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Protein

Protein KRI1 homolog

Gene

KRI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein KRI1 homolog
Gene namesi
Name:KRI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:25769. KRI1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162393682.

Polymorphism and mutation databases

BioMutaiKRI1.
DMDMi550544300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 703703Protein KRI1 homologPRO_0000298976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphothreonineCombined sources
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei94 – 941PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei141 – 1411PhosphoserineCombined sources
Modified residuei171 – 1711PhosphoserineCombined sources
Modified residuei280 – 2801PhosphoserineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei622 – 6221PhosphoserineCombined sources
Modified residuei628 – 6281PhosphoserineCombined sources
Modified residuei639 – 6391PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N9T8.
MaxQBiQ8N9T8.
PaxDbiQ8N9T8.
PRIDEiQ8N9T8.

PTM databases

iPTMnetiQ8N9T8.
PhosphoSiteiQ8N9T8.

Expressioni

Gene expression databases

BgeeiQ8N9T8.
CleanExiHS_KRI1.
ExpressionAtlasiQ8N9T8. baseline and differential.
GenevisibleiQ8N9T8. HS.

Organism-specific databases

HPAiHPA043110.
HPA043574.

Interactioni

Protein-protein interaction databases

BioGridi122394. 27 interactions.
IntActiQ8N9T8. 15 interactions.
MINTiMINT-2810961.
STRINGi9606.ENSP00000320917.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 423326Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the KRI1 family.Curated

Phylogenomic databases

eggNOGiKOG2409. Eukaryota.
ENOG410XR4G. LUCA.
HOVERGENiHBG108077.
InParanoidiQ8N9T8.
KOiK14786.
OrthoDBiEOG7D85WW.
TreeFamiTF320278.

Family and domain databases

InterProiIPR018034. Kri1.
IPR024626. Kri1-like_C.
[Graphical view]
PANTHERiPTHR14490. PTHR14490. 1 hit.
PfamiPF05178. Kri1. 1 hit.
PF12936. Kri1_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N9T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPRGSSQL RVNAAFAARY NRYREREELQ RLKDRYGDRD SSSDSSSESD
60 70 80 90 100
SSDERVEFDP QQERDFYKTL SLLKKKDPRI YQKDATFYNR TASSSDSEED
110 120 130 140 150
PEALEKQKKV RPMYLKDYER KVILEKAGKY VDEENSDGET SNHRLQETSS
160 170 180 190 200
QSYVEEQKQL KESFRAFVED SEDEDGAGEG GSSLLQKRAK TRQEKAQEEA
210 220 230 240 250
DYIEWLKGQK EIRNPDSLKE LTHLKEYWND PELDEGERFL RDYILNKRYE
260 270 280 290 300
EEEEEEEDEE EMEEEEGVHG PPVQLAVDDS SDEGELFLKK QEDFEQKYNF
310 320 330 340 350
RFEEPDSASV KTYPRSIASS VRRKDERRKE KREETRERKK REKAKKQEEL
360 370 380 390 400
KQLKNLKRKE ILAKLEKLRK VTGNEMLGLE EGDLEDDFDP AQHDQLMQKC
410 420 430 440 450
FGDEYYGAVE EEKPQFEEEE GLEDDWNWDT WDGPEQEGDW SQQELHCEDP
460 470 480 490 500
NFNMDADYDP SQPRKKKREA PLTGKKKRKS PFAAAVGQEK PVFEPGDKTF
510 520 530 540 550
EEYLDEYYRL DYEDIIDDLP CRFKYRTVVP CDFGLSTEEI LAADDKELNR
560 570 580 590 600
WCSLKKTCMY RSEQEELRDK RAYSQKAQNS WKKRQVFKSL CREEAETPAE
610 620 630 640 650
ATGKPQRDEA GPQRQLPALD GSLMGPESPP AQEEEAPVSP HKKPAPQKRR
660 670 680 690 700
RAKKARLLGP TVMLGGCEFS RQRLQAFGLN PKRLHFRQLG RQRRKQQGPK

NSS
Length:703
Mass (Da):82,598
Last modified:October 16, 2013 - v3
Checksum:i0C34E54AB1250141
GO

Sequence cautioni

The sequence BAB14357.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC04240.1 differs from that shown.Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651R → W in BAC04240 (PubMed:14702039).Curated
Sequence conflicti252 – 2521E → G in BAB14357 (PubMed:14702039).Curated
Sequence conflicti279 – 2791D → G in BAB14357 (PubMed:14702039).Curated
Sequence conflicti316 – 3161S → N in BAC04240 (PubMed:14702039).Curated
Sequence conflicti345 – 3451K → E in BAC04240 (PubMed:14702039).Curated
Sequence conflicti556 – 5561K → E in BAB15278 (PubMed:14702039).Curated
Sequence conflicti627 – 6271E → G in BAB15278 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381G → R.1 Publication
Corresponds to variant rs12984043 [ dbSNP | Ensembl ].
VAR_034751
Natural varianti179 – 1791E → A.
Corresponds to variant rs11545166 [ dbSNP | Ensembl ].
VAR_034752
Natural varianti266 – 2661E → K.Combined sources2 Publications
Corresponds to variant rs3745249 [ dbSNP | Ensembl ].
VAR_034753
Natural varianti309 – 3091S → L.
Corresponds to variant rs34743532 [ dbSNP | Ensembl ].
VAR_034754
Natural varianti336 – 3361R → W.
Corresponds to variant rs33999611 [ dbSNP | Ensembl ].
VAR_034755
Natural varianti349 – 3491E → Q.2 Publications
Corresponds to variant rs3826709 [ dbSNP | Ensembl ].
VAR_034756
Natural varianti445 – 4451L → P.
Corresponds to variant rs1982074 [ dbSNP | Ensembl ].
VAR_034757
Natural varianti703 – 7031S → P.2 Publications
Corresponds to variant rs3087689 [ dbSNP | Ensembl ].
VAR_034758

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023011 mRNA. Translation: BAB14357.1. Different initiation.
AK025907 mRNA. Translation: BAB15278.1. Different initiation.
AK093879 mRNA. Translation: BAC04240.1. Sequence problems.
AC011461 Genomic DNA. No translation available.
AC011475 Genomic DNA. No translation available.
BC002890 mRNA. Translation: AAH02890.3.
BC009876 mRNA. Translation: AAH09876.2.
BC112249 mRNA. Translation: AAI12250.1.
BC112251 mRNA. Translation: AAI12252.1.
RefSeqiNP_075384.3. NM_023008.3.
UniGeneiHs.709967.

Genome annotation databases

EnsembliENST00000312962; ENSP00000320917; ENSG00000129347.
GeneIDi65095.
KEGGihsa:65095.
UCSCiuc002moy.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023011 mRNA. Translation: BAB14357.1. Different initiation.
AK025907 mRNA. Translation: BAB15278.1. Different initiation.
AK093879 mRNA. Translation: BAC04240.1. Sequence problems.
AC011461 Genomic DNA. No translation available.
AC011475 Genomic DNA. No translation available.
BC002890 mRNA. Translation: AAH02890.3.
BC009876 mRNA. Translation: AAH09876.2.
BC112249 mRNA. Translation: AAI12250.1.
BC112251 mRNA. Translation: AAI12252.1.
RefSeqiNP_075384.3. NM_023008.3.
UniGeneiHs.709967.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122394. 27 interactions.
IntActiQ8N9T8. 15 interactions.
MINTiMINT-2810961.
STRINGi9606.ENSP00000320917.

PTM databases

iPTMnetiQ8N9T8.
PhosphoSiteiQ8N9T8.

Polymorphism and mutation databases

BioMutaiKRI1.
DMDMi550544300.

Proteomic databases

EPDiQ8N9T8.
MaxQBiQ8N9T8.
PaxDbiQ8N9T8.
PRIDEiQ8N9T8.

Protocols and materials databases

DNASUi65095.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312962; ENSP00000320917; ENSG00000129347.
GeneIDi65095.
KEGGihsa:65095.
UCSCiuc002moy.2. human.

Organism-specific databases

CTDi65095.
GeneCardsiKRI1.
H-InvDBHIX0014749.
HGNCiHGNC:25769. KRI1.
HPAiHPA043110.
HPA043574.
neXtProtiNX_Q8N9T8.
PharmGKBiPA162393682.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2409. Eukaryota.
ENOG410XR4G. LUCA.
HOVERGENiHBG108077.
InParanoidiQ8N9T8.
KOiK14786.
OrthoDBiEOG7D85WW.
TreeFamiTF320278.

Miscellaneous databases

ChiTaRSiKRI1. human.
GenomeRNAii65095.
PROiQ8N9T8.

Gene expression databases

BgeeiQ8N9T8.
CleanExiHS_KRI1.
ExpressionAtlasiQ8N9T8. baseline and differential.
GenevisibleiQ8N9T8. HS.

Family and domain databases

InterProiIPR018034. Kri1.
IPR024626. Kri1-like_C.
[Graphical view]
PANTHERiPTHR14490. PTHR14490. 1 hit.
PfamiPF05178. Kri1. 1 hit.
PF12936. Kri1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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], VARIANTS LYS-266; GLN-349 AND PRO-703.
    Tissue: Teratocarcinoma and Trachea.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 104-703, VARIANTS ARG-138; LYS-266; GLN-349 AND PRO-703.
    Tissue: Lung and Ovary.
  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-136 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. "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-628 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-93; SER-94; SER-95; SER-97; SER-136; SER-141; SER-171; SER-280; SER-281 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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-171 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-136; SER-171; SER-622; SER-628 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 THR-91; SER-95; SER-97; SER-136; SER-171 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-136; SER-171; SER-280; SER-281 AND SER-628, VARIANT [LARGE SCALE ANALYSIS] LYS-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKRI1_HUMAN
AccessioniPrimary (citable) accession number: Q8N9T8
Secondary accession number(s): Q2M1R5
, Q2M1R7, Q7L5J7, Q96G92, Q9BU50, Q9H6I1, Q9H978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 16, 2013
Last modified: June 8, 2016
This is version 103 of the entry and version 3 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 19
    Human chromosome 19: 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.