Reviewed, UniProtKB/Swiss-Prot O14578 (CTRO_HUMAN)

Names and origin

Protein names

Recommended name:
    Citron Rho-interacting kinase
      Short name=CRIK
    EC=2.7.11.1
Alternative name(s):
    Rho-interacting, serine/threonine-protein kinase 21

Gene names

Name:	CIT
Synonyms:	KIAA0949, STK21

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2027 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for KIF14 localization to the central spindle and midbody. May play a role in cytokinesis. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Plays an important role in the regulation of cytokinesis and the development of the central nervous system By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Directly interacts with KIF14 depending on the activation state (stronger interaction with the kinase-dead form). Homodimer By similarity.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 CNH domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Phorbol-ester binding SH3-binding Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	generation of neurons Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14578-1)

Also known as: Long;

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.

Isoform 2 (identifier: O14578-2)

Also known as: Short; CRIK-SK;

The sequence of this isoform differs from the canonical sequence as follows:
     481-482: EV → GG
     483-2027: Missing.

Isoform 3 (identifier: O14578-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-467: Missing.
     1239-1253: Missing.
     1919-1919: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 2027	2027	Citron Rho-interacting kinase
Regions
	Domain	97 – 360	264	Protein kinase
	Domain	361 – 431	71	AGC-kinase C-terminal
	Domain	1443 – 1563	121	PH
	Domain	1593 – 1883	291	CNH
	Nucleotide binding	103 – 111	9	ATP By similarity
	Zinc finger	1362 – 1411	50	Phorbol-ester/DAG-type
	Region	1091 – 1302	212	Interaction with Rho/Rac
	Coiled coil	453 – 1297	845	Potential
	Motif	1953 – 1958	6	SH3-binding Potential
Sites
	Active site	221	1	Proton acceptor By similarity
	Binding site	126	1	ATP By similarity
Amino acid modifications
	Modified residue	440	1	Phosphoserine
	Modified residue	480	1	Phosphoserine By similarity
	Modified residue	1196	1	Phosphotyrosine By similarity
	Modified residue	1478	1	Phosphotyrosine By similarity
	Modified residue	1582	1	Phosphoserine By similarity
	Modified residue	1971	1	Phosphoserine
	Modified residue	1993	1	Phosphoserine
Natural variations
	Alternative sequence	1 – 467	467	Missing in isoform 3.
	Alternative sequence	481 – 482	2	EV → GG in isoform 2.
	Alternative sequence	483 – 2027	1545	Missing in isoform 2.
	Alternative sequence	1239 – 1253	15	Missing in isoform 3.
	Alternative sequence	1919	1	Missing in isoform 3.
	Natural variant	7	1	G → E
	Natural variant	9	1	R → Q
	Natural variant	183	1	L → F
Experimental info
	Sequence conflict	12	1	L → S in AAP43922. Ref.2
	Sequence conflict	56	1	F → L in AAP43922. Ref.2
	Sequence conflict	218	1	V → L in AAP43922. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 6B1D8C3F661F357B	FASTA	2,027	231,431
	10 20 30 40 50 60 MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 70 80 90 100 110 120 ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 130 140 150 160 170 180 DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 190 200 210 220 230 240 DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 250 260 270 280 290 300 GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 310 320 330 340 350 360 SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 370 380 390 400 410 420 SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 430 440 450 460 470 480 YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS 490 500 510 520 530 540 EVEAVLSQKE VELKASETQR SLLEQDLATY ITECSSLKRS LEQARMEVSQ EDDKALQLLH 550 560 570 580 590 600 DIREQSRKLQ EIKEQEYQAQ VEEMRLMMNQ LEEDLVSARR RSDLYESELR ESRLAAEEFK 610 620 630 640 650 660 RKATECQHKL LKAKDQGKPE VGEYAKLEKI NAEQQLKIQE LQEKLEKAVK ASTEATELLQ 670 680 690 700 710 720 NIRQAKERAE RELEKLQNRE DSSEGIRKKL VEAEELEEKH REAQVSAQHL EVHLKQKEQH 730 740 750 760 770 780 YEEKIKVLDN QIKKDLADKE TLENMMQRHE EEAHEKGKIL SEQKAMINAM DSKIRSLEQR 790 800 810 820 830 840 IVELSEANKL AANSSLFTQR NMKAQEEMIS ELRQQKFYLE TQAGKLEAQN RKLEEQLEKI 850 860 870 880 890 900 SHQDHSDKNR LLELETRLRE VSLEHEEQKL ELKRQLTELQ LSLQERESQL TALQAARAAL 910 920 930 940 950 960 ESQLRQAKTE LEETTAEAEE EIQALTAHRD EIQRKFDALR NSCTVITDLE EQLNQLTEDN 970 980 990 1000 1010 1020 AELNNQNFYL SKQLDEASGA NDEIVQLRSE VDHLRREITE REMQLTSQKQ TMEALKTTCT 1030 1040 1050 1060 1070 1080 MLEEQVMDLE ALNDELLEKE RQWEAWRSVL GDEKSQFECR VRELQRMLDT EKQSRARADQ 1090 1100 1110 1120 1130 1140 RITESRQVVE LAVKEHKAEI LALQQALKEQ KLKAESLSDK LNDLEKKHAM LEMNARSLQQ 1150 1160 1170 1180 1190 1200 KLETERELKQ RLLEEQAKLQ QQMDLQKNHI FRLTQGLQEA LDRADLLKTE RSDLEYQLEN 1210 1220 1230 1240 1250 1260 IQVLYSHEKV KMEGTISQQT KLIDFLQAKM DQPAKKKKGL FSRRKEDPAL PTQVPLQYNE 1270 1280 1290 1300 1310 1320 LKLALEKEKA RCAELEEALQ KTRIELRSAR EEAAHRKATD HPHPSTPATA RQQIAMSAIV 1330 1340 1350 1360 1370 1380 RSPEHQPSAM SLLAPPSSRR KESSTPEEFS RRLKERMHHN IPHRFNVGLN MRATKCAVCL 1390 1400 1410 1420 1430 1440 DTVHFGRQAS KCLECQVMCH PKCSTCLPAT CGLPAEYATH FTEAFCRDKM NSPGLQTKEP 1450 1460 1470 1480 1490 1500 SSSLHLEGWM KVPRNNKRGQ QGWDRKYIVL EGSKVLIYDN EAREAGQRPV EEFELCLPDG 1510 1520 1530 1540 1550 1560 DVSIHGAVGA SELANTAKAD VPYILKMESH PHTTCWPGRT LYLLAPSFPD KQRWVTALES 1570 1580 1590 1600 1610 1620 VVAGGRVSRE KAEADAKLLG NSLLKLEGDD RLDMNCTLPF SDQVVLVGTE EGLYALNVLK 1630 1640 1650 1660 1670 1680 NSLTHVPGIG AVFQIYIIKD LEKLLMIAGE ERALCLVDVK KVKQSLAQSH LPAQPDISPN 1690 1700 1710 1720 1730 1740 IFEAVKGCHL FGAGKIENGL CICAAMPSKV VILRYNENLS KYCIRKEIET SEPCSCIHFT 1750 1760 1770 1780 1790 1800 NYSILIGTNK FYEIDMKQYT LEEFLDKNDH SLAPAVFAAS SNSFPVSIVQ VNSAGQREEY 1810 1820 1830 1840 1850 1860 LLCFHEFGVF VDSYGRRSRT DDLKWSRLPL AFAYREPYLF VTHFNSLEVI EIQARSSAGT 1870 1880 1890 1900 1910 1920 PARAYLDIPN PRYLGPAISS GAIYLASSYQ DKLRVICCKG NLVKESGTEH HRGPSTSRSS 1930 1940 1950 1960 1970 1980 PNKRGPPTYN EHITKRVASS PAPPEGPSHP REPSTPHRYR EGRTELRRDK SPGRPLEREK 1990 2000 2010 2020 SPGRMLSTRR ERSPGRLFED SSRGRLPAGA VRTPLSQVNK VWDQSSV
	Isoform 2 (Short) (CRIK-SK) [UniParc]. Checksum: 7F23D62DD30DC0CE		482	54,399
	10 20 30 40 50 60 MLKFKYGARN PLDAGAAEPI ASRASRLNLF FQGKPPFMTQ QQMSPLSREG ILDALFVLFE 70 80 90 100 110 120 ECSQPALMKI KHVSNFVRKY SDTIAELQEL QPSAKDFEVR SLVGCGHFAE VQVVREKATG 130 140 150 160 170 180 DIYAMKVMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNHL YLVMEYQPGG 190 200 210 220 230 240 DLLSLLNRYE DQLDENLIQF YLAELILAVH SVHLMGYVHR DIKPENILVD RTGHIKLVDF 250 260 270 280 290 300 GSAAKMNSNK MVNAKLPIGT PDYMAPEVLT VMNGDGKGTY GLDCDWWSVG VIAYEMIYGR 310 320 330 340 350 360 SPFAEGTSAR TFNNIMNFQR FLKFPDDPKV SSDFLDLIQS LLCGQKERLK FEGLCCHPFF 370 380 390 400 410 420 SKIDWNNIRN SPPPFVPTLK SDDDTSNFDE PEKNSWVSSS PCQLSPSGFS GEELPFVGFS 430 440 450 460 470 480 YSKALGILGR SESVVSGLDS PAKTSSMEKK LLIKSKELQD SQDKCHKMEQ EMTRLHRRVS GG
	Isoform 3 [UniParc]. Checksum: 309A4BA63CB1419D		1,544	177,035
	10 20 30 40 50 60 MEQEMTRLHR RVSEVEAVLS QKEVELKASE TQRSLLEQDL ATYITECSSL KRSLEQARME 70 80 90 100 110 120 VSQEDDKALQ LLHDIREQSR KLQEIKEQEY QAQVEEMRLM MNQLEEDLVS ARRRSDLYES 130 140 150 160 170 180 ELRESRLAAE EFKRKATECQ HKLLKAKDQG KPEVGEYAKL EKINAEQQLK IQELQEKLEK 190 200 210 220 230 240 AVKASTEATE LLQNIRQAKE RAERELEKLQ NREDSSEGIR KKLVEAEELE EKHREAQVSA 250 260 270 280 290 300 QHLEVHLKQK EQHYEEKIKV LDNQIKKDLA DKETLENMMQ RHEEEAHEKG KILSEQKAMI 310 320 330 340 350 360 NAMDSKIRSL EQRIVELSEA NKLAANSSLF TQRNMKAQEE MISELRQQKF YLETQAGKLE 370 380 390 400 410 420 AQNRKLEEQL EKISHQDHSD KNRLLELETR LREVSLEHEE QKLELKRQLT ELQLSLQERE 430 440 450 460 470 480 SQLTALQAAR AALESQLRQA KTELEETTAE AEEEIQALTA HRDEIQRKFD ALRNSCTVIT 490 500 510 520 530 540 DLEEQLNQLT EDNAELNNQN FYLSKQLDEA SGANDEIVQL RSEVDHLRRE ITEREMQLTS 550 560 570 580 590 600 QKQTMEALKT TCTMLEEQVM DLEALNDELL EKERQWEAWR SVLGDEKSQF ECRVRELQRM 610 620 630 640 650 660 LDTEKQSRAR ADQRITESRQ VVELAVKEHK AEILALQQAL KEQKLKAESL SDKLNDLEKK 670 680 690 700 710 720 HAMLEMNARS LQQKLETERE LKQRLLEEQA KLQQQMDLQK NHIFRLTQGL QEALDRADLL 730 740 750 760 770 780 KTERSDLEYQ LENIQVLYSH EKVKMEGTIS QQTKLIDFLQ AKMDQPAKKK KVPLQYNELK 790 800 810 820 830 840 LALEKEKARC AELEEALQKT RIELRSAREE AAHRKATDHP HPSTPATARQ QIAMSAIVRS 850 860 870 880 890 900 PEHQPSAMSL LAPPSSRRKE SSTPEEFSRR LKERMHHNIP HRFNVGLNMR ATKCAVCLDT 910 920 930 940 950 960 VHFGRQASKC LECQVMCHPK CSTCLPATCG LPAEYATHFT EAFCRDKMNS PGLQTKEPSS 970 980 990 1000 1010 1020 SLHLEGWMKV PRNNKRGQQG WDRKYIVLEG SKVLIYDNEA REAGQRPVEE FELCLPDGDV 1030 1040 1050 1060 1070 1080 SIHGAVGASE LANTAKADVP YILKMESHPH TTCWPGRTLY LLAPSFPDKQ RWVTALESVV 1090 1100 1110 1120 1130 1140 AGGRVSREKA EADAKLLGNS LLKLEGDDRL DMNCTLPFSD QVVLVGTEEG LYALNVLKNS 1150 1160 1170 1180 1190 1200 LTHVPGIGAV FQIYIIKDLE KLLMIAGEER ALCLVDVKKV KQSLAQSHLP AQPDISPNIF 1210 1220 1230 1240 1250 1260 EAVKGCHLFG AGKIENGLCI CAAMPSKVVI LRYNENLSKY CIRKEIETSE PCSCIHFTNY 1270 1280 1290 1300 1310 1320 SILIGTNKFY EIDMKQYTLE EFLDKNDHSL APAVFAASSN SFPVSIVQVN SAGQREEYLL 1330 1340 1350 1360 1370 1380 CFHEFGVFVD SYGRRSRTDD LKWSRLPLAF AYREPYLFVT HFNSLEVIEI QARSSAGTPA 1390 1400 1410 1420 1430 1440 RAYLDIPNPR YLGPAISSGA IYLASSYQDK LRVICCKGNL VKESGTEHHR GPSTSRSPNK 1450 1460 1470 1480 1490 1500 RGPPTYNEHI TKRVASSPAP PEGPSHPREP STPHRYREGR TELRRDKSPG RPLEREKSPG 1510 1520 1530 1540 RMLSTRRERS PGRLFEDSSR GRLPAGAVRT PLSQVNKVWD QSSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Huang C.Q., Wu S.L., Shan Y.X., Liu S., Xiao P.J. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and characterizing a novel human CRIK-SK gene." Mao Y., Xie Y., Wu Q. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed: 10231032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[4]	Ohara O., Nagase T., Kikuno R. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"KIF14 and citron kinase act together to promote efficient cytokinesis." Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A., Barr F.A. J. Cell Biol. 172:363-372(2006) [PubMed: 16431929] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIF14.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1971 AND SER-1993, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-7; GLN-9 AND PHE-183.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY257469 mRNA. Translation: AAP13528.1. AY209000 mRNA. Translation: AAP43922.1. AB023166 mRNA. Translation: BAA76793.2. Different initiation. AC002563 Genomic DNA. Translation: AAB71327.1. AC079317 Genomic DNA. No translation available. AC004813 Genomic DNA. No translation available.
RefSeq	NP_009105.1.
UniGene	Hs.119594
3D structure databases
HSSP	HSSP built from PDB template 1MRV based on UniProtKB P31751.
ModBase	Search...
PTM databases
PhosphoSite	O14578.
Genome annotation databases
Ensembl	ENSG00000122966. Homo sapiens. [Contig view]
GeneID	11113.
KEGG	hsa:11113.
Organism-specific databases
HGNC	HGNC:1985. CIT.
MIM	605629. gene.
PharmGKB	PA26522.
HUGE	Search...