KINH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KINH_HUMAN
• UniProt AC: P33176
• Protein Name: Kinesin-1 heavy chain
• Gene Name: KIF5B
• Organism: Homo sapiens (Human).
• Sequence Length: 963
• Subcellular Localization: Cytoplasm, cytoskeleton . Uniformly distributed between soma and neurites in hippocampal neurons.
• Protein Description: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes. [PubMed: 20386726]
• Protein Sequence: MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTNDKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGGKQV

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
2	Acetylation	------MADLAECNI ------CCCHHHCCE	22.11	22223895
10	Acetylation	DLAECNIKVMCRFRP CHHHCCEEEEEEECC	15.21	23749302
10	Malonylation	DLAECNIKVMCRFRP CHHHCCEEEEEEECC	15.21	26320211
10	Ubiquitination	DLAECNIKVMCRFRP CHHHCCEEEEEEECC	15.21	-
21	Phosphorylation	RFRPLNESEVNRGDK EECCCCHHHCCCCCC	45.85	24719451
28	Acetylation	SEVNRGDKYIAKFQG HHCCCCCCEEEEECC	41.18	19608861
38	Phosphorylation	AKFQGEDTVVIASKP EEECCCCEEEEECCC	16.63	28152594
43	Phosphorylation	EDTVVIASKPYAFDR CCEEEEECCCCCHHH	24.04	28152594
44	Acetylation	DTVVIASKPYAFDRV CEEEEECCCCCHHHH	32.78	25953088
44	Ubiquitination	DTVVIASKPYAFDRV CEEEEECCCCCHHHH	32.78	-
46	Phosphorylation	VVIASKPYAFDRVFQ EEEECCCCCHHHHCC	24.52	28152594
55	Phosphorylation	FDRVFQSSTSQEQVY HHHHCCCCCCHHHHH	22.69	21712546
65	Glutathionylation	QEQVYNDCAKKIVKD HHHHHHHHHHHHHHH	5.49	22555962
65	S-nitrosylation	QEQVYNDCAKKIVKD HHHHHHHHHHHHHHH	5.49	2212679
67	Acetylation	QVYNDCAKKIVKDVL HHHHHHHHHHHHHHH	49.73	25953088
67	Ubiquitination	QVYNDCAKKIVKDVL HHHHHHHHHHHHHHH	49.73	-
95	Sulfoxidation	SSGKTHTMEGKLHDP CCCCEEEEECEECCC	5.05	30846556
98	Acetylation	KTHTMEGKLHDPEGM CEEEEECEECCCCCC	29.37	25953088
105	Sulfoxidation	KLHDPEGMGIIPRIV EECCCCCCCCHHHHH	3.12	21406390
149	Phosphorylation	IRDLLDVSKTNLSVH HHHHHCHHCCCCCCC	33.17	26552605
150	Ubiquitination	RDLLDVSKTNLSVHE HHHHCHHCCCCCCCC	41.08	-
151	Phosphorylation	DLLDVSKTNLSVHED HHHCHHCCCCCCCCC	33.61	26552605
154	Phosphorylation	DVSKTNLSVHEDKNR CHHCCCCCCCCCCCC	24.41	25849741
159	Ubiquitination	NLSVHEDKNRVPYVK CCCCCCCCCCCCCCC	43.60	-
164	Phosphorylation	EDKNRVPYVKGCTER CCCCCCCCCCCCCCC	16.37	30631047
166	Acetylation	KNRVPYVKGCTERFV CCCCCCCCCCCCCEE	42.28	19608861
166	Malonylation	KNRVPYVKGCTERFV CCCCCCCCCCCCCEE	42.28	26320211
174	Glutathionylation	GCTERFVCSPDEVMD CCCCCEEECHHHHHH	4.49	22555962
175	Phosphorylation	CTERFVCSPDEVMDT CCCCEEECHHHHHHC	30.04	28348404
195	Phosphorylation	SNRHVAVTNMNEHSS CCCCEEEECCCCCCC	21.00	22210691
197	Sulfoxidation	RHVAVTNMNEHSSRS CCEEEECCCCCCCCC	4.55	30846556
201	Phosphorylation	VTNMNEHSSRSHSIF EECCCCCCCCCCEEE	22.67	21406692
202	Phosphorylation	TNMNEHSSRSHSIFL ECCCCCCCCCCEEEE	39.44	21406692
204	Phosphorylation	MNEHSSRSHSIFLIN CCCCCCCCCEEEEEE	24.43	23312004
206	Phosphorylation	EHSSRSHSIFLINVK CCCCCCCEEEEEEEE	19.11	23312004
213	Acetylation	SIFLINVKQENTQTE EEEEEEEEECCCCCC	47.62	26051181
213	Sumoylation	SIFLINVKQENTQTE EEEEEEEEECCCCCC	47.62	28112733
222	Ubiquitination	ENTQTEQKLSGKLYL CCCCCCHHHCCEEEE	38.09	21906983
224	Phosphorylation	TQTEQKLSGKLYLVD CCCCHHHCCEEEEEE	40.70	29391485
226	Ubiquitination	TEQKLSGKLYLVDLA CCHHHCCEEEEEECC	30.49	-
228	Phosphorylation	QKLSGKLYLVDLAGS HHHCCEEEEEECCCC	14.25	28152594
237	Malonylation	VDLAGSEKVSKTGAE EECCCCCCCCCCCCC	54.21	26320211
240	Ubiquitination	AGSEKVSKTGAEGAV CCCCCCCCCCCCCCH	54.70	-
252	Malonylation	GAVLDEAKNINKSLS CCHHHHHHHHHHHHH	57.20	26320211
252	Ubiquitination	GAVLDEAKNINKSLS CCHHHHHHHHHHHHH	57.20	21906983
256	Ubiquitination	DEAKNINKSLSALGN HHHHHHHHHHHHHHH	49.31	-
257	Phosphorylation	EAKNINKSLSALGNV HHHHHHHHHHHHHHH	24.06	28348404
259	Phosphorylation	KNINKSLSALGNVIS HHHHHHHHHHHHHHH	28.65	28348404
277	Phosphorylation	EGSTYVPYRDSKMTR CCCCCCCCCCCHHHH	19.60	-
294	Glutathionylation	QDSLGGNCRTTIVIC HHHCCCCCEEEEEEE	4.65	22555962
303	Phosphorylation	TTIVICCSPSSYNES EEEEEEECCCCCCCC	24.33	30576142
312	Phosphorylation	SSYNESETKSTLLFG CCCCCCHHCCEEECC	39.30	30576142
314	Phosphorylation	YNESETKSTLLFGQR CCCCHHCCEEECCCC	31.54	30576142
321	Methylation	STLLFGQRAKTIKNT CEEECCCCCCCCCCE	38.13	115481283
346	Acetylation	QWKKKYEKEKEKNKI HHHHHHHHHHHHHHH	71.62	6570053
382	Acetylation	PIDEQFDKEKANLEA CCCHHCCHHHHCCEE	63.50	23236377
382	Ubiquitination	PIDEQFDKEKANLEA CCCHHCCHHHHCCEE	63.50	-
384	Ubiquitination	DEQFDKEKANLEAFT CHHCCHHHHCCEEEE	48.60	-
394	Ubiquitination	LEAFTVDKDITLTND CEEEEECCCCEECCC	46.85	-
397	Phosphorylation	FTVDKDITLTNDKPA EEECCCCEECCCCCC	37.35	22199227
399	Phosphorylation	VDKDITLTNDKPATA ECCCCEECCCCCCCE	32.49	22199227
402	Ubiquitination	DITLTNDKPATAIGV CCEECCCCCCCEEEE	38.33	-
405	O-linked_Glycosylation	LTNDKPATAIGVIGN ECCCCCCCEEEEEEC	27.60	23301498
405	Phosphorylation	LTNDKPATAIGVIGN ECCCCCCCEEEEEEC	27.60	22199227
414	Phosphorylation	IGVIGNFTDAERRKC EEEEECCCHHHHHHH	38.00	-
420	Ubiquitination	FTDAERRKCEEEIAK CCHHHHHHHHHHHHH	52.82	-
427	Ubiquitination	KCEEEIAKLYKQLDD HHHHHHHHHHHHHCC	58.99	-
430	Acetylation	EEIAKLYKQLDDKDE HHHHHHHHHHCCCCH	55.62	26051181
430	Ubiquitination	EEIAKLYKQLDDKDE HHHHHHHHHHCCCCH	55.62	-
448	Ubiquitination	QQSQLVEKLKTQMLD HHHHHHHHHHHHCCC	48.05	-
451	Phosphorylation	QLVEKLKTQMLDQEE HHHHHHHHHCCCHHH	29.64	21406692
462	Phosphorylation	DQEELLASTRRDQDN CHHHHHHHHHCCHHH	23.55	24719451
463	Phosphorylation	QEELLASTRRDQDNM HHHHHHHHHCCHHHH	24.90	24719451
464	Dimethylation	EELLASTRRDQDNMQ HHHHHHHHCCHHHHH	37.37	-
464	Methylation	EELLASTRRDQDNMQ HHHHHHHHCCHHHHH	37.37	115390193
470	Sulfoxidation	TRRDQDNMQAELNRL HHCCHHHHHHHHHHH	5.56	21406390
505	Ubiquitination	LAVNYDQKSQEVEDK HHCCCCCCCHHHHHH	51.73	-
512	Acetylation	KSQEVEDKTKEYELL CCHHHHHHHHHHHHH	48.25	23749302
513	Phosphorylation	SQEVEDKTKEYELLS CHHHHHHHHHHHHHH	41.24	28796482
514	Ubiquitination	QEVEDKTKEYELLSD HHHHHHHHHHHHHHH	65.13	-
516	Phosphorylation	VEDKTKEYELLSDEL HHHHHHHHHHHHHHH	17.27	28796482
526	Ubiquitination	LSDELNQKSATLASI HHHHHHHHHHHHHHH	40.77	-
539	Ubiquitination	SIDAELQKLKEMTNH HHHHHHHHHHHHCHH	74.32	-
543	Sulfoxidation	ELQKLKEMTNHQKKR HHHHHHHHCHHHHHH	4.32	30846556
544	Phosphorylation	LQKLKEMTNHQKKRA HHHHHHHCHHHHHHH	30.55	28270605
549	Acetylation	EMTNHQKKRAAEMMA HHCHHHHHHHHHHHH	40.47	7408757
557	Phosphorylation	RAAEMMASLLKDLAE HHHHHHHHHHHHHHH	19.15	24719451
560	Acetylation	EMMASLLKDLAEIGI HHHHHHHHHHHHHCE	56.86	7408767
582	Sulfoxidation	KQPEGTGMIDEEFTV CCCCCCCCCCCCHHH	3.33	30846556
593	Phosphorylation	EFTVARLYISKMKSE CHHHHHHHHHHHHHH	9.52	27107777
599	Phosphorylation	LYISKMKSEVKTMVK HHHHHHHHHHHHHHH	44.09	23836654
602	Acetylation	SKMKSEVKTMVKRCK HHHHHHHHHHHHHHH	27.18	25953088
609	Acetylation	KTMVKRCKQLESTQT HHHHHHHHHHHHHCC	63.05	7619063
609	Ubiquitination	KTMVKRCKQLESTQT HHHHHHHHHHHHHCC	63.05	-
613	Phosphorylation	KRCKQLESTQTESNK HHHHHHHHHCCHHHH	34.11	24850871
614	Phosphorylation	RCKQLESTQTESNKK HHHHHHHHCCHHHHH	30.09	24850871
618	Phosphorylation	LESTQTESNKKMEEN HHHHCCHHHHHHHHH	58.29	24850871
622	Sulfoxidation	QTESNKKMEENEKEL CCHHHHHHHHHHHHH	9.25	30846556
632	Glutathionylation	NEKELAACQLRISQH HHHHHHHHHHHHHHH	3.05	22555962
644	Ubiquitination	SQHEAKIKSLTEYLQ HHHHHHHHHHHHHHH	38.41	-
645	Phosphorylation	QHEAKIKSLTEYLQN HHHHHHHHHHHHHHH	43.95	28152594
647	Phosphorylation	EAKIKSLTEYLQNVE HHHHHHHHHHHHHHH	29.67	28152594
649	Phosphorylation	KIKSLTEYLQNVEQK HHHHHHHHHHHHHHH	14.35	28152594
656	Acetylation	YLQNVEQKKRQLEES HHHHHHHHHHHHHHH	36.10	25953088
656	Ubiquitination	YLQNVEQKKRQLEES HHHHHHHHHHHHHHH	36.10	-
657	Ubiquitination	LQNVEQKKRQLEESV HHHHHHHHHHHHHHH	45.10	-
663	Phosphorylation	KKRQLEESVDALSEE HHHHHHHHHHHHHHH	18.87	-
679	Ubiquitination	VQLRAQEKVHEMEKE HHHHHHHHHHHHHHH	36.49	-
683	Sulfoxidation	AQEKVHEMEKEHLNK HHHHHHHHHHHHHHH	5.56	30846556
690	Ubiquitination	MEKEHLNKVQTANEV HHHHHHHHHHHHHHH	41.92	-
698	Ubiquitination	VQTANEVKQAVEQQI HHHHHHHHHHHHHHH	26.76	-
717	Phosphorylation	ETHQKQISSLRDEVE HHHHHHHHHHHHHHH	22.33	24719451
718	Phosphorylation	THQKQISSLRDEVEA HHHHHHHHHHHHHHH	29.11	25954137
728	Acetylation	DEVEAKAKLITDLQD HHHHHHHHHHHHHHH	39.45	25953088
761	Acetylation	LKATDQEKSRKLHEL HHCCHHHHHHHHHHH	50.34	20167786
764	Acetylation	TDQEKSRKLHELTVM CHHHHHHHHHHHHHH	62.38	20167786
764	Malonylation	TDQEKSRKLHELTVM CHHHHHHHHHHHHHH	62.38	26320211
764	Ubiquitination	TDQEKSRKLHELTVM CHHHHHHHHHHHHHH	62.38	-
771	Sulfoxidation	KLHELTVMQDRREQA HHHHHHHHHHHHHHH	2.64	21406390
783	Acetylation	EQARQDLKGLEETVA HHHHHHHHHHHHHHH	70.51	25953088
783	Ubiquitination	EQARQDLKGLEETVA HHHHHHHHHHHHHHH	70.51	2190698
791	Ubiquitination	GLEETVAKELQTLHN HHHHHHHHHHHHHHH	55.40	-
795	Phosphorylation	TVAKELQTLHNLRKL HHHHHHHHHHHHHHH	42.48	21082442
801	Malonylation	QTLHNLRKLFVQDLA HHHHHHHHHHHHHHH	49.82	26320211
801	Ubiquitination	QTLHNLRKLFVQDLA HHHHHHHHHHHHHHH	49.82	-
814	Phosphorylation	LATRVKKSAEIDSDD HHHHHHHHHCCCCCC	25.97	29396449
819	Phosphorylation	KKSAEIDSDDTGGSA HHHHCCCCCCCCCCH	42.94	25159151
822	Phosphorylation	AEIDSDDTGGSAAQK HCCCCCCCCCCHHHH	48.73	28985074
825	Phosphorylation	DSDDTGGSAAQKQKI CCCCCCCCHHHHHHH	23.06	21815630
829	Ubiquitination	TGGSAAQKQKISFLE CCCCHHHHHHHHHHH	49.16	-
833	Phosphorylation	AAQKQKISFLENNLE HHHHHHHHHHHHCHH	30.71	25159151
844	Ubiquitination	NNLEQLTKVHKQLVR HCHHHHHHHHHHHHH	51.43	-
847	Ubiquitination	EQLTKVHKQLVRDNA HHHHHHHHHHHHCCC	48.60	-
885	Ubiquitination	ESALKEAKENASRDR HHHHHHHHHHHHHHH	53.22	-
901	Methylation	RYQQEVDRIKEAVRS HHHHHHHHHHHHHHH	47.24	-
917	Phosphorylation	NMARRGHSAQIAKPI CHHHCCCCCCCCCCC	25.37	20068231
922	Acetylation	GHSAQIAKPIRPGQH CCCCCCCCCCCCCCC	42.48	26051181
922	Ubiquitination	GHSAQIAKPIRPGQH CCCCCCCCCCCCCCC	42.48	-
933	Phosphorylation	PGQHPAASPTHPSAI CCCCCCCCCCCCCCC	32.22	29255136
935	Phosphorylation	QHPAASPTHPSAIRG CCCCCCCCCCCCCCC	43.88	29255136
938	Phosphorylation	AASPTHPSAIRGGGA CCCCCCCCCCCCCCC	28.82	29255136
950	O-linked_Glycosylation	GGAFVQNSQPVAVRG CCCCCCCCCCEEECC	20.83	23301498
950	Phosphorylation	GGAFVQNSQPVAVRG CCCCCCCCCCEEECC	20.83	28857561
956	Methylation	NSQPVAVRGGGGKQV CCCCEEECCCCCCCC	28.44	24129315

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

Oops, there are no upstream regulatory protein records of KINH_HUMAN !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KINH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNP23_HUMAN	SNAP23	physical	12475239
SNP25_HUMAN	SNAP25	physical	12475239
KLC1_HUMAN	KLC1	physical	12475239
1433F_HUMAN	YWHAH	physical	11969417
KLC2_HUMAN	KLC2	physical	22939629
KLC1_HUMAN	KLC1	physical	22939629
KLC4_HUMAN	KLC4	physical	22939629
ZBT8B_HUMAN	ZBTB8B	physical	22939629
MCCA_HUMAN	MCCC1	physical	22939629
TWF1_HUMAN	TWF1	physical	22939629
SRP68_HUMAN	SRP68	physical	22939629
RN168_HUMAN	RNF168	physical	22939629
ACACA_HUMAN	ACACA	physical	22863883
ICAL_HUMAN	CAST	physical	22863883
COPE_HUMAN	COPE	physical	22863883
CSN5_HUMAN	COPS5	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB4_HUMAN	PSMB4	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB6_HUMAN	PSMB6	physical	22863883
PSB7_HUMAN	PSMB7	physical	22863883
PSME1_HUMAN	PSME1	physical	22863883
PTN23_HUMAN	PTPN23	physical	22863883
RBGP1_HUMAN	RABGAP1	physical	22863883
P4R3B_HUMAN	SMEK2	physical	22863883
KAP3_HUMAN	PRKAR2B	physical	25416956
VPS52_HUMAN	VPS52	physical	25416956
TAXB1_HUMAN	TAX1BP1	physical	25416956
ZBT8A_HUMAN	ZBTB8A	physical	25416956
LSM2_HUMAN	LSM2	physical	26344197
KLC1_HUMAN	KLC1	physical	26496610
NHS_HUMAN	NHS	physical	26496610
PIT1_HUMAN	POU1F1	physical	26496610
TBA1A_HUMAN	TUBA1A	physical	26496610
OGT1_HUMAN	OGT	physical	26496610
SQSTM_HUMAN	SQSTM1	physical	26496610
XPR1_HUMAN	XPR1	physical	26496610
NCOR1_HUMAN	NCOR1	physical	26496610
TRAK1_HUMAN	TRAK1	physical	26496610
KDIS_HUMAN	KIDINS220	physical	26496610
KLC2_HUMAN	KLC2	physical	26496610
KLC4_HUMAN	KLC4	physical	26496610
S38AA_HUMAN	SLC38A10	physical	26496610
KLC3_HUMAN	KLC3	physical	26496610
OSTM1_MOUSE	Ostm1	physical	26598607

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-933, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-166, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-933, AND MASS SPECTROMETRY.
PubMed: 19413330