|
|
|
|
|
|
Description:
Calcium and integrin-binding protein 1 (Calmyrin) (DNA-PKcs-interacting protein) (Kinase-interacting protein) (KIP) (CIB) (SNK-interacting protein 2-28) (SIP2-28).
Molecular weight: 21586
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
double-strand break repair( GO:0006302 )
Important dates:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
07-MAR-2006, entry version 56.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein KIP1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U83236 | AAB39758.1 | - |
| EMBL | U85611 | AAB53387.1 | - |
| EMBL | U82226 | AAC51106.1 | - |
| EMBL | AB021866 | BAA36281.1 | - |
| EMBL | CR456955 | CAG33236.1 | - |
| EMBL | BC000846 | AAH00846.1 | - |
| PDB | 1DGU | NMR | A=8-190. |
| PDB | 1DGV | NMR | A=8-190. |
| PDB | 1XO5 | X-ray | A/B=8-190. |
| IntAct | Q99828 | -.1 | |
| Ensembl | ENSG00000185043 | Homo sapiens.1 | |
| H-InvDB | HIX0012576 | -.1 | |
| HGNC | HGNC:16920 | CIB1.1 | |
| MIM | 602293 | gene. | |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0007155 | P:cell adhesion | TAS. |
| GO | GO:0006302 | P:double-strand break repair | TAS. |
| GO | GO:0006974 | P:response to DNA damage stimulus | IDA. |
| InterPro | IPR011992 | EF-Hand_type. | |
| InterPro | IPR002048 | EF_hand_Ca_bd. | |
| Pfam | PF00036 | efhand | 2. |
| ProDom | PD000012 | EF-hand | 1. |
| SMART | SM00054 | EFh | 1. |
| PROSITE | PS00018 | EF_HAND_1 | 2. |
| PROSITE | PS50222 | EF_HAND_2 | 2. |
Keywords:
3D-structure; Calcium; Lipoprotein; Membrane; Myristate; Polymorphism; Repeat.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Yuan O.;
RT "SNK, a Ser/Thr protein kinase, associated proteins.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=98040126; PubMed=9372844; DOI=10.1016/S0921-8777(97)00035-9;
RA Wu X., Lieber M.R.;
RT "Interaction between DNA-dependent protein kinase and a novel protein,
RT KIP.";
RL Mutat. Res. 385:13-20(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND VARIANT SER-43.
RC TISSUE=Fetal liver;
RX MEDLINE=97184102; PubMed=9030514; DOI=10.1074/jbc.272.8.4651;
RA Naik U.P., Patel P.M., Parise L.V.;
RT "Identification of a novel calcium-binding protein that interacts with
RT the integrin alphaIIb cytoplasmic domain.";
RL J. Biol. Chem. 272:4651-4654(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=20284952; PubMed=10826701;
RA Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.;
RT "Genomic structure of mouse and human genes for DNA-PKcs interacting
RT protein (KIP).";
RL DNA Seq. 10:415-418(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-43.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-43.
RC TISSUE=Cervix;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP MYRISTOYLATION, AND INTERACTION WITH PSEN2.
RX PubMed=10366599; DOI=10.1083/jcb.145.6.1277;
RA Stabler S.M., Ostrowski L.L., Janicki S.M., Monteiro M.J.;
RT "A myristoylated calcium-binding protein that preferentially interacts
RT with the Alzheimer's disease presenilin 2 protein.";
RL J. Cell Biol. 145:1277-1292(1999).
RN [8]
RP STRUCTURE BY NMR OF 8-190.
RX MEDLINE=20283154; PubMed=10822252;
RX DOI=10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.3.CO;2-1;
RA Hwang P.M., Vogel H.J.;
RT "Structures of the platelet calcium- and integrin-binding protein and
RT the alphaIIb-integrin cytoplasmic domain suggest a mechanism for
RT calcium-regulated recognition; homology modelling and NMR studies.";
RL J. Mol. Recognit. 13:83-92(2000).
Feature:
INIT_MET 0 0
CHAIN 1 190 Calcium and integrin-binding protein 1.
/FTId=PRO_0000073531.
DOMAIN 102 137 EF-hand 1.
DOMAIN 147 182 EF-hand 2.
CA_BIND 115 126 1 (Potential).
CA_BIND 160 171 2 (Potential).
LIPID 1 1 N-myristoyl glycine.
VARIANT 43 43 T -> S (in dbSNP:3210935).
/FTId=VAR_019565.
CONFLICT 135 135 T -> M (in Ref. 5).
HELIX 13 15
STRAND 16 16
STRAND 21 21
HELIX 23 34
TURN 35 36
STRAND 37 37
HELIX 39 41
STRAND 43 43
HELIX 44 49
STRAND 52 53
HELIX 54 58
TURN 59 59
STRAND 60 60
HELIX 61 64
TURN 65 65
TURN 67 68
HELIX 69 76
STRAND 79 79
TURN 80 81
STRAND 84 85
HELIX 87 97
STRAND 98 98
TURN 99 100
STRAND 101 101
HELIX 103 114
TURN 116 117
STRAND 119 122
HELIX 124 134
TURN 146 147
HELIX 148 159
TURN 161 162
STRAND 164 167
HELIX 169 178
HELIX 180 189
Comments:
-!- FUNCTION: May convert the inactive conformation of integrin alpha-
IIb/beta3 to an active form through the binding to the integrin
cytoplasmic domain.
-!- SUBUNIT: Interacts with the heterodimeric integrin alpha-
IIb/beta3. Interacts with the protein kinases Snk and with the
region immediately upstream of the kinase domain of DNA-PK.
Interacts with PSEN2.
-!- INTERACTION:
Q01780:EXOSC10; NbExp=1; IntAct=EBI-372594, EBI-358236;
-!- SUBCELLULAR LOCATION: Membrane-anchored.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Contains 2 EF-hand domains.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 190
GGSGSRLSKE LLAEYQDLTF LTKQEILLAH RRFCELLPQE QRTVESSLRA QVPFEQILSL
PELKANPFKE RICRVFSTSP AKDSLSFEDF LDLLSVFSDT ATPDIKSHYA FRIFDFDDDG
TLNREDLSRL VNCLTGEGED TRLSASEMKQ LIDNILEESD IDRDGTINLS EFQHVISRSP
DFASSFKIVL