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Q9H7F0

- AT133_HUMAN

UniProt

Q9H7F0 - AT133_HUMAN

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Protein

Probable cation-transporting ATPase 13A3

Gene

ATP13A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei498 – 49814-aspartylphosphate intermediateBy similarity
Metal bindingi883 – 8831MagnesiumBy similarity
Metal bindingi887 – 8871MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cation-transporting ATPase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cation-transporting ATPase 13A3 (EC:3.6.3.-)
Alternative name(s):
ATPase family homolog up-regulated in senescence cells 1
Gene namesi
Name:ATP13A3
Synonyms:AFURS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:24113. ATP13A3.

Subcellular locationi

Membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921HelicalSequence AnalysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence AnalysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence AnalysisAdd
BLAST
Transmembranei410 – 43021HelicalSequence AnalysisAdd
BLAST
Transmembranei449 – 46921HelicalSequence AnalysisAdd
BLAST
Transmembranei941 – 96121HelicalSequence AnalysisAdd
BLAST
Transmembranei963 – 98321HelicalSequence AnalysisAdd
BLAST
Transmembranei1000 – 102021HelicalSequence AnalysisAdd
BLAST
Transmembranei1074 – 109421HelicalSequence AnalysisAdd
BLAST
Transmembranei1106 – 112621HelicalSequence AnalysisAdd
BLAST
Transmembranei1144 – 116421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134971145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12261226Probable cation-transporting ATPase 13A3PRO_0000046425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Phosphoserine2 Publications
Modified residuei817 – 8171Phosphoserine6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H7F0.
PaxDbiQ9H7F0.
PRIDEiQ9H7F0.

PTM databases

PhosphoSiteiQ9H7F0.

Expressioni

Gene expression databases

BgeeiQ9H7F0.
CleanExiHS_ATP13A3.
ExpressionAtlasiQ9H7F0. baseline and differential.
GenevestigatoriQ9H7F0.

Organism-specific databases

HPAiHPA029471.

Interactioni

Protein-protein interaction databases

BioGridi122719. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9H7F0.
SMRiQ9H7F0. Positions 163-1027.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 2344Poly-Tyr

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00530000063001.
HOGENOMiHOG000171813.
HOVERGENiHBG065757.
InParanoidiQ9H7F0.
KOiK14951.
OMAiENRHRIS.
OrthoDBiEOG7B5WV2.
PhylomeDBiQ9H7F0.
TreeFamiTF300331.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 3 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H7F0-1) [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
MDREERKTIN QGQEDEMEIY GYNLSRWKLA IVSLGVICSG GFLLLLLYWM
60 70 80 90 100
PEWRVKATCV RAAIKDCEVV LLRTTDEFKM WFCAKIRVLS LETYPVSSPK
110 120 130 140 150
SMSNKLSNGH AVCLIENPTE ENRHRISKYS QTESQQIRYF THHSVKYFWN
160 170 180 190 200
DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT KGMHAYRKLL YGVNEIAVKV
210 220 230 240 250
PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV MSIVSIVSSL
260 270 280 290 300
YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN
310 320 330 340 350
GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN
360 370 380 390 400
PETHKRHTLF CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK
410 420 430 440 450
PTDFKLYRDA YLFLLCLVAV AGIGFIYTII NSILNEVQVG VIIIESLDII
460 470 480 490 500
TITVPPALPA AMTAGIVYAQ RRLKKIGIFC ISPQRINICG QLNLVCFDKT
510 520 530 540 550
GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA CMATCHSLTK
560 570 580 590 600
IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE
610 620 630 640 650
STPAGNQEME LFELPATYEI GIVRQFPFSS ALQRMSVVAR VLGDRKMDAY
660 670 680 690 700
MKGAPEAIAG LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH
710 720 730 740 750
KVQNISRDAI ENNMDFMGLI IMQNKLKQET PAVLEDLHKA NIRTVMVTGD
760 770 780 790 800
SMLTAVSVAR DCGMILPQDK VIIAEALPPK DGKVAKINWH YADSLTQCSH
810 820 830 840 850
PSAIDPEAIP VKLVHDSLED LQMTRYHFAM NGKSFSVILE HFQDLVPKLM
860 870 880 890 900
LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL
910 920 930 940 950
SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY
960 970 980 990 1000
FSVTLLYSIL SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG
1010 1020 1030 1040 1050
LISGALLFSV LSQIIICIGF QSLGFFWVKQ QPWYEVWHPK SDACNTTGSG
1060 1070 1080 1090 1100
FWNSSHVDNE TELDEHNIQN YENTTVFFIS SFQYLIVAIA FSKGKPFRQP
1110 1120 1130 1140 1150
CYKNYFFVFS VIFLYIFILF IMLYPVASVD QVLQIVCVPY QWRVTMLIIV
1160 1170 1180 1190 1200
LVNAFVSITV EESVDRWGKC CLPWALGCRK KTPKAKYMYL AQELLVDPEW
1210 1220
PPKPQTTTEA KALVKENGSC QIITIT
Length:1,226
Mass (Da):138,043
Last modified:February 10, 2009 - v4
Checksum:i8DD1C0451223C7AB
GO
Isoform 2 (identifier: Q9H7F0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-277: Missing.
     278-279: NE → MS
     936-978: FCVFKFMALY...LFIDLAIILV → SCELALFSIV...FHNCAFYSLV
     979-1226: Missing.

Note: Dubious isoform produced through aberrant splice sites.

Show »
Length:701
Mass (Da):77,310
Checksum:i7927AFFE8413247F
GO

Sequence cautioni

The sequence BAB14942.1 differs from that shown. Reason: Frameshift at position 1065. Curated
The sequence BAB14942.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11398.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471E → Q in CAC84902. (PubMed:11867234)Curated
Sequence conflicti730 – 7301T → P in CAC84902. (PubMed:11867234)Curated
Sequence conflicti784 – 7841V → F in BAC11398. (PubMed:14702039)Curated
Sequence conflicti807 – 8071E → G in BAC11398. (PubMed:14702039)Curated
Sequence conflicti964 – 9641G → R in BAC11398. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 277277Missing in isoform 2. 1 PublicationVSP_007314Add
BLAST
Alternative sequencei278 – 2792NE → MS in isoform 2. 1 PublicationVSP_036300
Alternative sequencei936 – 97843FCVFK…AIILV → SCELALFSIVTYSLDHFIIS ILISSMLVLFFSDFHNCAFY SLV in isoform 2. 1 PublicationVSP_007315Add
BLAST
Alternative sequencei979 – 1226248Missing in isoform 2. 1 PublicationVSP_007316Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ306929 mRNA. Translation: CAC84902.1.
AC108676 Genomic DNA. No translation available.
AC125362 Genomic DNA. No translation available.
AK024639 mRNA. Translation: BAB14942.1. Sequence problems.
AK075094 mRNA. Translation: BAC11398.1. Different initiation.
CCDSiCCDS43187.1. [Q9H7F0-1]
RefSeqiNP_078800.3. NM_024524.3. [Q9H7F0-1]
UniGeneiHs.529609.

Genome annotation databases

EnsembliENST00000256031; ENSP00000256031; ENSG00000133657. [Q9H7F0-1]
ENST00000439040; ENSP00000416508; ENSG00000133657. [Q9H7F0-1]
GeneIDi79572.
KEGGihsa:79572.
UCSCiuc003fty.4. human. [Q9H7F0-1]

Polymorphism databases

DMDMi223590262.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ306929 mRNA. Translation: CAC84902.1 .
AC108676 Genomic DNA. No translation available.
AC125362 Genomic DNA. No translation available.
AK024639 mRNA. Translation: BAB14942.1 . Sequence problems.
AK075094 mRNA. Translation: BAC11398.1 . Different initiation.
CCDSi CCDS43187.1. [Q9H7F0-1 ]
RefSeqi NP_078800.3. NM_024524.3. [Q9H7F0-1 ]
UniGenei Hs.529609.

3D structure databases

ProteinModelPortali Q9H7F0.
SMRi Q9H7F0. Positions 163-1027.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122719. 6 interactions.

PTM databases

PhosphoSitei Q9H7F0.

Polymorphism databases

DMDMi 223590262.

Proteomic databases

MaxQBi Q9H7F0.
PaxDbi Q9H7F0.
PRIDEi Q9H7F0.

Protocols and materials databases

DNASUi 79572.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256031 ; ENSP00000256031 ; ENSG00000133657 . [Q9H7F0-1 ]
ENST00000439040 ; ENSP00000416508 ; ENSG00000133657 . [Q9H7F0-1 ]
GeneIDi 79572.
KEGGi hsa:79572.
UCSCi uc003fty.4. human. [Q9H7F0-1 ]

Organism-specific databases

CTDi 79572.
GeneCardsi GC03M194123.
HGNCi HGNC:24113. ATP13A3.
HPAi HPA029471.
MIMi 610232. gene.
neXtProti NX_Q9H7F0.
PharmGKBi PA134971145.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0474.
GeneTreei ENSGT00530000063001.
HOGENOMi HOG000171813.
HOVERGENi HBG065757.
InParanoidi Q9H7F0.
KOi K14951.
OMAi ENRHRIS.
OrthoDBi EOG7B5WV2.
PhylomeDBi Q9H7F0.
TreeFami TF300331.

Miscellaneous databases

ChiTaRSi ATP13A3. human.
GeneWikii ATP13A3.
GenomeRNAii 79572.
NextBioi 68532.
PROi Q9H7F0.
SOURCEi Search...

Gene expression databases

Bgeei Q9H7F0.
CleanExi HS_ATP13A3.
ExpressionAtlasi Q9H7F0. baseline and differential.
Genevestigatori Q9H7F0.

Family and domain databases

Gene3Di 2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProi IPR004014. ATPase_P-typ_cation-transptr_N.
IPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view ]
Pfami PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SUPFAMi SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsi TIGR01494. ATPase_P-type. 3 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning the AFURS1 gene which is up-regulated in senescent human parenchymal kidney cells."
    Habtemichael N., Kovacs G.
    Gene 283:271-275(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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.
    , 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 402-1226 (ISOFORM 1).
    Tissue: Coronary artery and Placenta.
  4. "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-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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 SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAT133_HUMAN
AccessioniPrimary (citable) accession number: Q9H7F0
Secondary accession number(s): Q8NC11, Q96KS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 10, 2009
Last modified: November 26, 2014
This is version 119 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3