEAGRVE
HHHHHHHHHHCCCCE
45.1120167786
723PhosphorylationGRVELELSMTKLRAE
CCCEEEEEHHHHHHH
18.2827794612
725PhosphorylationVELELSMTKLRAEEA
CEEEEEHHHHHHHHH
24.4527794612
737PhosphorylationEEASLQDSLSKLSAL
HHHHHHHHHHHHHHH
22.9124719451
739PhosphorylationASLQDSLSKLSALNE
HHHHHHHHHHHHHCH
35.1927251275
807PhosphorylationARQGLEGSLRVAEQA
HHCHHHHHHHHHHHH
12.02-
830PhosphorylationPTLRHERSQLQEQLA
HHHHHHHHHHHHHHH
32.05-
844PhosphorylationAQLSRQLSGREQELE
HHHHHHHHCHHHHHH
27.71-
958PhosphorylationLRQQIIATQEKASLD
HHHHHHHHHHHHHCC
27.1824719451
1065PhosphorylationSEKQQALSLKESEKT
HHHHHHHCCCHHHHH
40.1724719451
1065O-linked_GlycosylationSEKQQALSLKESEKT
HHHHHHHCCCHHHHH
40.1730379171
1109PhosphorylationRQEQDRSTVNALTSE
HHHHHHHHHHHHHHH
20.7625690035
1151PhosphorylationDLGKQRDSCLREAEE
HHHHHHHHHHHHHHH
19.76-
1218PhosphorylationEREALRRSNEELRSA
HHHHHHHCHHHHHHH
42.0029802988
1224PhosphorylationRSNEELRSAVKKAES
HCHHHHHHHHHHHHH
50.4630266825
1231PhosphorylationSAVKKAESERISLKL
HHHHHHHHHHHHHHH
36.7130266825
1259UbiquitinationEARTAVGKEAGELRT
HHHHHHHHHHHHHHH
37.4829967540
1290UbiquitinationQELRRQMKMLDSENT
HHHHHHHHHHHCCCH
28.1529967540
1390UbiquitinationHARGLELKLEAARAE
HHHHHHHHHHHHHHH
34.60-
1442MethylationGLRSALRRGLGLGRA
HHHHHHHHCCCCCCC
45.60-
1451PhosphorylationLGLGRAPSPAPRPVP
CCCCCCCCCCCCCCC
32.4826055452
1460PhosphorylationAPRPVPGSPARDAPA
CCCCCCCCCCCCCCC
14.8730266825
1470PhosphorylationRDAPAEGSGEGLNSP
CCCCCCCCCCCCCCC
25.7725850435
1476PhosphorylationGSGEGLNSPSTLECS
CCCCCCCCCCCCCCC
25.8525850435
1478PhosphorylationGEGLNSPSTLECSPG
CCCCCCCCCCCCCCC
45.5025850435
1479PhosphorylationEGLNSPSTLECSPGS
CCCCCCCCCCCCCCC
29.9325850435
1483PhosphorylationSPSTLECSPGSQPPS
CCCCCCCCCCCCCCC
23.9525850435
1486PhosphorylationTLECSPGSQPPSPGP
CCCCCCCCCCCCCCC
42.7825850435
1490PhosphorylationSPGSQPPSPGPATSP
CCCCCCCCCCCCCCC
49.5325850435
1495PhosphorylationPPSPGPATSPASPDL
CCCCCCCCCCCCCCC
38.0727251275
1496PhosphorylationPSPGPATSPASPDLD
CCCCCCCCCCCCCCC
22.1527251275
1499PhosphorylationGPATSPASPDLDPEA
CCCCCCCCCCCCHHH
23.4927251275
1575PhosphorylationRSVDGRLSGVQAELA
HHHCCCHHHHHHHHH
35.2428555341
1587PhosphorylationELALQEESVRRSERE
HHHHCHHHHHHHHHH
21.8527251275
1598PhosphorylationSERERRATLDQVATL
HHHHHHHHHHHHHHH
29.1127251275
1608PhosphorylationQVATLERSLQATESE
HHHHHHHHHHHHHHH
18.5626437602
1612PhosphorylationLERSLQATESELRAS
HHHHHHHHHHHHHHC
27.3829978859
1614PhosphorylationRSLQATESELRASQE
HHHHHHHHHHHHCHH
37.2629978859
1619PhosphorylationTESELRASQEKISKM
HHHHHHHCHHHHHHH
32.2225849741
1622UbiquitinationELRASQEKISKMKAN
HHHHCHHHHHHHHHC
44.6429967540
1647PhosphorylationLKEVLDASESRTVKL
HHHHHHHCCCCCHHH
35.4523911959
1660PhosphorylationKLELQRRSLEGELQR
HHHHHHHHHHHHHHH
32.7225159151
1685MethylationQAQALQDRVDSLQRQ
HHHHHHHHHHHHHHH
22.60-
1732PhosphorylationRDKVRGLTEALAQSS
HHHHHHHHHHHHHCH
23.2622210691
1741PhosphorylationALAQSSASLNSTRDK
HHHHCHHHCCCCCCC
29.9922210691
1832PhosphorylationGEAAALNTVQKLQDE
HHHHHHHHHHHHHHH
25.7622817900
1849PhosphorylationLLQERLGSLQRALAQ
HHHHHHHHHHHHHHH
26.3922817900
1892PhosphorylationVEREKLRSHEDTVRL
HHHHHHHCCHHHHHH
41.4823312004
1892O-linked_GlycosylationVEREKLRSHEDTVRL
HHHHHHHCCHHHHHH
41.4830379171
1900PhosphorylationHEDTVRLSAEKGRLD
CHHHHHHHHHCCCCC
24.6628985074
1909PhosphorylationEKGRLDRTLTGAELE
HCCCCCCCCCHHHHH
28.4827251275
1911PhosphorylationGRLDRTLTGAELELA
CCCCCCCCHHHHHHH
33.4628857561
1937PhosphorylationQVVVLEQSHSPAQLE
HEEEEECCCCCHHHH
19.2928348404
1939PhosphorylationVVLEQSHSPAQLEVD
EEEECCCCCHHHHHH
27.4626657352
2004PhosphorylationLQQELRRSSAPFSPP
HHHHHHHCCCCCCCC
25.1522199227
2005PhosphorylationQQELRRSSAPFSPPS
HHHHHHCCCCCCCCC
37.8425159151
2009PhosphorylationRRSSAPFSPPSGPPE
HHCCCCCCCCCCCCC
34.5425159151
2012PhosphorylationSAPFSPPSGPPEK--
CCCCCCCCCCCCC--
68.2822199227

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 CROCC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CROCC_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 CROCC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RN152_HUMANRNF152physical
21988832
HDGF_HUMANHDGFphysical
22863883
XBP1_HUMANXBP1physical
28514442
PEX14_HUMANPEX14physical
28514442
PUSL1_HUMANPUSL1physical
28514442
SRBD1_HUMANSRBD1physical
28514442
UBR1_HUMANUBR1physical
28514442
GIT1_HUMANGIT1physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
SCOC_HUMANSCOCphysical
28514442
UBR2_HUMANUBR2physical
28514442
TGFA1_HUMANTGFBRAP1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CROCC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1619, AND MASSSPECTROMETRY.

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