BCCIP_HUMAN - dbPTM
BCCIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCCIP_HUMAN
UniProt AC Q9P287
Protein Name BRCA2 and CDKN1A-interacting protein
Gene Name BCCIP
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, spindle pole . Colocalizes with BRCA2 in discrete nuclear foci (PubMed:15713648). In interphase, preferential localizes to the mother c
Protein Description During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole. [PubMed: 28394342 Isoform 2/alpha is particularly important for the regulation of microtubule anchoring, microtubule stability, spindle architecture and spindle orientation, compared to isoform 1/beta]
Protein Sequence MASRSKRRAVESGVPQPPDPPVQRDEEEEKEVENEDEDDDDSDKEKDEEDEVIDEEVNIEFEAYSLSDNDYDGIKKLLQQLFLKAPVNTAELTDLLIQQNHIGSVIKQTDVSEDSNDDMDEDEVFGFISLLNLTERKGTQCVEQIQELVLRFCEKNCEKSMVEQLDKFLNDTTKPVGLLLSERFINVPPQIALPMYQQLQKELAGAHRTNKPCGKCYFYLLISKTFVEAGKNNSKKKPSNKKKAALMFANAEEEFFYEKAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV
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
7Dimethylation-MASRSKRRAVESGV
-CCCHHHHHHHHCCC		32.79-
8DimethylationMASRSKRRAVESGVP
CCCHHHHHHHHCCCC		46.88-
12PhosphorylationSKRRAVESGVPQPPD
HHHHHHHCCCCCCCC		38.1919060867
42PhosphorylationEDEDDDDSDKEKDEE
CCCCCCCCHHHHHHH		58.5428355574
65PhosphorylationNIEFEAYSLSDNDYD
CEEEEEEECCCCCHH		28.5724275569
75UbiquitinationDNDYDGIKKLLQQLF
CCCHHHHHHHHHHHH		42.7823000965
76 (in isoform 2)Ubiquitination-53.1321890473
76UbiquitinationNDYDGIKKLLQQLFL
CCHHHHHHHHHHHHH		53.1323000965
76 (in isoform 3)Ubiquitination-53.1321890473
76 (in isoform 1)Ubiquitination-53.1321890473
76UbiquitinationNDYDGIKKLLQQLFL
CCHHHHHHHHHHHHH		53.1321890473
84UbiquitinationLLQQLFLKAPVNTAE
HHHHHHHHCCCCHHH		43.22-
109PhosphorylationIGSVIKQTDVSEDSN
CCCEECCCCCCCCCC		33.1122115753
112PhosphorylationVIKQTDVSEDSNDDM
EECCCCCCCCCCCCC		38.2025159151
115PhosphorylationQTDVSEDSNDDMDED
CCCCCCCCCCCCCHH		37.8025159151
129PhosphorylationDEVFGFISLLNLTER
HHHHHHHHHHHCCCC		25.2520068231
134PhosphorylationFISLLNLTERKGTQC
HHHHHHCCCCCCCHH		32.4427080861
137UbiquitinationLLNLTERKGTQCVEQ
HHHCCCCCCCHHHHH		61.14-
141GlutathionylationTERKGTQCVEQIQEL
CCCCCCHHHHHHHHH		3.5022555962
155AcetylationLVLRFCEKNCEKSMV
HHHHHHHHHCHHHHH		68.9925953088
155UbiquitinationLVLRFCEKNCEKSMV
HHHHHHHHHCHHHHH		68.9933845483
159AcetylationFCEKNCEKSMVEQLD
HHHHHCHHHHHHHHH		46.1623236377
159 (in isoform 2)Ubiquitination-46.16-
159UbiquitinationFCEKNCEKSMVEQLD
HHHHHCHHHHHHHHH		46.1621963094
174UbiquitinationKFLNDTTKPVGLLLS
HHHCCCCCCCHHHHC		39.5421890473
174 (in isoform 1)Ubiquitination-39.5421890473
174 (in isoform 2)Ubiquitination-39.5421890473
174 (in isoform 3)Ubiquitination-39.5421890473
174UbiquitinationKFLNDTTKPVGLLLS
HHHCCCCCCCHHHHC		39.5423000965
201UbiquitinationPMYQQLQKELAGAHR
HHHHHHHHHHHCCCC		64.3929967540
201 (in isoform 2)Ubiquitination-64.39-
209O-linked_GlycosylationELAGAHRTNKPCGKC
HHHCCCCCCCCCCHH		37.4123301498
211AcetylationAGAHRTNKPCGKCYF
HCCCCCCCCCCHHHH		40.8626051181
211UbiquitinationAGAHRTNKPCGKCYF
HCCCCCCCCCCHHHH		40.8629967540
217PhosphorylationNKPCGKCYFYLLISK
CCCCCHHHHHHHHHH		9.9521406692
219PhosphorylationPCGKCYFYLLISKTF
CCCHHHHHHHHHHHH		3.6721406692
223PhosphorylationCYFYLLISKTFVEAG
HHHHHHHHHHHHHHC		26.1321406692
225PhosphorylationFYLLISKTFVEAGKN
HHHHHHHHHHHHCCC		26.5626074081
231UbiquitinationKTFVEAGKNNSKKKP
HHHHHHCCCCCCCCC		61.0633845483
231 (in isoform 2)Ubiquitination-61.06-
234PhosphorylationVEAGKNNSKKKPSNK
HHHCCCCCCCCCCCH		56.0726074081
235AcetylationEAGKNNSKKKPSNKK
HHCCCCCCCCCCCHH		67.9212439411
235 (in isoform 2)Ubiquitination-67.92-
243 (in isoform 2)Ubiquitination-40.27-
257 (in isoform 4)Phosphorylation-23.1128796482
257 (in isoform 2)Phosphorylation-23.1128796482
266PhosphorylationKAILKFNYSVQEESD
HHHHHCCCCCCCCCC		17.2228152594
267PhosphorylationAILKFNYSVQEESDT
HHHHCCCCCCCCCCC		20.5928152594
281PhosphorylationTCLGGKWSFDDVPMT
CCCCCCCCCCCCCCC		23.4527080861
286 (in isoform 2)Phosphorylation-28.11-
288PhosphorylationSFDDVPMTPLRTVML
CCCCCCCCCCEEEEE		17.0727080861
3072-HydroxyisobutyrylationKMNEIMDKLKEYLSV
HHHHHHHHHHHHHCC		44.04-
307AcetylationKMNEIMDKLKEYLSV
HHHHHHHHHHHHHCC		44.0425953088
311PhosphorylationIMDKLKEYLSV----
HHHHHHHHHCC----		11.5928152594
313PhosphorylationDKLKEYLSV------
HHHHHHHCC------		25.5328152594
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 BCCIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCCIP_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 BCCIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK2_HUMANCDK2physical
10878006
PTN_HUMANPTNphysical
16169070
CDN1A_HUMANCDKN1Aphysical
10878006
RL23_HUMANRPL23physical
22939629
GNL3_HUMANGNL3physical
22939629
GRWD1_HUMANGRWD1physical
22939629
AL9A1_HUMANALDH9A1physical
22863883
CAN1_HUMANCAPN1physical
22863883
IF5A1_HUMANEIF5Aphysical
22863883
KYNU_HUMANKYNUphysical
22863883
LDHA_HUMANLDHAphysical
22863883
SPSY_HUMANSMSphysical
22863883
1433B_HUMANYWHABphysical
22863883
CCD33_HUMANCCDC33physical
25416956
RL23_HUMANRPL23physical
26186194
IF6_HUMANEIF6physical
26186194
GLD2_HUMANPAPD4physical
26186194
RPC9_HUMANCRCPphysical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
GLD2_HUMANPAPD4physical
28514442
RL23_HUMANRPL23physical
28514442
IF6_HUMANEIF6physical
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 BCCIP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-112 AND SER-115,AND MASS SPECTROMETRY.

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