dbPTM

HMHA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMHA1_HUMAN
UniProt AC	Q92619
Protein Name	Rho GTPase-activating protein 45 {ECO:0000312\|HGNC:HGNC:17102}
Gene Name	ARHGAP45 {ECO:0000312\|HGNC:HGNC:17102}
Organism	Homo sapiens (Human).
Sequence Length	1136
Subcellular Localization	Cytoplasm . Cell projection, ruffle membrane .
Protein Description	Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity.; Precursor of the histocompatibility antigen HA-1. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. Specifically, mismatching for mHag HA-1 which is recognized as immunodominant, is shown to be associated with the development of severe GVHD after HLA-identical BMT. HA-1 is presented to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte (CTL) reactivity against hematologic malignancies after treatment by HLA-identical allogenic BMT. It induces cell recognition and lysis by CTL..
Protein Sequence	MFSRKKRELMKTPSISKKNRAGSPSPQPSGELPRKDGADAVFPGPSLEPPAGSSGVKATGTLKRPTSLSRHASAAGFPLSGAASWTLGRSHRSPLTAASPGELPTEGAGPDVVEDISHLLADVARFAEGLEKLKECVLRDDLLEARRPRAHECLGEALRVMHQIISKYPLLNTVETLTAAGTLIAKVKAFHYESNNDLEKQEFEKALETIAVAFSSTVSEFLMGEVDSSTLLAVPPGDSSQSMESLYGPGSEGTPPSLEDCDAGCLPAEEVDVLLQRCEGGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESRVVSNDSDSDLEEASELLSSSEASALGHLSFLEQQQSEASLEVASGSHSGSEEQLEATAREDGDGDEDGPAQQLSGFNTNQSNNVLQAPLPPMRLRGGRMTLGSCRERQPEFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	KKRELMKTPSISKKN HHHHHHCCCCCCCCC	14.33	23401153
14	Phosphorylation	RELMKTPSISKKNRA HHHHCCCCCCCCCCC	44.73	23401153
16	Phosphorylation	LMKTPSISKKNRAGS HHCCCCCCCCCCCCC	41.75	26552605
23	Phosphorylation	SKKNRAGSPSPQPSG CCCCCCCCCCCCCCC	22.63	29255136
25	Phosphorylation	KNRAGSPSPQPSGEL CCCCCCCCCCCCCCC	37.55	23401153
29	Phosphorylation	GSPSPQPSGELPRKD CCCCCCCCCCCCCCC	39.38	23927012
46	Phosphorylation	DAVFPGPSLEPPAGS CCCCCCCCCCCCCCC	51.81	23312004
53	Phosphorylation	SLEPPAGSSGVKATG CCCCCCCCCCCCCCE	26.48	25159151
54	Phosphorylation	LEPPAGSSGVKATGT CCCCCCCCCCCCCEE	46.84	25159151
61	Phosphorylation	SGVKATGTLKRPTSL CCCCCCEEECCCCCC	25.42	23401153
66	Phosphorylation	TGTLKRPTSLSRHAS CEEECCCCCCCCCHH	46.46	23401153
67	Phosphorylation	GTLKRPTSLSRHASA EEECCCCCCCCCHHH	27.34	23401153
69	Phosphorylation	LKRPTSLSRHASAAG ECCCCCCCCCHHHCC	23.06	28270605
73	Phosphorylation	TSLSRHASAAGFPLS CCCCCCHHHCCCCCC	16.72	23401153
80	Phosphorylation	SAAGFPLSGAASWTL HHCCCCCCCHHHHCC	26.99	30576142
84	Phosphorylation	FPLSGAASWTLGRSH CCCCCHHHHCCCCCC	21.76	28450419
86	Phosphorylation	LSGAASWTLGRSHRS CCCHHHHCCCCCCCC	19.48	28122231
89	Phosphorylation	AASWTLGRSHRSPLT HHHHCCCCCCCCCCC	32.19	27251275
90	Phosphorylation	ASWTLGRSHRSPLTA HHHCCCCCCCCCCCC	22.81	22115753
93	Phosphorylation	TLGRSHRSPLTAASP CCCCCCCCCCCCCCC	20.88	25159151
96	Phosphorylation	RSHRSPLTAASPGEL CCCCCCCCCCCCCCC	24.46	22115753
99	Phosphorylation	RSPLTAASPGELPTE CCCCCCCCCCCCCCC	30.85	25159151
102	Phosphorylation	LTAASPGELPTEGAG CCCCCCCCCCCCCCC	55.76	27251275
105	Phosphorylation	ASPGELPTEGAGPDV CCCCCCCCCCCCCCH	60.73	22115753
109	Phosphorylation	ELPTEGAGPDVVEDI CCCCCCCCCCHHHHH	29.78	27251275
112	Phosphorylation	TEGAGPDVVEDISHL CCCCCCCHHHHHHHH	5.97	27251275
115	Phosphorylation	AGPDVVEDISHLLAD CCCCHHHHHHHHHHH	35.76	27251275
117	Phosphorylation	PDVVEDISHLLADVA CCHHHHHHHHHHHHH	22.02	28060719
132	Ubiquitination	RFAEGLEKLKECVLR HHHHHHHHHHHHHHC	70.65	-
134	Ubiquitination	AEGLEKLKECVLRDD HHHHHHHHHHHHCHH	61.20	-
166	O-linked_Glycosylation	RVMHQIISKYPLLNT HHHHHHHHCCCCCCH	27.97	29351928
166	Phosphorylation	RVMHQIISKYPLLNT HHHHHHHHCCCCCCH	27.97	24719451
188	Ubiquitination	GTLIAKVKAFHYESN HHHHHHHHHHHHCCC	44.63	-
194	Phosphorylation	VKAFHYESNNDLEKQ HHHHHHCCCCHHHHH	33.49	-
295	Phosphorylation	YAKNMAKYMKDLISY HHHHHHHHHHHHHHH	10.40	22817900
305	Acetylation	DLISYLEKRTTLEME HHHHHHHHHHCHHHH	53.07	23749302
307	Phosphorylation	ISYLEKRTTLEMEFA HHHHHHHHCHHHHHH	46.96	24719451
321	Acetylation	AKGLQKIAHNCRQSV HHHHHHHHHHHHHHH	8.55	19608861
385	Acetylation	EKRRKEIKEAWHRAQ HHHHHHHHHHHHHHH	42.33	26822725
394	Ubiquitination	AWHRAQRKLQEAESN HHHHHHHHHHHHHHH	42.30	-
433	Phosphorylation	AEEEQAGSAPGAGST HHHHHCCCCCCCCCH	34.01	28060719
439	Phosphorylation	GSAPGAGSTATKTLD CCCCCCCCHHHHHHH	17.84	30576142
440	Phosphorylation	SAPGAGSTATKTLDK CCCCCCCHHHHHHHH	37.11	30576142
442	Phosphorylation	PGAGSTATKTLDKRR CCCCCHHHHHHHHHH	25.34	28450419
444	O-linked_Glycosylation	AGSTATKTLDKRRRL CCCHHHHHHHHHHHH	35.52	29351928
444	Phosphorylation	AGSTATKTLDKRRRL CCCHHHHHHHHHHHH	35.52	28450419
465	Phosphorylation	KAEEAMATYRTCVAD HHHHHHHHHHHHHHC	10.64	-
466	Phosphorylation	AEEAMATYRTCVADA HHHHHHHHHHHHHCH	8.39	-
468	Phosphorylation	EAMATYRTCVADAKT HHHHHHHHHHHCHHH	10.83	-
474	Acetylation	RTCVADAKTQKQELE HHHHHCHHHHHHHHH	52.62	25953088
474	Ubiquitination	RTCVADAKTQKQELE HHHHHCHHHHHHHHH	52.62	-
477	Acetylation	VADAKTQKQELEDTK HHCHHHHHHHHHHHH	51.47	18526177
484	Acetylation	KQELEDTKVTALRQI HHHHHHHHHHHHHHH	50.32	25953088
484	Ubiquitination	KQELEDTKVTALRQI HHHHHHHHHHHHHHH	50.32	-
534	Phosphorylation	LCESSKLYDPGQQYA HHCCCCCCCCHHHHH	24.67	28796482
540	Phosphorylation	LYDPGQQYASHVRQL CCCCHHHHHHHHHHH	11.37	28796482
542	Phosphorylation	DPGQQYASHVRQLQR CCHHHHHHHHHHHHH	19.99	28796482
557	Phosphorylation	DQEPDVHYDFEPHVS CCCCCCCCCCCCCCC	23.36	23927012
564	Phosphorylation	YDFEPHVSANAWSPV CCCCCCCCCCCCCHH	16.87	22167270
569	Phosphorylation	HVSANAWSPVMRARK CCCCCCCCHHHHHHH	12.76	22167270
577	Phosphorylation	PVMRARKSSFNVSDV HHHHHHHCCCCHHHH	34.31	23401153
578	Phosphorylation	VMRARKSSFNVSDVA HHHHHHCCCCHHHHC	24.71	29255136
582	Phosphorylation	RKSSFNVSDVARPEA HHCCCCHHHHCCHHH	27.72	29255136
585	Phosphorylation	SFNVSDVARPEAAGS CCCHHHHCCHHHCCC	26.71	27251275
592	Phosphorylation	ARPEAAGSPPEEGGC CCHHHCCCCCCCCCC	32.33	23401153
594	Phosphorylation	PEAAGSPPEEGGCTE HHHCCCCCCCCCCCC	54.70	27251275
598	Phosphorylation	GSPPEEGGCTEGTPA CCCCCCCCCCCCCCC	20.60	27251275
600	Phosphorylation	PPEEGGCTEGTPAKD CCCCCCCCCCCCCCC	40.50	23927012
603	Phosphorylation	EGGCTEGTPAKDHRA CCCCCCCCCCCCCCC	17.53	23927012
608	Phosphorylation	EGTPAKDHRAGRGHQ CCCCCCCCCCCCCCC	22.30	27251275
616	Phosphorylation	RAGRGHQVHKSWPLS CCCCCCCCCCCCCCC	5.21	27251275
619	Phosphorylation	RGHQVHKSWPLSISD CCCCCCCCCCCCCCC	21.03	23401153
623	Phosphorylation	VHKSWPLSISDSDSG CCCCCCCCCCCCCCC	18.90	23927012
625	Phosphorylation	KSWPLSISDSDSGLD CCCCCCCCCCCCCCC	27.90	23927012
627	Phosphorylation	WPLSISDSDSGLDPG CCCCCCCCCCCCCCC	27.21	23927012
629	Phosphorylation	LSISDSDSGLDPGPG CCCCCCCCCCCCCCC	45.25	23927012
635	Phosphorylation	DSGLDPGPGAGDFKK CCCCCCCCCCCCHHH	34.54	27251275
643	Phosphorylation	GAGDFKKFERTSSSG CCCCHHHEEECCCCC	8.72	27251275
646	Phosphorylation	DFKKFERTSSSGTMS CHHHEEECCCCCCCC	26.26	27080861
647	Phosphorylation	FKKFERTSSSGTMSS HHHEEECCCCCCCCC	28.82	27080861
648	Phosphorylation	KKFERTSSSGTMSST HHEEECCCCCCCCCC	31.97	27080861
649	Phosphorylation	KFERTSSSGTMSSTE HEEECCCCCCCCCCE	37.74	27080861
651	Phosphorylation	ERTSSSGTMSSTEEL EECCCCCCCCCCEEC	18.81	27080861
653	Phosphorylation	TSSSGTMSSTEELVD CCCCCCCCCCEECCC	33.67	27080861
654	Phosphorylation	SSSGTMSSTEELVDP CCCCCCCCCEECCCC	29.08	27080861
655	Phosphorylation	SSGTMSSTEELVDPD CCCCCCCCEECCCCC	26.60	27080861
667	Phosphorylation	DPDGGAGASAFEQAD CCCCCCCCHHHHHHC	9.35	27251275
668	Phosphorylation	PDGGAGASAFEQADL CCCCCCCHHHHHHCC	32.35	27080861
679	Phosphorylation	QADLNGMTPELPVAV HHCCCCCCCCCCEEC	18.27	27080861
737	Ubiquitination	ECCLACHKKCLETLA HHHHHHHHHHHHHHH	45.10	-
738	Ubiquitination	CCLACHKKCLETLAI HHHHHHHHHHHHHHH	22.01	-
816	Ubiquitination	CQAFENGKELVELSQ HHHHHCCHHHHHHHH	60.50	-
834	Ubiquitination	HDISNVLKLYLRQLP CHHHHHHHHHHHCCC	30.70	-
846	Phosphorylation	QLPEPLISFRLYHEL CCCCCCHHHHHHHHH	16.40	24719451
858	Ubiquitination	HELVGLAKDSLKAEA HHHHHHHHHHHHHHH	53.55	-
862	Ubiquitination	GLAKDSLKAEAEAKA HHHHHHHHHHHHHHH	48.40	-
878	Phosphorylation	SRGRQDGSESEAVAV HCCCCCCCHHHHHHH	46.36	28270605
880	Phosphorylation	GRQDGSESEAVAVAL CCCCCCHHHHHHHHH	32.33	28270605
896	Phosphorylation	GRLRELLRDLPPENR HHHHHHHHCCCCCCH	56.92	27251275
926	Phosphorylation	VEQDNKMTPGNLGIV HHCCCCCCCCCCEEE	29.65	26434776
937	Phosphorylation	LGIVFGPTLLRPRPT CEEEECCCCCCCCCC	38.51	26434776
944	Phosphorylation	TLLRPRPTEATVSLS CCCCCCCCCCEEEHH	39.26	23663014
947	Phosphorylation	RPRPTEATVSLSSLV CCCCCCCEEEHHHHC	12.37	29255136
949	Phosphorylation	RPTEATVSLSSLVDY CCCCCEEEHHHHCCC	20.41	29255136
951	Phosphorylation	TEATVSLSSLVDYPH CCCEEEHHHHCCCHH	17.70	23401153
952	Phosphorylation	EATVSLSSLVDYPHQ CCEEEHHHHCCCHHH	37.39	29255136
956	Phosphorylation	SLSSLVDYPHQARVI EHHHHCCCHHHHHHH	8.64	23663014
968	Phosphorylation	RVIETLIVHYGLVFE HHHHHHHHHHCEEEC	2.98	27251275
1001	Phosphorylation	EVVVQVPYLEAGEAV EEEEECCCCCCCCEE	20.51	23532336
1023	Phosphorylation	AADGCRESRVVSNDS HCCCCCCCCCCCCCC	15.83	28122231
1027	Phosphorylation	CRESRVVSNDSDSDL CCCCCCCCCCCCCCH	31.87	-
1030	Phosphorylation	SRVVSNDSDSDLEEA CCCCCCCCCCCHHHH	43.17	22468782
1032	Phosphorylation	VVSNDSDSDLEEASE CCCCCCCCCHHHHHH	48.31	22468782
1038	Phosphorylation	DSDLEEASELLSSSE CCCHHHHHHHHHHHH	31.86	24275569
1047	Phosphorylation	LLSSSEASALGHLSF HHHHHHHHHHHHHHH	21.70	26074081
1053	Phosphorylation	ASALGHLSFLEQQQS HHHHHHHHHHHHHHC	23.31	26074081
1068	Phosphorylation	EASLEVASGSHSGSE HHHEEECCCCCCCCH	46.10	26074081
1070	Phosphorylation	SLEVASGSHSGSEEQ HEEECCCCCCCCHHH	16.40	26074081
1072	Phosphorylation	EVASGSHSGSEEQLE EECCCCCCCCHHHHH	45.79	26074081
1074	Phosphorylation	ASGSHSGSEEQLEAT CCCCCCCCHHHHHHH	40.76	26074081
1127	Phosphorylation	GGRMTLGSCRERQPE CCCCCCCCHHHCCCC	17.08	30001349

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 HMHA1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HMHA1_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 HMHA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HMHA1_HUMAN !!

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 HMHA1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-305, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-73; SER-93;SER-99; SER-569 AND SER-619, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND MASSSPECTROMETRY.	16964243 [Abstract]