PHOCN_HUMAN - dbPTM
PHOCN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHOCN_HUMAN
UniProt AC Q9Y3A3
Protein Name MOB-like protein phocein
Gene Name MOB4
Organism Homo sapiens (Human).
Sequence Length 225
Subcellular Localization Cytoplasm, perinuclear region . Membrane
Peripheral membrane protein . Golgi apparatus, Golgi stack membrane
Peripheral membrane protein . In a perinuclear punctate pattern. Associated with membranes and the Golgi stacks.
Protein Description May play a role in membrane trafficking, specifically in membrane budding reactions..
Protein Sequence MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLELNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVCRRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
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
3Sulfoxidation-----MVMAEGTAVL
-----CCCCCCCEEE		2.4421406390
7Phosphorylation-MVMAEGTAVLRRNR
-CCCCCCCEEEECCC		12.7122210691
21PhosphorylationRPGTKAQDFYNWPDE
CCCCCHHHHCCCCCC		53.5127642862
21 (in isoform 3)Phosphorylation-53.5128674419
29PhosphorylationFYNWPDESFDEMDST
HCCCCCCCHHHHHHH		45.4328348404
35PhosphorylationESFDEMDSTLAVQQY
CCHHHHHHHHHHHHH		24.8228348404
36PhosphorylationSFDEMDSTLAVQQYI
CHHHHHHHHHHHHHH		17.9328348404
42PhosphorylationSTLAVQQYIQQNIRA
HHHHHHHHHHHHHHH		5.4327050516
108AcetylationTATEQWIFLCAAHKT
CHHHHHHHHHHHCCC		4.1219608861
114AcetylationIFLCAAHKTPKECPA
HHHHHHCCCCCCCCC		62.8926051181
117AcetylationCAAHKTPKECPAIDY
HHHCCCCCCCCCCCC		76.7426051181
119AcetylationAHKTPKECPAIDYTR
HCCCCCCCCCCCCCC		3.2619608861
138PhosphorylationGAACLLNSNKYFPSR
HHHHHHCCCCCCCCC		34.3728152594
140MalonylationACLLNSNKYFPSRVS
HHHHCCCCCCCCCEE		48.3526320211
140UbiquitinationACLLNSNKYFPSRVS
HHHHCCCCCCCCCEE		48.3519608861
140AcetylationACLLNSNKYFPSRVS
HHHHCCCCCCCCCEE		48.3523954790
141PhosphorylationCLLNSNKYFPSRVSI
HHHCCCCCCCCCEEE		25.6028152594
144PhosphorylationNSNKYFPSRVSIKES
CCCCCCCCCEEECHH		35.1028152594
147PhosphorylationKYFPSRVSIKESSVA
CCCCCCEEECHHHHH		27.1728450419
149UbiquitinationFPSRVSIKESSVAKL
CCCCEEECHHHHHHH		44.00-
155MalonylationIKESSVAKLGSVCRR
ECHHHHHHHHHHHHH		51.7526320211
155AcetylationIKESSVAKLGSVCRR
ECHHHHHHHHHHHHH		51.7525953088
192PhosphorylationTFLCHRFTKFVMKYN
HHHHHHHHHHHHHHC		24.4324719451
198PhosphorylationFTKFVMKYNLMSKDN
HHHHHHHHCCCCCCC		8.74-
218PhosphorylationLEEEVQNSVSGESEA
CHHHHHHHCCCCCCC		10.6828348404
220PhosphorylationEEVQNSVSGESEA--
HHHHHHCCCCCCC--		36.3424719451
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 PHOCN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHOCN_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 PHOCN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAB39_HUMANCAB39physical
17353931
RBCC1_HUMANRB1CC1physical
17353931
TAP26_HUMANCCDC59physical
17353931
DPYL1_HUMANCRMP1physical
16169070
FADD_HUMANFADDphysical
16169070
MED10_HUMANMED10physical
16169070
PKHM1_HUMANPLEKHM1physical
16169070
MED31_HUMANMED31physical
16169070
GDF9_HUMANGDF9physical
16169070
KDIS_HUMANKIDINS220physical
16169070
MYL6_HUMANMYL6physical
16169070
SCMH1_HUMANSCMH1physical
16169070
SETB1_HUMANSETDB1physical
16169070
UB2V2_HUMANUBE2V2physical
16169070
MCM2_HUMANMCM2physical
16169070
PUR6_HUMANPAICSphysical
16169070
PTPRS_HUMANPTPRSphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
STK26_HUMANSTK26physical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
STRN4_HUMANSTRN4physical
18782753
STK25_HUMANSTK25physical
18782753
STK24_HUMANSTK24physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
SIKE1_HUMANSIKE1physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
TCPB_HUMANCCT2physical
18782753
TCPQ_HUMANCCT8physical
18782753
CTTB2_HUMANCTTNBP2physical
18782753
TCPG_HUMANCCT3physical
18782753
TCPA_HUMANTCP1physical
18782753
TCPE_HUMANCCT5physical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
TCPZ_HUMANCCT6Aphysical
18782753
TCPH_HUMANCCT7physical
18782753
STRP1_HUMANSTRIP1physical
19156129
CTTB2_HUMANCTTNBP2physical
19156129
SIKE1_HUMANSIKE1physical
19156129
STRP2_HUMANSTRIP2physical
19156129
CT2NL_HUMANCTTNBP2NLphysical
19156129
STK26_HUMANSTK26physical
19156129
STRN3_HUMANSTRN3physical
19156129
STRN4_HUMANSTRN4physical
19156129
FGOP2_HUMANFGFR1OP2physical
19156129
DYL1_HUMANDYNLL1physical
19156129
SLMAP_HUMANSLMAPphysical
19156129
STRN_HUMANSTRNphysical
19156129
2AAA_HUMANPPP2R1Aphysical
19156129
PP2AB_HUMANPPP2CBphysical
19156129
PP2AA_HUMANPPP2CAphysical
19156129
TCPG_HUMANCCT3physical
19156129
LATS1_HUMANLATS1physical
19739119
LATS2_HUMANLATS2physical
19739119
SPTB2_HUMANSPTBN1physical
22863883
SF3B1_HUMANSF3B1physical
26344197
STRN_HUMANSTRNphysical
26344197
STRN3_HUMANSTRN3physical
26344197
STRN4_HUMANSTRN4physical
26344197
PKN3_HUMANPKN3physical
27173435
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 PHOCN_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND MASS SPECTROMETRY.

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