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Protein

Ankycorbin

Gene

RAI14

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ankycorbin
Alternative name(s):
Ankyrin repeat and coiled-coil structure-containing protein
Novel retinal pigment epithelial cell protein
Retinoic acid-induced protein 14
Gene namesi
Name:RAI14
Synonyms:KIAA1334, NORPEG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:14873. RAI14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34189.

Polymorphism and mutation databases

BioMutaiRAI14.
DMDMi108860920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 980980AnkycorbinPRO_0000239630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei249 – 2491PhosphothreonineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei286 – 2861PhosphoserineCombined sources
Modified residuei293 – 2931PhosphoserineCombined sources
Modified residuei295 – 2951PhosphothreonineCombined sources
Modified residuei297 – 2971PhosphothreonineCombined sources
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei318 – 3181PhosphoserineBy similarity
Modified residuei327 – 3271PhosphoserineCombined sources
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei340 – 3401PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei419 – 4191PhosphoserineCombined sources
Modified residuei512 – 5121PhosphoserineCombined sources
Modified residuei515 – 5151PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei915 – 9151PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9P0K7.
MaxQBiQ9P0K7.
PaxDbiQ9P0K7.
PeptideAtlasiQ9P0K7.
PRIDEiQ9P0K7.

PTM databases

iPTMnetiQ9P0K7.
PhosphoSiteiQ9P0K7.
SwissPalmiQ9P0K7.

Expressioni

Tissue specificityi

Highly expressed in placenta, muscle, kidney and testis. Moderately expressed in heart, brain, lung, liver and intestine. Isoform 2 is widely expressed and expressed in fetal and adult testes, and spermatozoa.3 Publications

Inductioni

Up-regulated by all-trans-retinoic acid (ATRA) in retinal pigment epithelial cells (ARPE-19).1 Publication

Gene expression databases

BgeeiQ9P0K7.
CleanExiHS_RAI14.
ExpressionAtlasiQ9P0K7. baseline and differential.
GenevisibleiQ9P0K7. HS.

Organism-specific databases

HPAiHPA036949.
HPA036950.

Interactioni

Subunit structurei

Doesn't bind directly to F-actin.By similarity

Protein-protein interaction databases

BioGridi117526. 66 interactions.
IntActiQ9P0K7. 47 interactions.
MINTiMINT-1138088.
STRINGi9606.ENSP00000427123.

Structurei

3D structure databases

ProteinModelPortaliQ9P0K7.
SMRiQ9P0K7. Positions 12-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 5134ANK 1Add
BLAST
Repeati52 – 8130ANK 2Add
BLAST
Repeati85 – 11430ANK 3Add
BLAST
Repeati118 – 14730ANK 4Add
BLAST
Repeati151 – 18030ANK 5Add
BLAST
Repeati184 – 21330ANK 6Add
BLAST
Repeati217 – 24731ANK 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili349 – 37426Sequence analysisAdd
BLAST
Coiled coili425 – 947523Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi270 – 2767Nuclear localization signal1 Publication

Sequence similaritiesi

Contains 7 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IEWD. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00530000063369.
HOGENOMiHOG000154070.
HOVERGENiHBG093886.
InParanoidiQ9P0K7.
OMAiEDMKEAM.
OrthoDBiEOG7X9G6C.
PhylomeDBiQ9P0K7.
TreeFamiTF331274.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9P0K7-1) [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
MKSLKAKFRK SDTNEWNKND DRLLQAVENG DAEKVASLLG KKGASATKHD
60 70 80 90 100
SEGKTAFHLA AAKGHVECLR VMITHGVDVT AQDTTGHSAL HLAAKNSHHE
110 120 130 140 150
CIRKLLQSKC PAESVDSSGK TALHYAAAQG CLQAVQILCE HKSPINLKDL
160 170 180 190 200
DGNIPLLLAV QNGHSEICHF LLDHGADVNS RNKSGRTALM LACEIGSSNA
210 220 230 240 250
VEALIKKGAD LNLVDSLGYN ALHYSKLSEN AGIQSLLLSK ISQDADLKTP
260 270 280 290 300
TKPKQHDQVS KISSERSGTP KKRKAPPPPI SPTQLSDVSS PRSITSTPLS
310 320 330 340 350
GKESVFFAEP PFKAEISSIR ENKDRLSDST TGADSLLDIS SEADQQDLLS
360 370 380 390 400
LLQAKVASLT LHNKELQDKL QAKSPKEAEA DLSFDSYHST QTDLGPSLGK
410 420 430 440 450
PGETSPPDSK SSPSVLIHSL GKSTTDNDVR IQQLQEILQD LQKRLESSEA
460 470 480 490 500
ERKQLQVELQ SRRAELVCLN NTEISENSSD LSQKLKETQS KYEEAMKEVL
510 520 530 540 550
SVQKQMKLGL VSPESMDNYS HFHELRVTEE EINVLKQDLQ NALEESERNK
560 570 580 590 600
EKVRELEEKL VEREKGTVIK PPVEEYEEMK SSYCSVIENM NKEKAFLFEK
610 620 630 640 650
YQEAQEEIMK LKDTLKSQMT QEASDEAEDM KEAMNRMIDE LNKQVSELSQ
660 670 680 690 700
LYKEAQAELE DYRKRKSLED VTAEYIHKAE HEKLMQLTNV SRAKAEDALS
710 720 730 740 750
EMKSQYSKVL NELTQLKQLV DAQKENSVSI TEHLQVITTL RTAAKEMEEK
760 770 780 790 800
ISNLKEHLAS KEVEVAKLEK QLLEEKAAMT DAMVPRSSYE KLQSSLESEV
810 820 830 840 850
SVLASKLKES VKEKEKVHSE VVQIRSEVSQ VKREKENIQT LLKSKEQEVN
860 870 880 890 900
ELLQKFQQAQ EELAEMKRYA ESSSKLEEDK DKKINEMSKE VTKLKEALNS
910 920 930 940 950
LSQLSYSTSS SKRQSQQLEA LQQQVKQLQN QLAECKKQHQ EVISVYRMHL
960 970 980
LYAVQGQMDE DVQKVLKQIL TMCKNQSQKK
Length:980
Mass (Da):110,041
Last modified:June 13, 2006 - v2
Checksum:iDFCF4B7913B30B69
GO
Isoform 2 (identifier: Q9P0K7-2) [UniParc]FASTAAdd to basket

Also known as: sNORPEG

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MKSLKAKFRKSD → MQPTYLPWLSAKEKK

Show »
Length:983
Mass (Da):110,423
Checksum:i9B18E2F9DBFF5A6D
GO
Isoform 3 (identifier: Q9P0K7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MKSLKAKFRKSD → MEAK

Show »
Length:972
Mass (Da):109,080
Checksum:i5862375423E1C605
GO
Isoform 4 (identifier: Q9P0K7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     255-283: Missing.

Note: No experimental confirmation available.
Show »
Length:951
Mass (Da):106,905
Checksum:iF5CB369061C23BB6
GO

Sequence cautioni

The sequence BAA92572.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB43236.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041K → R in AAF44722 (PubMed:11042181).Curated
Sequence conflicti272 – 2721K → T in AAF44722 (PubMed:11042181).Curated
Sequence conflicti272 – 2721K → T in AAQ63889 (Ref. 3) Curated
Sequence conflicti434 – 4341L → P in AAQ63889 (Ref. 3) Curated
Sequence conflicti491 – 4911K → Q in AAQ63889 (Ref. 3) Curated
Sequence conflicti602 – 6021Q → P in AAQ63889 (Ref. 3) Curated
Sequence conflicti607 – 6071E → G in AAQ63889 (Ref. 3) Curated
Sequence conflicti610 – 6101K → E in AAQ63889 (Ref. 3) Curated
Sequence conflicti636 – 6361R → G in CAB43236 (PubMed:17974005).Curated
Sequence conflicti766 – 7661A → L in AAQ63889 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441A → T.
Corresponds to variant rs17521570 [ dbSNP | Ensembl ].
VAR_026673
Natural varianti45 – 451S → N.
Corresponds to variant rs35941954 [ dbSNP | Ensembl ].
VAR_055517
Natural varianti499 – 4991V → L.
Corresponds to variant rs10472941 [ dbSNP | Ensembl ].
VAR_055518
Natural varianti870 – 8701A → S.2 Publications
Corresponds to variant rs1048944 [ dbSNP | Ensembl ].
VAR_055519

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212MKSLK…FRKSD → MQPTYLPWLSAKEKK in isoform 2. 1 PublicationVSP_019248Add
BLAST
Alternative sequencei1 – 1212MKSLK…FRKSD → MEAK in isoform 3. 1 PublicationVSP_019249Add
BLAST
Alternative sequencei255 – 28329Missing in isoform 4. 1 PublicationVSP_045814Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155135 mRNA. Translation: AAF44722.1.
AY317139 mRNA. Translation: AAP84319.1.
AY354204 mRNA. Translation: AAQ63889.2.
AB037755 mRNA. Translation: BAA92572.1. Different initiation.
AK314379 mRNA. No translation available.
AC016602 Genomic DNA. No translation available.
AC025754 Genomic DNA. No translation available.
AC026801 Genomic DNA. No translation available.
BC052988 mRNA. Translation: AAH52988.1.
AL050011 mRNA. Translation: CAB43236.2. Different initiation.
CCDSiCCDS34142.1. [Q9P0K7-1]
CCDS54837.1. [Q9P0K7-4]
CCDS54838.1. [Q9P0K7-3]
CCDS54839.1. [Q9P0K7-2]
PIRiT08700.
RefSeqiNP_001138992.1. NM_001145520.1. [Q9P0K7-1]
NP_001138993.1. NM_001145521.1. [Q9P0K7-1]
NP_001138994.1. NM_001145522.1. [Q9P0K7-4]
NP_001138995.1. NM_001145523.1. [Q9P0K7-3]
NP_001138997.1. NM_001145525.1. [Q9P0K7-2]
NP_056392.2. NM_015577.2. [Q9P0K7-1]
XP_006714532.1. XM_006714469.2. [Q9P0K7-1]
XP_011512319.1. XM_011514017.1. [Q9P0K7-1]
XP_011512320.1. XM_011514018.1. [Q9P0K7-1]
XP_011512321.1. XM_011514019.1. [Q9P0K7-1]
XP_011512322.1. XM_011514020.1. [Q9P0K7-1]
XP_011512323.1. XM_011514021.1. [Q9P0K7-1]
XP_011512324.1. XM_011514022.1. [Q9P0K7-1]
UniGeneiHs.431400.

Genome annotation databases

EnsembliENST00000265109; ENSP00000265109; ENSG00000039560. [Q9P0K7-1]
ENST00000428746; ENSP00000388725; ENSG00000039560. [Q9P0K7-1]
ENST00000503673; ENSP00000422942; ENSG00000039560. [Q9P0K7-1]
ENST00000506376; ENSP00000423854; ENSG00000039560. [Q9P0K7-3]
ENST00000512629; ENSP00000422377; ENSG00000039560. [Q9P0K7-4]
ENST00000515799; ENSP00000427123; ENSG00000039560. [Q9P0K7-2]
GeneIDi26064.
KEGGihsa:26064.
UCSCiuc003jir.4. human. [Q9P0K7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155135 mRNA. Translation: AAF44722.1.
AY317139 mRNA. Translation: AAP84319.1.
AY354204 mRNA. Translation: AAQ63889.2.
AB037755 mRNA. Translation: BAA92572.1. Different initiation.
AK314379 mRNA. No translation available.
AC016602 Genomic DNA. No translation available.
AC025754 Genomic DNA. No translation available.
AC026801 Genomic DNA. No translation available.
BC052988 mRNA. Translation: AAH52988.1.
AL050011 mRNA. Translation: CAB43236.2. Different initiation.
CCDSiCCDS34142.1. [Q9P0K7-1]
CCDS54837.1. [Q9P0K7-4]
CCDS54838.1. [Q9P0K7-3]
CCDS54839.1. [Q9P0K7-2]
PIRiT08700.
RefSeqiNP_001138992.1. NM_001145520.1. [Q9P0K7-1]
NP_001138993.1. NM_001145521.1. [Q9P0K7-1]
NP_001138994.1. NM_001145522.1. [Q9P0K7-4]
NP_001138995.1. NM_001145523.1. [Q9P0K7-3]
NP_001138997.1. NM_001145525.1. [Q9P0K7-2]
NP_056392.2. NM_015577.2. [Q9P0K7-1]
XP_006714532.1. XM_006714469.2. [Q9P0K7-1]
XP_011512319.1. XM_011514017.1. [Q9P0K7-1]
XP_011512320.1. XM_011514018.1. [Q9P0K7-1]
XP_011512321.1. XM_011514019.1. [Q9P0K7-1]
XP_011512322.1. XM_011514020.1. [Q9P0K7-1]
XP_011512323.1. XM_011514021.1. [Q9P0K7-1]
XP_011512324.1. XM_011514022.1. [Q9P0K7-1]
UniGeneiHs.431400.

3D structure databases

ProteinModelPortaliQ9P0K7.
SMRiQ9P0K7. Positions 12-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117526. 66 interactions.
IntActiQ9P0K7. 47 interactions.
MINTiMINT-1138088.
STRINGi9606.ENSP00000427123.

PTM databases

iPTMnetiQ9P0K7.
PhosphoSiteiQ9P0K7.
SwissPalmiQ9P0K7.

Polymorphism and mutation databases

BioMutaiRAI14.
DMDMi108860920.

Proteomic databases

EPDiQ9P0K7.
MaxQBiQ9P0K7.
PaxDbiQ9P0K7.
PeptideAtlasiQ9P0K7.
PRIDEiQ9P0K7.

Protocols and materials databases

DNASUi26064.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265109; ENSP00000265109; ENSG00000039560. [Q9P0K7-1]
ENST00000428746; ENSP00000388725; ENSG00000039560. [Q9P0K7-1]
ENST00000503673; ENSP00000422942; ENSG00000039560. [Q9P0K7-1]
ENST00000506376; ENSP00000423854; ENSG00000039560. [Q9P0K7-3]
ENST00000512629; ENSP00000422377; ENSG00000039560. [Q9P0K7-4]
ENST00000515799; ENSP00000427123; ENSG00000039560. [Q9P0K7-2]
GeneIDi26064.
KEGGihsa:26064.
UCSCiuc003jir.4. human. [Q9P0K7-1]

Organism-specific databases

CTDi26064.
GeneCardsiRAI14.
HGNCiHGNC:14873. RAI14.
HPAiHPA036949.
HPA036950.
MIMi606586. gene.
neXtProtiNX_Q9P0K7.
PharmGKBiPA34189.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEWD. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00530000063369.
HOGENOMiHOG000154070.
HOVERGENiHBG093886.
InParanoidiQ9P0K7.
OMAiEDMKEAM.
OrthoDBiEOG7X9G6C.
PhylomeDBiQ9P0K7.
TreeFamiTF331274.

Miscellaneous databases

ChiTaRSiRAI14. human.
GeneWikiiRAI14.
GenomeRNAii26064.
PROiQ9P0K7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0K7.
CleanExiHS_RAI14.
ExpressionAtlasiQ9P0K7. baseline and differential.
GenevisibleiQ9P0K7. HS.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and developmental expression of NORPEG, a novel gene induced by retinoic acid."
    Kutty R.K., Kutty G., Samuel W., Duncan T., Bridges C.C., El-Sherbeeny A., Nagineni C.N., Smith S.B., Wiggert B.
    J. Biol. Chem. 276:2831-2840(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
    Tissue: Retinal pigment epithelium.
  2. "Expression of a novel alternative transcript of the novel retinal pigment epithelial cell gene NORPEG in human testes."
    Yuan W., Zheng Y., Huo R., Lu L., Huang X.-Y., Yin L.-L., Li J.-M., Zhou Z.-M., Sha J.-H.
    Asian J. Androl. 7:277-288(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Testis.
  3. Sha J.H., Zhou Z.M., Li J.M.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "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 4), VARIANT SER-870.
    Tissue: Placenta.
  6. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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), VARIANT SER-870.
    Tissue: Skin.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-980.
    Tissue: Brain.
  9. Cited for: TISSUE SPECIFICITY.
  10. Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
    Tissue: Retinal pigment epithelium.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-249; SER-340; SER-341; SER-358; SER-512 AND SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-293; THR-295; THR-297 AND SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-249; THR-297; SER-358; SER-419 AND SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  19. "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 THR-249; SER-281; SER-286; SER-327; SER-329; SER-350 AND SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRAI14_HUMAN
AccessioniPrimary (citable) accession number: Q9P0K7
Secondary accession number(s): E9PED3
, Q6V1W9, Q7Z5I4, Q7Z733, Q9P2L2, Q9Y3T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: July 6, 2016
This is version 125 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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.