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Q14C86 (GAPD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTPase-activating protein and VPS9 domain-containing protein 1
Alternative name(s):
GAPex-5
Rab5-activating protein 6
Gene names
Name:GAPVD1
Synonyms:GAPEX5, KIAA1521, RAP6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1478 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras. Ref.1

Subunit structure

Interacts with TRIP10/CIP4 By similarity. Interacts with RAB5A. Ref.1

Subcellular location

Membrane; Peripheral membrane protein. Endosome. Note: Recruited to the plasma membrane by TRIP10/CIP4 in response to insulin. Ref.1

Sequence similarities

Belongs to the GAPVD1 family.

Contains 1 Ras-GAP domain.

Contains 1 VPS9 domain.

Sequence caution

The sequence AAH21119.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH21119.1 differs from that shown. Reason: Frameshift at position 742.

The sequence BAA90959.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA90959.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA96045.3 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14C86-1)

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.
Isoform 2 (identifier: Q14C86-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1057-1074: Missing.
Isoform 3 (identifier: Q14C86-3)

The sequence of this isoform differs from the canonical sequence as follows:
     989-1015: Missing.
     1057-1074: Missing.
Isoform 4 (identifier: Q14C86-4)

The sequence of this isoform differs from the canonical sequence as follows:
     557-577: Missing.
     1057-1074: Missing.
Isoform 5 (identifier: Q14C86-5)

The sequence of this isoform differs from the canonical sequence as follows:
     810-835: Missing.
Isoform 6 (identifier: Q14C86-6)

The sequence of this isoform differs from the canonical sequence as follows:
     810-810: G → DFLYILQPKQHFQHIEAEADMRIQLSSS
     1057-1074: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14781478GTPase-activating protein and VPS9 domain-containing protein 1
PRO_0000324771

Regions

Domain131 – 353223Ras-GAP
Domain1338 – 1478141VPS9

Amino acid modifications

Modified residue3901Phosphothreonine Ref.9 Ref.12 Ref.13 Ref.16
Modified residue4581Phosphothreonine Ref.13
Modified residue4661Phosphoserine Ref.13 Ref.15
Modified residue4701Phosphothreonine Ref.13
Modified residue5661Phosphoserine Ref.13
Modified residue7661Phosphoserine Ref.15
Modified residue9021Phosphoserine Ref.13 Ref.15 Ref.16 Ref.18
Modified residue9031Phosphoserine Ref.13
Modified residue9661Phosphoserine Ref.16
Modified residue10191Phosphoserine Ref.9 Ref.12 Ref.13 Ref.16
Modified residue10961Phosphoserine Ref.11 Ref.13 Ref.15
Modified residue11051Phosphoserine By similarity

Natural variations

Alternative sequence557 – 57721Missing in isoform 4.
VSP_032358
Alternative sequence810 – 83526Missing in isoform 5.
VSP_032359
Alternative sequence8101G → DFLYILQPKQHFQHIEAEAD MRIQLSSS in isoform 6.
VSP_032360
Alternative sequence989 – 101527Missing in isoform 3.
VSP_032361
Alternative sequence1057 – 107418Missing in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_032362

Experimental info

Sequence conflict2941V → E in ABB71126. Ref.1
Sequence conflict3061C → R in ABB71126. Ref.1
Sequence conflict3521A → T in BAA90959. Ref.7
Sequence conflict3661S → C in ABB71126. Ref.1
Sequence conflict4191N → D in BAA90959. Ref.7
Sequence conflict4551L → F in ABB71126. Ref.1
Sequence conflict4711P → L in ABB71126. Ref.1
Sequence conflict5301M → I in AAH21119. Ref.6
Sequence conflict5321E → G in BAA90959. Ref.7
Sequence conflict7411C → F in AAH21119. Ref.6
Sequence conflict9021S → G in BAA90959. Ref.7
Sequence conflict9311P → S in AAH13635. Ref.6
Sequence conflict10371R → W in ABB71126. Ref.1
Sequence conflict11621L → S in ABB71126. Ref.1
Sequence conflict14251V → L in ABB71126. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: DD429B0EB207276C

FASTA1,478164,980
        10         20         30         40         50         60 
MVKLDIHTLA HHLKQERLYV NSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII 

        70         80         90        100        110        120 
TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL 

       130        140        150        160        170        180 
NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI 

       190        200        210        220        230        240 
LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPSQ QEKLFGEKGS 

       250        260        270        280        290        300 
DRFRQKVQEM VESNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG 

       310        320        330        340        350        360 
EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGSEEGD 

       370        380        390        400        410        420 
PRTKSSLGKF DKSCVAAFLD VVIGGRAVET PPLSSVNLLE GLSRTVVYIT YSQLITLVNF 

       430        440        450        460        470        480 
MKSVMSGDQL REDRMALDNL LANLPPAKPG KSSSLEMTPY NTPQLSPATT PANKKNRLPI 

       490        500        510        520        530        540 
ATRSRSRTNM LMDLHMDHEG SSQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL 

       550        560        570        580        590        600 
SDGGQGDVPV DENKLHGKPD KTLRFSLCSD NLEGISEGPS NRSNSVSSLD LEGESVSELG 

       610        620        630        640        650        660 
AGPSGSNGVE ALQLLEHEQA TTQDNLDDKL RKFEIRDMMG LTDDRDISET VSETWSTDVL 

       670        680        690        700        710        720 
GSDFDPNIDE DRLQEIAGAA AENMLGSLLC LPGSGSVLLD PCTGSTISET TSEAWSVEVL 

       730        740        750        760        770        780 
PSDSEAPDLK QEERLQELES CSGLGSTSDD TDVREVSSRP STPGLSVVSG ISATSEDIPN 

       790        800        810        820        830        840 
KIEDLRSECS SDFGGKDSVT SPDMDEITHG AHQLTSPPSQ SESLLAMFDP LSSHEGASAV 

       850        860        870        880        890        900 
VRPKVHYARP SHPPPDPPIL EGAVGGNEAR LPNFGSHVLT PAEMEAFKQR HSYPERLVRS 

       910        920        930        940        950        960 
RSSDIVSSVR RPMSDPSWNR RPGNEERELP PAAAIGATSL VAAPHSSSSS PSKDSSRGET 

       970        980        990       1000       1010       1020 
EERKDSDDEK SDRNRPWWRK RFVSAMPKAP IPFRKKEKQE KDKDDLGPDR FSTLTDDPSP 

      1030       1040       1050       1060       1070       1080 
RLSAQAQVAE DILDKYRNAI KRTSPSDGAM ANYESTGDNH DRDLSSKLLY HSDKEVMGDG 

      1090       1100       1110       1120       1130       1140 
ESAHDSPRDE ALQNISADDL PDSASQAAHP QDSAFSYRDA KKKLRLALCS ADSVAFPVLT 

      1150       1160       1170       1180       1190       1200 
HSTRNGLPDH TDPEDNEIVC FLKVQIAEAI NLQDKNLMAQ LQETMRCVCR FDNRTCRKLL 

      1210       1220       1230       1240       1250       1260 
ASIAEDYRKR APYIAYLTRC RQGLQTTQAH LERLLQRVLR DKEVANRYFT TVCVRLLLES 

      1270       1280       1290       1300       1310       1320 
KEKKIREFIQ DFQKLTAADD KTAQVEDFLQ FLYGAMAQDV IWQNASEEQL QDAQLAIERS 

      1330       1340       1350       1360       1370       1380 
VMNRIFKLAF YPNQDGDILR DQVLHEHIQR LSKVVTANHR ALQIPEVYLR EAPWPSAQSE 

      1390       1400       1410       1420       1430       1440 
IRTISAYKTP RDKVQCILRM CSTIMNLLSL ANEDSVPGAD DFVPVLVFVL IKANPPCLLS 

      1450       1460       1470 
TVQYISSFYA SCLSGEESYW WMQFTAAVEF IKTIDDRK 

« Hide

Isoform 2 [UniParc].

Checksum: FC321A20FB94016F
Show »

FASTA1,460162,898
Isoform 3 [UniParc].

Checksum: C0F51AB2B99F64A5
Show »

FASTA1,433159,755
Isoform 4 [UniParc].

Checksum: D4B3957383169E05
Show »

FASTA1,439160,606
Isoform 5 [UniParc].

Checksum: D139984862F731BB
Show »

FASTA1,452162,231
Isoform 6 [UniParc].

Checksum: 9065582BC51473FB
Show »

FASTA1,487166,168

References

« Hide 'large scale' references
[1]"Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis."
Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L., Barbieri M.A.
Biochem. Biophys. Res. Commun. 340:967-975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A.
[2]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 2 AND 3).
Tissue: Placenta.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-996 (ISOFORM 5).
Tissue: Colon.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-1478 (ISOFORM 6).
Tissue: Testis.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390; THR-458; SER-466; THR-470; SER-566; SER-902; SER-903; SER-1019 AND SER-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-766; SER-902 AND SER-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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 THR-390; SER-902; SER-966 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ233254 mRNA. Translation: ABB71126.1.
AB040954 mRNA. Translation: BAA96045.3. Different initiation.
AL627223, AL354710 Genomic DNA. Translation: CAH71014.2.
AL627223, AL354710 Genomic DNA. Translation: CAO03611.1.
AL354710, AL627223 Genomic DNA. Translation: CAQ08737.1.
AL627223, AL354710 Genomic DNA. Translation: CAO03610.1.
AL354710, AL627223 Genomic DNA. Translation: CAQ08735.1.
AL354710, AL627223 Genomic DNA. Translation: CAQ08736.1.
CH471090 Genomic DNA. Translation: EAW87622.1.
CH471090 Genomic DNA. Translation: EAW87623.1.
BC013635 mRNA. Translation: AAH13635.1.
BC021119 mRNA. Translation: AAH21119.1. Sequence problems.
BC114937 mRNA. Translation: AAI14938.1.
BC114962 mRNA. Translation: AAI14963.1.
AK000126 mRNA. Translation: BAA90959.1. Sequence problems.
AL080196 mRNA. Translation: CAB45770.1.
AL834325 mRNA. Translation: CAD38993.1.
PIRT12506.
RefSeqNP_001269608.1. NM_001282679.1.
NP_001269609.1. NM_001282680.1.
NP_001269610.1. NM_001282681.1.
XP_005251958.1. XM_005251901.1.
XP_005251961.1. XM_005251904.1.
UniGeneHs.495134.

3D structure databases

ProteinModelPortalQ14C86.
SMRQ14C86. Positions 1263-1477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117568. 17 interactions.
IntActQ14C86. 4 interactions.
MINTMINT-1631145.

Polymorphism databases

DMDM172046859.

Proteomic databases

PaxDbQ14C86.
PRIDEQ14C86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265956; ENSP00000265956; ENSG00000165219. [Q14C86-5]
ENST00000297933; ENSP00000297933; ENSG00000165219. [Q14C86-2]
ENST00000312123; ENSP00000309582; ENSG00000165219. [Q14C86-4]
ENST00000394104; ENSP00000377664; ENSG00000165219. [Q14C86-1]
ENST00000394105; ENSP00000377665; ENSG00000165219. [Q14C86-6]
ENST00000470056; ENSP00000419767; ENSG00000165219. [Q14C86-3]
ENST00000495955; ENSP00000419063; ENSG00000165219. [Q14C86-1]
GeneID26130.
KEGGhsa:26130.
UCSCuc004bpp.3. human. [Q14C86-6]
uc004bpq.3. human. [Q14C86-2]
uc004bpr.3. human. [Q14C86-4]
uc004bps.3. human. [Q14C86-3]
uc010mwx.3. human. [Q14C86-1]
uc010mwy.1. human. [Q14C86-5]

Organism-specific databases

CTD26130.
GeneCardsGC09P128024.
H-InvDBHIX0008383.
HGNCHGNC:23375. GAPVD1.
HPAHPA029386.
HPA029387.
MIM611714. gene.
neXtProtNX_Q14C86.
PharmGKBPA142671748.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275317.
HOVERGENHBG107936.
OMAEMVDSNE.
PhylomeDBQ14C86.
TreeFamTF105908.

Gene expression databases

ArrayExpressQ14C86.
BgeeQ14C86.
GenevestigatorQ14C86.

Family and domain databases

Gene3D1.10.506.10. 1 hit.
InterProIPR001936. RasGAP.
IPR008936. Rho_GTPase_activation_prot.
IPR003123. VPS9.
IPR013995. VPS9_subgr.
[Graphical view]
PfamPF00616. RasGAP. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
SMARTSM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGAPVD1. human.
GeneWikiGAPVD1.
GenomeRNAi26130.
NextBio48153.
PMAP-CutDBQ14C86.
PROQ14C86.
SOURCESearch...

Entry information

Entry nameGAPD1_HUMAN
AccessionPrimary (citable) accession number: Q14C86
Secondary accession number(s): A8MYK3 expand/collapse secondary AC list , B0QZ62, B0QZ63, B0QZ64, Q14C76, Q2Q1W1, Q8ND92, Q8WU86, Q96CZ4, Q9NXQ1, Q9P207, Q9Y4N0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM