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Q52LW3

- RHG29_HUMAN

UniProt

Q52LW3 - RHG29_HUMAN

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Protein

Rho GTPase-activating protein 29

Gene

ARHGAP29

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri612 – 65746Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. PDZ domain binding Source: MGI
  3. Rho GTPase activator activity Source: ProtInc

GO - Biological processi

  1. positive regulation of Rho GTPase activity Source: GOC
  2. regulation of small GTPase mediated signal transduction Source: Reactome
  3. Rho protein signal transduction Source: ProtInc
  4. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 29
Alternative name(s):
PTPL1-associated RhoGAP protein 1
Rho-type GTPase-activating protein 29
Gene namesi
Name:ARHGAP29
Synonyms:PARG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30207. ARHGAP29.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394548.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12611261Rho GTPase-activating protein 29PRO_0000317582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711PhosphoserineBy similarity
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei949 – 9491Phosphoserine1 Publication
Modified residuei1019 – 10191Phosphoserine1 Publication
Modified residuei1146 – 11461Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ52LW3.
PaxDbiQ52LW3.
PRIDEiQ52LW3.

PTM databases

PhosphoSiteiQ52LW3.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in skeletal muscle and heart. Expressed at intermediate level in placenta, liver and pancreas. Weakly expressed in brain, lung and kidney.1 Publication

Inductioni

Strongly down-regulated in mantle-cell lymphomas. Up-regulated in migrating glioma cells.2 Publications

Gene expression databases

BgeeiQ52LW3.
CleanExiHS_ARHGAP29.
ExpressionAtlasiQ52LW3. baseline and differential.
GenevestigatoriQ52LW3.

Organism-specific databases

HPAiHPA026534.

Interactioni

Subunit structurei

Interacts with PTPN13/PTPL1. Interacts with RAP2A via its coiled coil domain. Interacts with RASIP1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi114806. 10 interactions.
IntActiQ52LW3. 7 interactions.
MINTiMINT-1465191.
STRINGi9606.ENSP00000260526.

Structurei

3D structure databases

ProteinModelPortaliQ52LW3.
SMRiQ52LW3. Positions 193-469, 612-886.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini671 – 886216Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1258 – 12614Interaction with PTPN13/PTPL1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili296 – 418123Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri612 – 65746Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG310169.
GeneTreeiENSGT00760000119098.
HOGENOMiHOG000043077.
HOVERGENiHBG108406.
InParanoidiQ52LW3.
OMAiEYSNQAR.
PhylomeDBiQ52LW3.
TreeFamiTF351450.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 2 hits.
PROSITEiPS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q52LW3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIAHKQKKTK KKRAWASGQL STDITTSEMG LKSLSSNSIF DPDYIKELVN
60 70 80 90 100
DIRKFSHMLL YLKEAIFSDC FKEVIHIRLE ELLRVLKSIM NKHQNLNSVD
110 120 130 140 150
LQNAAEMLTA KVKAVNFTEV NEENKNDLFQ EVFSSIETLA FTFGNILTNF
160 170 180 190 200
LMGDVGNDSL LRLPVSRETK SFENVSVESV DSSSEKGNFS PLELDNVLLK
210 220 230 240 250
NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNM VKLAEATRTN
260 270 280 290 300
IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM
310 320 330 340 350
EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE
360 370 380 390 400
EEHLSSSGGL AKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR
410 420 430 440 450
NDLENTKREI LAQLRTLVFQ CDLTLKAVTV NLFHMQHLQA ASLADSLQSL
460 470 480 490 500
CDSAKLYDPG QEYSEFVKAT NSTEEEKVDG NVNKHLNSSQ PSGFGPANSL
510 520 530 540 550
EDVVRLPDSS NKIEEDRCSN SADITGPSFI RSWTFGMFSD SESTGGSSES
560 570 580 590 600
RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SETGPNSLGT
610 620 630 640 650
FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFQGVECEE CLLVCHRKCL
660 670 680 690 700
ENLVIICGHQ KLPGKIHLFG AEFTQVAKKE PDGIPFILKI CASEIENRAL
710 720 730 740 750
CLQGIYRVCG NKIKTEKLCQ ALENGMHLVD ISEFSSHDIC DVLKLYLRQL
760 770 780 790 800
PEPFILFRLY KEFIDLAKEI QHVNEEQETK KNSLEDKKWP NMCIEINRIL
810 820 830 840 850
LKSKDLLRQL PASNFNSLHF LIVHLKRVVD HAEENKMNSK NLGVIFGPSL
860 870 880 890 900
IRPRPTTAPI TISSLAEYSN QARLVEFLIT YSQKIFDGSL QPQDVMCSIG
910 920 930 940 950
VVDQGCFPKP LLSPEERDIE RSMKSLFFSS KEDIHTSESE SKIFERATSF
960 970 980 990 1000
EESERKQNAL GKCDACLSDK AQLLLDQEAE SASQKIEDGK TPKPLSLKSD
1010 1020 1030 1040 1050
RSTNNVERHT PRTKIRPVSL PVDRLLLASP PNERNGRNMG NVNLDKFCKN
1060 1070 1080 1090 1100
PAFEGVNRKD AATTVCSKFN GFDQQTLQKI QDKQYEQNSL TAKTTMIMPS
1110 1120 1130 1140 1150
ALQEKGVTTS LQISGDHSIN ATQPSKPYAE PVRSVREASE RRSSDSYPLA
1160 1170 1180 1190 1200
PVRAPRTLQP QHWTTFYKPH APIISIRGNE EKPASPSAAV PPGTDHDPHG
1210 1220 1230 1240 1250
LVVKSMPDPD KASACPGQAT GQPKEDSEEL GLPDVNPMCQ RPRLKRMQQF
1260
EDLEGEIPQF V
Length:1,261
Mass (Da):142,064
Last modified:February 5, 2008 - v2
Checksum:i3E46445EA5DA76C8
GO
Isoform 2 (identifier: Q52LW3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     383-393: EEANELYKVCV → TIFFFFICKLN
     394-1261: Missing.

Note: No experimental confirmation available.

Show »
Length:393
Mass (Da):45,194
Checksum:i6FF8EDA79AB7061C
GO

Sequence cautioni

The sequence AAH67839.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581M → I in AAB81012. (PubMed:9305890)Curated
Sequence conflicti160 – 1601L → F in AAB81012. (PubMed:9305890)Curated
Sequence conflicti166 – 1661S → Y in AAH67839. (PubMed:15489334)Curated
Sequence conflicti212 – 2121A → V in BAD92110. 1 PublicationCurated
Sequence conflicti386 – 3861N → D in AAB81012. (PubMed:9305890)Curated
Sequence conflicti403 – 4031L → V in AAB81012. (PubMed:9305890)Curated
Sequence conflicti446 – 4461S → R in AAB81012. (PubMed:9305890)Curated
Sequence conflicti452 – 4521D → G in AAB81012. (PubMed:9305890)Curated
Sequence conflicti675 – 6751Q → L in AAB81012. (PubMed:9305890)Curated
Sequence conflicti720 – 7201Q → L in AAB81012. (PubMed:9305890)Curated
Sequence conflicti856 – 8561T → Q in AAB81012. (PubMed:9305890)Curated
Sequence conflicti991 – 9911T → A in AAB81012. (PubMed:9305890)Curated
Sequence conflicti1190 – 11901V → C in AAB81012. (PubMed:9305890)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti552 – 5521S → C in a breast cancer sample; somatic mutation. 1 Publication
VAR_038552
Natural varianti1192 – 11921P → L.
Corresponds to variant rs11165091 [ dbSNP | Ensembl ].
VAR_049145
Natural varianti1255 – 12551G → D.2 Publications
Corresponds to variant rs1999272 [ dbSNP | Ensembl ].
VAR_038553

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei383 – 39311EEANELYKVCV → TIFFFFICKLN in isoform 2. 1 PublicationVSP_031058Add
BLAST
Alternative sequencei394 – 1261868Missing in isoform 2. 1 PublicationVSP_031059Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U90920 mRNA. Translation: AAB81012.1.
AL162735 Genomic DNA. Translation: CAH71750.1.
AL162735 Genomic DNA. Translation: CAH71751.1.
CH471097 Genomic DNA. Translation: EAW73052.1.
CH471097 Genomic DNA. Translation: EAW73051.1.
BC022483 mRNA. Translation: AAH22483.1.
BC067839 mRNA. Translation: AAH67839.1. Sequence problems.
BC093741 mRNA. Translation: AAH93741.1.
BC093767 mRNA. Translation: AAH93767.1.
AB208873 mRNA. Translation: BAD92110.1.
CCDSiCCDS748.1. [Q52LW3-1]
PIRiE59430.
RefSeqiNP_004806.3. NM_004815.3. [Q52LW3-1]
UniGeneiHs.483238.

Genome annotation databases

EnsembliENST00000260526; ENSP00000260526; ENSG00000137962. [Q52LW3-1]
ENST00000370217; ENSP00000359237; ENSG00000137962. [Q52LW3-2]
GeneIDi9411.
KEGGihsa:9411.
UCSCiuc001dqj.4. human. [Q52LW3-1]
uc001dql.3. human. [Q52LW3-2]

Polymorphism databases

DMDMi166977701.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U90920 mRNA. Translation: AAB81012.1 .
AL162735 Genomic DNA. Translation: CAH71750.1 .
AL162735 Genomic DNA. Translation: CAH71751.1 .
CH471097 Genomic DNA. Translation: EAW73052.1 .
CH471097 Genomic DNA. Translation: EAW73051.1 .
BC022483 mRNA. Translation: AAH22483.1 .
BC067839 mRNA. Translation: AAH67839.1 . Sequence problems.
BC093741 mRNA. Translation: AAH93741.1 .
BC093767 mRNA. Translation: AAH93767.1 .
AB208873 mRNA. Translation: BAD92110.1 .
CCDSi CCDS748.1. [Q52LW3-1 ]
PIRi E59430.
RefSeqi NP_004806.3. NM_004815.3. [Q52LW3-1 ]
UniGenei Hs.483238.

3D structure databases

ProteinModelPortali Q52LW3.
SMRi Q52LW3. Positions 193-469, 612-886.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114806. 10 interactions.
IntActi Q52LW3. 7 interactions.
MINTi MINT-1465191.
STRINGi 9606.ENSP00000260526.

PTM databases

PhosphoSitei Q52LW3.

Polymorphism databases

DMDMi 166977701.

Proteomic databases

MaxQBi Q52LW3.
PaxDbi Q52LW3.
PRIDEi Q52LW3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260526 ; ENSP00000260526 ; ENSG00000137962 . [Q52LW3-1 ]
ENST00000370217 ; ENSP00000359237 ; ENSG00000137962 . [Q52LW3-2 ]
GeneIDi 9411.
KEGGi hsa:9411.
UCSCi uc001dqj.4. human. [Q52LW3-1 ]
uc001dql.3. human. [Q52LW3-2 ]

Organism-specific databases

CTDi 9411.
GeneCardsi GC01M094616.
H-InvDB HIX0021585.
HGNCi HGNC:30207. ARHGAP29.
HPAi HPA026534.
MIMi 610496. gene.
neXtProti NX_Q52LW3.
PharmGKBi PA128394548.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310169.
GeneTreei ENSGT00760000119098.
HOGENOMi HOG000043077.
HOVERGENi HBG108406.
InParanoidi Q52LW3.
OMAi EYSNQAR.
PhylomeDBi Q52LW3.
TreeFami TF351450.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.

Miscellaneous databases

GenomeRNAii 9411.
NextBioi 35256.
PROi Q52LW3.
SOURCEi Search...

Gene expression databases

Bgeei Q52LW3.
CleanExi HS_ARHGAP29.
ExpressionAtlasi Q52LW3. baseline and differential.
Genevestigatori Q52LW3.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
InterProi IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 2 hits.
PROSITEi PS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1."
    Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H.
    J. Biol. Chem. 272:24333-24338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 64-72; 221-228; 349-357; 456-468; 666-678; 943-946; 971-985; 1015-1024; 1069-1079 AND 1212-1224, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PTPN13, VARIANT ASP-1255.
    Tissue: Skeletal muscle.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Colon.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1261 (ISOFORM 1), VARIANT ASP-1255.
    Tissue: Brain.
  6. "Glioma cell motility is associated with reduced transcription of proapoptotic and proliferation genes: a cDNA microarray analysis."
    Mariani L., Beaudry C., McDonough W.S., Hoelzinger D.B., Demuth T., Ross K.R., Berens T., Coons S.W., Watts G., Trent J.M., Wei J.S., Giese A., Berens M.E.
    J. Neurooncol. 53:161-176(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector."
    Myagmar B.-E., Umikawa M., Asato T., Taira K., Oshiro M., Hino A., Takei K., Uezato H., Kariya K.
    Biochem. Biophys. Res. Commun. 329:1046-1052(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAP2A.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: INDUCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-179; SER-949 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-552.

Entry informationi

Entry nameiRHG29_HUMAN
AccessioniPrimary (citable) accession number: Q52LW3
Secondary accession number(s): O15463
, Q59H86, Q5VYZ0, Q6NVX2, Q8TBI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3