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Protein

MAP7 domain-containing protein 1

Gene

MAP7D1

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
MAP7 domain-containing protein 1
Alternative name(s):
Arginine/proline-rich coiled-coil domain-containing protein 1
Proline/arginine-rich coiled-coil domain-containing protein 1
Gene namesi
Name:MAP7D1
Synonyms:KIAA1187, PARCC1, RPRC1
ORF Names:PP2464
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25514. MAP7D1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394970.

Polymorphism and mutation databases

BioMutaiMAP7D1.
DMDMi121942584.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 841841MAP7 domain-containing protein 1PRO_0000306807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471PhosphothreonineCombined sources
Modified residuei51 – 511PhosphothreonineCombined sources
Modified residuei70 – 701PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei399 – 3991PhosphoserineCombined sources
Cross-linki439 – 439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei442 – 4421PhosphoserineCombined sources
Modified residuei446 – 4461PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources
Modified residuei460 – 4601PhosphoserineCombined sources
Modified residuei479 – 4791PhosphoserineBy similarity
Modified residuei496 – 4961PhosphoserineBy similarity
Modified residuei544 – 5441PhosphoserineCombined sources
Modified residuei548 – 5481PhosphoserineCombined sources
Modified residuei552 – 5521PhosphoserineCombined sources
Modified residuei554 – 5541PhosphothreonineCombined sources
Modified residuei742 – 7421PhosphoserineCombined sources
Modified residuei813 – 8131PhosphothreonineCombined sources
Modified residuei816 – 8161PhosphothreonineCombined sources
Modified residuei834 – 8341PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ3KQU3.
MaxQBiQ3KQU3.
PaxDbiQ3KQU3.
PRIDEiQ3KQU3.

PTM databases

iPTMnetiQ3KQU3.
PhosphoSiteiQ3KQU3.

Expressioni

Gene expression databases

BgeeiQ3KQU3.
CleanExiHS_MAP7D1.
ExpressionAtlasiQ3KQU3. baseline and differential.
GenevisibleiQ3KQU3. HS.

Organism-specific databases

HPAiHPA028075.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MYCP011062EBI-713229,EBI-447544

Protein-protein interaction databases

BioGridi120825. 32 interactions.
IntActiQ3KQU3. 24 interactions.
MINTiMINT-2874531.
STRINGi9606.ENSP00000362244.

Structurei

3D structure databases

ProteinModelPortaliQ3KQU3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili128 – 22295Sequence analysisAdd
BLAST
Coiled coili412 – 44130Sequence analysisAdd
BLAST
Coiled coili593 – 721129Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 127114Pro-richAdd
BLAST
Compositional biasi467 – 589123Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MAP7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IH56. Eukaryota.
ENOG410XTH2. LUCA.
GeneTreeiENSGT00660000095160.
HOVERGENiHBG071099.
InParanoidiQ3KQU3.
KOiK16806.
OMAiAPQEPQW.
OrthoDBiEOG77DJ5Q.
PhylomeDBiQ3KQU3.
TreeFamiTF332273.

Family and domain databases

InterProiIPR008604. MAP7_fam.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 2 hits.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3KQU3-1) [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
MESGPRAELG AGAPPAVVAR TPPEPRPSPE GDPSPPPPPM SALVPDTPPD
60 70 80 90 100
TPPAMKNATS SKQLPLEPES PSGQVGPRPA PPQEESPSSE AKSRGPTPPA
110 120 130 140 150
MGPRDARPPR RSSQPSPTAV PASDSPPTKQ EVKKAGERHK LAKERREERA
160 170 180 190 200
KYLAAKKAVW LEKEEKAKAL REKQLQERRR RLEEQRLKAE QRRAALEERQ
210 220 230 240 250
RQKLEKNKER YEAAIQRSVK KTWAEIRQQR WSWAGALHHS SPGHKTSGSR
260 270 280 290 300
CSVSAVNLPK HVDSIINKRL SKSSATLWNS PSRNRSLQLS AWESSIVDRL
310 320 330 340 350
MTPTLSFLAR SRSAVTLPRN GRDQGRGCDP GRGPTWGRAG ASLARGPQPD
360 370 380 390 400
RTHPSAAVPV CPRSASASPL TPCSVTRSVH RCAPAGERGE RRKPNAGGSP
410 420 430 440 450
APVRRRPEAS PVQKKEKKDK ERENEKEKSA LARERSLKKR QSLPASPRAR
460 470 480 490 500
LSASTASELS PKSKARPSSP STSWHRPASP CPSPGPGHTL PPKPPSPRGT
510 520 530 540 550
TASPKGRVRR KEEAKESPSA AGPEDKSQSK RRASNEKESA APASPAPSPA
560 570 580 590 600
PSPTPAPPQK EQPPAETPTD AAVLTSPPAP APPVTPSKPM AGTTDREEAT
610 620 630 640 650
RLLAEKRRQA REQREREEQE RRLQAERDKR MREEQLAREA EARAEREAEA
660 670 680 690 700
RRREEQEARE KAQAEQEEQE RLQKQKEEAE ARSREEAERQ RLEREKHFQQ
710 720 730 740 750
QEQERQERRK RLEEIMKRTR KSEVSETKQK QDSKEANANG SSPEPVKAVE
760 770 780 790 800
ARSPGLQKEA VQKEEPIPQE PQWSLPSKEL PASLVNGLQP LPAHQENGFS
810 820 830 840
TNGPSGDKSL SRTPETLLPF AEAEAFLKKA VVQSPQVTEV L
Length:841
Mass (Da):92,820
Last modified:November 8, 2005 - v1
Checksum:i47F5931376A931EF
GO
Isoform 2 (identifier: Q3KQU3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     247-283: Missing.
     729-729: Missing.

Show »
Length:803
Mass (Da):88,726
Checksum:i5B8E46883590DF6A
GO
Isoform 3 (identifier: Q3KQU3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-454: Missing.
     455-459: TASEL → MNGPV
     570-578: Missing.
     729-729: Missing.

Note: No experimental confirmation available.
Show »
Length:377
Mass (Da):42,105
Checksum:iE220BB255F897F21
GO
Isoform 4 (identifier: Q3KQU3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     325-356: Missing.
     729-729: Missing.

Show »
Length:808
Mass (Da):89,467
Checksum:iBB3AFDF24FBB8273
GO

Sequence cautioni

The sequence AAG17244.1 differs from that shown. Reason: Frameshift at positions 80, 207 and 736. Curated
The sequence BAA86501.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071N → S in AAG17244 (PubMed:15498874).Curated
Sequence conflicti794 – 7941H → R in BAC04654 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041R → W.
Corresponds to variant rs2296266 [ dbSNP | Ensembl ].
VAR_035312
Natural varianti531 – 5311R → S.
Corresponds to variant rs12563354 [ dbSNP | Ensembl ].
VAR_053970

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 454454Missing in isoform 3. 1 PublicationVSP_028483Add
BLAST
Alternative sequencei247 – 28337Missing in isoform 2. 2 PublicationsVSP_028484Add
BLAST
Alternative sequencei325 – 35632Missing in isoform 4. 1 PublicationVSP_028485Add
BLAST
Alternative sequencei455 – 4595TASEL → MNGPV in isoform 3. 1 PublicationVSP_028486
Alternative sequencei570 – 5789Missing in isoform 3. 1 PublicationVSP_028487
Alternative sequencei729 – 7291Missing in isoform 2, isoform 3 and isoform 4. 4 PublicationsVSP_028488

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033013 mRNA. Translation: BAA86501.2. Different initiation.
AK001212 mRNA. Translation: BAA91557.1.
AK095939 mRNA. Translation: BAC04654.1.
CH471059 Genomic DNA. Translation: EAX07381.1.
CH471059 Genomic DNA. Translation: EAX07382.1.
BC027334 mRNA. Translation: AAH27334.1.
BC106053 mRNA. Translation: AAI06054.1.
AF218002 mRNA. Translation: AAG17244.1. Frameshift.
AL136547 mRNA. Translation: CAB66482.2.
CR457254 mRNA. Translation: CAG33535.1.
CCDSiCCDS30673.1. [Q3KQU3-1]
CCDS65492.1. [Q3KQU3-4]
CCDS65493.1. [Q3KQU3-2]
RefSeqiNP_001273294.1. NM_001286365.1. [Q3KQU3-2]
NP_001273295.1. NM_001286366.1. [Q3KQU3-4]
NP_060537.3. NM_018067.4. [Q3KQU3-1]
UniGeneiHs.356096.

Genome annotation databases

EnsembliENST00000316156; ENSP00000320228; ENSG00000116871. [Q3KQU3-2]
ENST00000373150; ENSP00000362243; ENSG00000116871. [Q3KQU3-4]
ENST00000373151; ENSP00000362244; ENSG00000116871. [Q3KQU3-1]
GeneIDi55700.
KEGGihsa:55700.
UCSCiuc001bzz.5. human. [Q3KQU3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033013 mRNA. Translation: BAA86501.2. Different initiation.
AK001212 mRNA. Translation: BAA91557.1.
AK095939 mRNA. Translation: BAC04654.1.
CH471059 Genomic DNA. Translation: EAX07381.1.
CH471059 Genomic DNA. Translation: EAX07382.1.
BC027334 mRNA. Translation: AAH27334.1.
BC106053 mRNA. Translation: AAI06054.1.
AF218002 mRNA. Translation: AAG17244.1. Frameshift.
AL136547 mRNA. Translation: CAB66482.2.
CR457254 mRNA. Translation: CAG33535.1.
CCDSiCCDS30673.1. [Q3KQU3-1]
CCDS65492.1. [Q3KQU3-4]
CCDS65493.1. [Q3KQU3-2]
RefSeqiNP_001273294.1. NM_001286365.1. [Q3KQU3-2]
NP_001273295.1. NM_001286366.1. [Q3KQU3-4]
NP_060537.3. NM_018067.4. [Q3KQU3-1]
UniGeneiHs.356096.

3D structure databases

ProteinModelPortaliQ3KQU3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120825. 32 interactions.
IntActiQ3KQU3. 24 interactions.
MINTiMINT-2874531.
STRINGi9606.ENSP00000362244.

PTM databases

iPTMnetiQ3KQU3.
PhosphoSiteiQ3KQU3.

Polymorphism and mutation databases

BioMutaiMAP7D1.
DMDMi121942584.

Proteomic databases

EPDiQ3KQU3.
MaxQBiQ3KQU3.
PaxDbiQ3KQU3.
PRIDEiQ3KQU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316156; ENSP00000320228; ENSG00000116871. [Q3KQU3-2]
ENST00000373150; ENSP00000362243; ENSG00000116871. [Q3KQU3-4]
ENST00000373151; ENSP00000362244; ENSG00000116871. [Q3KQU3-1]
GeneIDi55700.
KEGGihsa:55700.
UCSCiuc001bzz.5. human. [Q3KQU3-1]

Organism-specific databases

CTDi55700.
GeneCardsiMAP7D1.
H-InvDBHIX0000427.
HGNCiHGNC:25514. MAP7D1.
HPAiHPA028075.
neXtProtiNX_Q3KQU3.
PharmGKBiPA162394970.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH56. Eukaryota.
ENOG410XTH2. LUCA.
GeneTreeiENSGT00660000095160.
HOVERGENiHBG071099.
InParanoidiQ3KQU3.
KOiK16806.
OMAiAPQEPQW.
OrthoDBiEOG77DJ5Q.
PhylomeDBiQ3KQU3.
TreeFamiTF332273.

Miscellaneous databases

ChiTaRSiMAP7D1. human.
GenomeRNAii55700.
NextBioi60538.
PROiQ3KQU3.

Gene expression databases

BgeeiQ3KQU3.
CleanExiHS_MAP7D1.
ExpressionAtlasiQ3KQU3. baseline and differential.
GenevisibleiQ3KQU3. HS.

Family and domain databases

InterProiIPR008604. MAP7_fam.
[Graphical view]
PANTHERiPTHR15073. PTHR15073. 2 hits.
PfamiPF05672. MAP7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "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.
  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] (ISOFORM 3).
    Tissue: Heart and Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 625-841 (ISOFORMS 2/3/4).
    Tissue: Bone and Uterus.
  6. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-841 (ISOFORM 4).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-841 (ISOFORM 2).
    Tissue: Amygdala.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-841 (ISOFORMS 2/3/4).
  9. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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 SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-439.
    Tissue: Mammary cancer.
  13. "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-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; THR-51; SER-86; SER-113; SER-116; SER-125; SER-460; SER-544; SER-548; SER-552 AND SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. "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-125; SER-460; SER-544 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-70; SER-442; SER-446; SER-452; SER-460; SER-742; THR-813; THR-816 AND SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-113; SER-399; SER-460; SER-544 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-552 AND THR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMA7D1_HUMAN
AccessioniPrimary (citable) accession number: Q3KQU3
Secondary accession number(s): D3DPS4
, Q7L8J5, Q8N905, Q8TAK0, Q9HBQ2, Q9NW29, Q9ULN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 8, 2005
Last modified: April 13, 2016
This is version 94 of the entry and version 1 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 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.